PPIA_HUMAN
ID PPIA_HUMAN Reviewed; 165 AA.
AC P62937; A8K220; P05092; Q3KQW3; Q567Q0; Q6IBU5; Q96IX3; Q9BRU4; Q9BTY9;
AC Q9UC61;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE Short=PPIase A;
DE EC=5.2.1.8 {ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:25678563, ECO:0000305|PubMed:19207730, ECO:0000305|PubMed:26095851};
DE AltName: Full=Cyclophilin A;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=Rotamase A;
DE Contains:
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;
GN Name=PPIA; Synonyms=CYPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leukemic T-cell;
RX PubMed=3297675; DOI=10.1002/j.1460-2075.1987.tb04843.x;
RA Haendler B., Hofer-Warbinek R., Hofer E.;
RT "Complementary DNA for human T-cell cyclophilin.";
RL EMBO J. 6:947-950(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2197089; DOI=10.1111/j.1432-1033.1990.tb15598.x;
RA Haendler B., Hofer E.;
RT "Characterization of the human cyclophilin gene and of related processed
RT pseudogenes.";
RL Eur. J. Biochem. 190:477-482(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Subthalamic nucleus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Blood, Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle,
RC Skin, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-30.
RX PubMed=7657784; DOI=10.1093/oxfordjournals.humrep.a136138;
RA Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.;
RT "Identification of cyclophilin A from human decidual and placental tissue
RT in the first trimester of pregnancy.";
RL Hum. Reprod. 10:1305-1310(1995).
RN [10]
RP PROTEIN SEQUENCE OF 2-19.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP TRP-121.
RX PubMed=2001362; DOI=10.1021/bi00223a003;
RA Liu J., Chen C.-M., Walsh C.T.;
RT "Human and Escherichia coli cyclophilins: sensitivity to inhibition by the
RT immunosuppressant cyclosporin A correlates with a specific tryptophan
RT residue.";
RL Biochemistry 30:2306-2310(1991).
RN [14]
RP INTERACTION WITH HIV-1 CAPSID PROTEIN (MICROBIAL INFECTION).
RX PubMed=8513493; DOI=10.1016/0092-8674(93)90637-6;
RA Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.;
RT "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A
RT and B.";
RL Cell 73:1067-1078(1993).
RN [15]
RP INTERACTION WITH BSG.
RX PubMed=11353871; DOI=10.1073/pnas.111583198;
RA Pushkarsky T., Zybarth G., Dubrovsky L., Yurchenko V., Tang H., Guo H.,
RA Toole B., Sherry B., Bukrinsky M.;
RT "CD147 facilitates HIV-1 infection by interacting with virus-associated
RT cyclophilin A.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6360-6365(2001).
RN [16]
RP FUNCTION, INTERACTION WITH BSG, AND MUTAGENESIS OF PHE-60; PHE-113; TRP-121
RP AND HIS-126.
RX PubMed=11943775; DOI=10.1074/jbc.m201593200;
RA Yurchenko V., Zybarth G., O'Connor M., Dai W.W., Franchin G., Hao T.,
RA Guo H., Hung H.C., Toole B., Gallay P., Sherry B., Bukrinsky M.;
RT "Active site residues of cyclophilin A are crucial for its signaling
RT activity via CD147.";
RL J. Biol. Chem. 277:22959-22965(2002).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [18]
RP FUNCTION.
RX PubMed=15130913; DOI=10.1161/01.atv.0000130664.51010.28;
RA Jin Z.G., Lungu A.O., Xie L., Wang M., Wong C., Berk B.C.;
RT "Cyclophilin A is a proinflammatory cytokine that activates endothelial
RT cells.";
RL Arterioscler. Thromb. Vasc. Biol. 24:1186-1191(2004).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH BSG, AND INTERACTION WITH
RP SARS-COV NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=15688292; DOI=10.1086/427811;
RA Chen Z., Mi L., Xu J., Yu J., Wang X., Jiang J., Xing J., Shang P.,
RA Qian A., Li Y., Shaw P.X., Wang J., Duan S., Ding J., Fan C., Zhang Y.,
RA Yang Y., Yu X., Feng Q., Li B., Yao X., Zhang Z., Li L., Xue X., Zhu P.;
RT "Function of HAb18G/CD147 in invasion of host cells by severe acute
RT respiratory syndrome coronavirus.";
RL J. Infect. Dis. 191:755-760(2005).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=16527992; DOI=10.1161/01.res.0000216405.85080.a6;
RA Suzuki J., Jin Z.G., Meoli D.F., Matoba T., Berk B.C.;
RT "Cyclophilin A is secreted by a vesicular pathway in vascular smooth muscle
RT cells.";
RL Circ. Res. 98:811-817(2006).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP FUNCTION, INTERACTION WITH INFLUENZA A VIRUS MATRIX PROTEIN 1 (MICROBIAL
RP INFECTION), CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-55.
RX PubMed=19207730; DOI=10.1111/j.1462-5822.2009.01286.x;
RA Liu X., Sun L., Yu M., Wang Z., Xu C., Xue Q., Zhang K., Ye X.,
RA Kitamura Y., Liu W.;
RT "Cyclophilin A interacts with influenza A virus M1 protein and impairs the
RT early stage of the viral replication.";
RL Cell. Microbiol. 11:730-741(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82;
RP LYS-125 AND LYS-131, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [24]
RP INTERACTION WITH MEASLES VIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=20147391; DOI=10.1128/jvi.02168-09;
RA Watanabe A., Yoneda M., Ikeda F., Terao-Muto Y., Sato H., Kai C.;
RT "CD147/EMMPRIN acts as a functional entry receptor for measles virus on
RT epithelial cells.";
RL J. Virol. 84:4183-4193(2010).
RN [25]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-121.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BSG, AND MUTAGENESIS OF
RP ARG-55; ARG-69; HIS-70 AND THR-107.
RX PubMed=21245143; DOI=10.1074/jbc.c110.181347;
RA Song F., Zhang X., Ren X.B., Zhu P., Xu J., Wang L., Li Y.F., Zhong N.,
RA Ru Q., Zhang D.W., Jiang J.L., Xia B., Chen Z.N.;
RT "Cyclophilin A (CyPA) induces chemotaxis independent of its peptidylprolyl
RT cis-trans isomerase activity: direct binding between CyPA and the
RT ectodomain of CD147.";
RL J. Biol. Chem. 286:8197-8203(2011).
RN [29]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCV NS5A (MICROBIAL
RP INFECTION), CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-126.
RX PubMed=21593166; DOI=10.1128/jvi.00393-11;
RA Foster T.L., Gallay P., Stonehouse N.J., Harris M.;
RT "Cyclophilin A interacts with domain II of hepatitis C virus NS5A and
RT stimulates RNA binding in an isomerase-dependent manner.";
RL J. Virol. 85:7460-7464(2011).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [31]
RP FUNCTION.
RX PubMed=22347431; DOI=10.1371/journal.pone.0031063;
RA Liu X., Zhao Z., Xu C., Sun L., Chen J., Zhang L., Liu W.;
RT "Cyclophilin A restricts influenza A virus replication through degradation
RT of the M1 protein.";
RL PLoS ONE 7:e31063-e31063(2012).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [33]
RP FUNCTION.
RX PubMed=23180369; DOI=10.1007/s10753-012-9578-7;
RA Wei Y., Jinchuan Y., Yi L., Jun W., Zhongqun W., Cuiping W.;
RT "Antiapoptotic and proapoptotic signaling of cyclophilin A in endothelial
RT cells.";
RL Inflammation 36:567-572(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP MAP3K5, AND MUTAGENESIS OF ARG-55.
RX PubMed=26095851; DOI=10.1016/j.bbrc.2015.06.078;
RA Kim H., Oh Y., Kim K., Jeong S., Chon S., Kim D., Jung M.H., Pak Y.K.,
RA Ha J., Kang I., Choe W.;
RT "Cyclophilin A regulates JNK/p38-MAPK signaling through its physical
RT interaction with ASK1.";
RL Biochem. Biophys. Res. Commun. 464:112-117(2015).
RN [37]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TARDBP; HNRNPA1; HNRNPA2B1;
RP HNRNPC; RBMX; HNRNPK AND HNRNPM, SUBCELLULAR LOCATION, ACETYLATION AT
RP LYS-125, AND MUTAGENESIS OF ARG-55 AND LYS-125.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [38]
RP ACETYLATION AT VAL-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [39]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28 AND LYS-82, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [41]
RP FUNCTION.
RX PubMed=30328013; DOI=10.1007/s12250-018-0058-6;
RA Mahesutihan M., Zheng W., Cui L., Li Y., Jiao P., Yang W., Liu W., Li J.,
RA Fan W., Yang L., Liu W., Sun L.;
RT "CypA Regulates AIP4-Mediated M1 Ubiquitination of Influenza A Virus.";
RL Virol. Sin. 33:440-448(2018).
RN [42]
RP FUNCTION, AND INTERACTION WITH FOXO1.
RX PubMed=31063815; DOI=10.1016/j.cellsig.2019.04.014;
RA Xie Y., Li X., Ge J.;
RT "Cyclophilin A-FoxO1 signaling pathway in endothelial cell apoptosis.";
RL Cell. Signal. 61:57-65(2019).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND STRUCTURE BY NMR.
RX PubMed=1896075; DOI=10.1038/353276a0;
RA Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H., Wuethrich K.,
RA Walkinshaw M.D.;
RT "Structure of human cyclophilin and its binding site for cyclosporin A
RT determined by X-ray crystallography and NMR spectroscopy.";
RL Nature 353:276-279(1991).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1946361; DOI=10.1073/pnas.88.21.9483;
RA Ke H., Zydowsky L.D., Liu J., Walsh C.T.;
RT "Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
RX PubMed=8421501; DOI=10.1038/361091a0;
RA Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M.,
RA Walkinshaw M.D.;
RT "X-ray structure of a decameric cyclophilin-cyclosporin crystal complex.";
RL Nature 361:91-94(1993).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8263916; DOI=10.1006/jmbi.1993.1664;
RA Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.;
RT "X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex
RT at 2.1-A resolution.";
RL J. Mol. Biol. 234:1119-1130(1993).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8652511; DOI=10.1021/bi9602775;
RA Zhao Y., Ke H.;
RT "Crystal structure implies that cyclophilin predominantly catalyzes the
RT trans to cis isomerization.";
RL Biochemistry 35:7356-7361(1996).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
RX PubMed=9385632; DOI=10.1002/pro.5560061103;
RA Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.;
RT "Crystal structure of cyclophilin A complexed with a binding site peptide
RT from the HIV-1 capsid protein.";
RL Protein Sci. 6:2297-2307(1997).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9769216; DOI=10.1006/jmbi.1998.2108;
RA Kallen J., Mikol V., Taylor P., Walkinshaw M.D.;
RT "X-ray structures and analysis of 11 cyclosporin derivatives complexed with
RT cyclophilin A.";
RL J. Mol. Biol. 283:435-449(1998).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPP3CA.
RX PubMed=12218175; DOI=10.1073/pnas.192206699;
RA Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
RT "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but
RT distinct recognition of immunophilin-drug complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH PPP3CA.
RX PubMed=12357034; DOI=10.1073/pnas.212504399;
RA Jin L., Harrison S.C.;
RT "Crystal structure of human calcineurin complexed with cyclosporin A and
RT human cyclophilin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
RN [52]
RP STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
RX PubMed=8421500; DOI=10.1038/361088a0;
RA Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T., Holzman T.F.,
RA Simmer R.L., Fesik S.W.;
RT "Solution structure of the cyclosporin A/cyclophilin complex by NMR.";
RL Nature 361:88-91(1993).
RN [53]
RP STRUCTURE BY NMR.
RX PubMed=9299338; DOI=10.1006/jmbi.1997.1220;
RA Ottiger M., Zerbe O., Guentert P., Wuethrich K.;
RT "The NMR solution conformation of unligated human cyclophilin A.";
RL J. Mol. Biol. 272:64-81(1997).
RN [54]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) ALONE AND IN COMPLEX WITH
RP CYCLOSPORINE AND HIV-1 CAPSID, AND ACETYLATION AT LYS-125.
RX PubMed=20364129; DOI=10.1038/nchembio.342;
RA Lammers M., Neumann H., Chin J.W., James L.C.;
RT "Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV
RT isomerization.";
RL Nat. Chem. Biol. 6:331-337(2010).
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357,
CC PubMed:21245143, PubMed:25678563, PubMed:21593166). Exerts a strong
CC chemotactic effect on leukocytes partly through activation of one of
CC its membrane receptors BSG/CD147, initiating a signaling cascade that
CC culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143).
CC Activates endothelial cells (ECs) in a pro-inflammatory manner by
CC stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases
CC and by inducing expression of adhesion molecules including SELE and
CC VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the
CC FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC
CC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative
CC stress, initiates proapoptotic and antiapoptotic signaling in ECs via
CC activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic
CC protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase
CC activity, autophosphorylation and oxidative stress-induced apoptosis
CC mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly
CC of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes
CC and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent
CC expression of HDAC6, ATG7 and VCP which are involved in clearance of
CC protein aggregates (PubMed:25678563). Plays an important role in
CC platelet activation and aggregation (By similarity). Regulates calcium
CC mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via
CC increased ROS production as well as by facilitating the interaction
CC between integrin and the cell cytoskeleton (By similarity). Binds
CC heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits
CC replication of influenza A virus (IAV) (PubMed:19207730). Inhibits
CC ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by
CC impairing the interaction of ITCH/AIP4 with M1, followed by the
CC suppression of the nuclear export of M1, and finally reduction of the
CC replication of IAV (PubMed:30328013, PubMed:22347431).
CC {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11943775,
CC ECO:0000269|PubMed:15130913, ECO:0000269|PubMed:19207730,
CC ECO:0000269|PubMed:2001362, ECO:0000269|PubMed:20676357,
CC ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:21593166,
CC ECO:0000269|PubMed:22347431, ECO:0000269|PubMed:23180369,
CC ECO:0000269|PubMed:25678563, ECO:0000269|PubMed:26095851,
CC ECO:0000269|PubMed:30328013, ECO:0000269|PubMed:31063815}.
CC -!- FUNCTION: (Microbial infection) May act as a mediator between human
CC SARS coronavirus nucleoprotein and BSG/CD147 in the process of invasion
CC of host cells by the virus (PubMed:15688292).
CC {ECO:0000269|PubMed:15688292}.
CC -!- FUNCTION: (Microbial infection) Stimulates RNA-binding ability of HCV
CC NS5A in a peptidyl-prolyl cis-trans isomerase activity-dependent
CC manner. {ECO:0000269|PubMed:21593166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:2001362,
CC ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:21245143,
CC ECO:0000269|PubMed:21593166, ECO:0000269|PubMed:25678563,
CC ECO:0000305|PubMed:19207730, ECO:0000305|PubMed:26095851};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC {ECO:0000269|PubMed:2001362}.
CC -!- SUBUNIT: Interacts with protein phosphatase PPP3CA/calcineurin A
CC (PubMed:12218175, PubMed:12357034). Interacts with PRPF19 isoform 2
CC (via N-terminus) (By similarity). Interacts with isoform 2 of BSG/CD147
CC (PubMed:15688292, PubMed:11353871, PubMed:11943775, PubMed:21245143).
CC Interacts with FOXO1; the interaction promotes FOXO1 dephosphorylation,
CC nuclear accumulation and transcriptional activity (PubMed:31063815).
CC Interacts with integrin ITGA2B:ITGB3; the interaction is ROS and
CC peptidyl-prolyl cis-trans isomerase (PPIase) activity-dependent and is
CC increased in the presence of thrombin (By similarity). Interacts with
CC MAP3K5 (PubMed:26095851). Interacts with TARDBP; the interaction is
CC dependent on the RNA-binding activity of TARDBP and the PPIase activity
CC of PPIA/CYPA and the acetylation of PPIA/CYPA at Lys-125 favors the
CC interaction (PubMed:25678563). Interacts with HNRNPA1, HNRNPA2B1,
CC HNRNPC, RBMX, HNRNPK and HNRNPM (PubMed:25678563).
CC {ECO:0000250|UniProtKB:P17742, ECO:0000269|PubMed:11353871,
CC ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:12218175,
CC ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:15688292,
CC ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:25678563,
CC ECO:0000269|PubMed:26095851, ECO:0000269|PubMed:31063815}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 capsid protein
CC (PubMed:20364129, PubMed:8513493). {ECO:0000269|PubMed:20364129,
CC ECO:0000269|PubMed:8513493}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human SARS coronavirus
CC nucleoprotein. {ECO:0000269|PubMed:15688292}.
CC -!- SUBUNIT: (Microbial infection) Interacts with measles virus
CC nucleoprotein. {ECO:0000269|PubMed:20147391}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus matrix
CC protein 1. {ECO:0000269|PubMed:19207730}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV NS5A; the interaction
CC stimulates RNA-binding ability of NS5A and is dependent on the
CC peptidyl-prolyl cis-trans isomerase activity of PPIA/CYPA.
CC {ECO:0000269|PubMed:21593166}.
CC -!- INTERACTION:
CC P62937; P05067: APP; NbExp=4; IntAct=EBI-437708, EBI-77613;
CC P62937; P35613: BSG; NbExp=2; IntAct=EBI-437708, EBI-750709;
CC P62937; Q00535: CDK5; NbExp=3; IntAct=EBI-437708, EBI-1041567;
CC P62937; P46108-1: CRK; NbExp=4; IntAct=EBI-437708, EBI-287556;
CC P62937; O43614: HCRTR2; NbExp=3; IntAct=EBI-437708, EBI-25884102;
CC P62937; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-437708, EBI-739832;
CC P62937; O75376: NCOR1; NbExp=3; IntAct=EBI-437708, EBI-347233;
CC P62937; Q16849: PTPRN; NbExp=3; IntAct=EBI-437708, EBI-728153;
CC P62937; P62841: RPS15; NbExp=3; IntAct=EBI-437708, EBI-372635;
CC P62937; O00267: SUPT5H; NbExp=2; IntAct=EBI-437708, EBI-710464;
CC P62937; Q72497: gag; Xeno; NbExp=7; IntAct=EBI-437708, EBI-1036263;
CC P62937; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-437708, EBI-25475856;
CC P62937; P59595: N; Xeno; NbExp=4; IntAct=EBI-437708, EBI-7602718;
CC P62937; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=4; IntAct=EBI-437708, EBI-25475797;
CC P62937; PRO_0000045602 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-437708, EBI-6927873;
CC P62937-2; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-25884072, EBI-5280499;
CC P62937-2; Q14032: BAAT; NbExp=3; IntAct=EBI-25884072, EBI-8994378;
CC P62937-2; Q6PH81: C16orf87; NbExp=3; IntAct=EBI-25884072, EBI-6598617;
CC P62937-2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-25884072, EBI-742887;
CC P62937-2; Q96NE9-2: FRMD6; NbExp=3; IntAct=EBI-25884072, EBI-13213391;
CC P62937-2; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-25884072, EBI-618189;
CC P62937-2; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-25884072, EBI-9088619;
CC P62937-2; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-25884072, EBI-11959863;
CC P62937-2; P52597: HNRNPF; NbExp=3; IntAct=EBI-25884072, EBI-352986;
CC P62937-2; Q02363: ID2; NbExp=3; IntAct=EBI-25884072, EBI-713450;
CC P62937-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-25884072, EBI-743960;
CC P62937-2; Q9H8H3: METTL7A; NbExp=3; IntAct=EBI-25884072, EBI-1390168;
CC P62937-2; Q9BRX2: PELO; NbExp=3; IntAct=EBI-25884072, EBI-1043580;
CC P62937-2; P07225: PROS1; NbExp=3; IntAct=EBI-25884072, EBI-2803380;
CC P62937-2; Q13573: SNW1; NbExp=3; IntAct=EBI-25884072, EBI-632715;
CC P62937-2; P56693: SOX10; NbExp=3; IntAct=EBI-25884072, EBI-1167533;
CC P62937-2; Q13586: STIM1; NbExp=3; IntAct=EBI-25884072, EBI-448878;
CC P62937-2; Q13033-2: STRN3; NbExp=3; IntAct=EBI-25884072, EBI-1053876;
CC P62937-2; P15884: TCF4; NbExp=3; IntAct=EBI-25884072, EBI-533224;
CC P62937-2; Q9UJA5: TRMT6; NbExp=3; IntAct=EBI-25884072, EBI-934061;
CC P62937-2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-25884072, EBI-12040603;
CC P62937-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-25884072, EBI-14104088;
CC P62937-2; Q15776: ZKSCAN8; NbExp=3; IntAct=EBI-25884072, EBI-2602314;
CC P62937-2; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-25884072, EBI-12010736;
CC P62937-2; O15535: ZSCAN9; NbExp=3; IntAct=EBI-25884072, EBI-751531;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26095851}. Secreted
CC {ECO:0000269|PubMed:16527992}. Nucleus {ECO:0000269|PubMed:25678563}.
CC Note=Secretion occurs in response to oxidative stress in vascular
CC smooth muscle through a vesicular secretory pathway that includes Rho
CC GTPase signaling, actin remodeling, and myosin II activation.
CC {ECO:0000269|PubMed:16527992}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62937-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62937-2; Sequence=VSP_056050;
CC -!- PTM: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans
CC isomerization and stabilizes cis rather than trans forms of the HIV-1
CC capsid. PPIA acetylation also antagonizes the immunosuppressive effects
CC of cyclosporine by inhibiting the sequential steps of cyclosporine
CC binding and calcineurin inhibition (PubMed:20364129, Ref.12).
CC Acetylation at Lys-125 favors its interaction with TARDBP
CC (PubMed:25678563). {ECO:0000269|PubMed:20364129,
CC ECO:0000269|PubMed:25678563, ECO:0000269|Ref.12}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ppia/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
CC URL="https://en.wikipedia.org/wiki/Cyclophilin";
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DR EMBL; Y00052; CAA68264.1; -; mRNA.
DR EMBL; X52851; CAA37039.1; -; Genomic_DNA.
DR EMBL; AK290085; BAF82774.1; -; mRNA.
DR EMBL; AK293003; BAF85692.1; -; mRNA.
DR EMBL; CR456707; CAG32988.1; -; mRNA.
DR EMBL; AB451307; BAG70121.1; -; mRNA.
DR EMBL; AB451438; BAG70252.1; -; mRNA.
DR EMBL; AY739283; AAU13906.1; -; Genomic_DNA.
DR EMBL; AC004854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC013436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000689; AAH00689.1; -; mRNA.
DR EMBL; BC003026; AAH03026.2; -; mRNA.
DR EMBL; BC005320; AAH05320.1; -; mRNA.
DR EMBL; BC005982; AAH05982.1; -; mRNA.
DR EMBL; BC007104; AAH07104.1; -; mRNA.
DR EMBL; BC013915; AAH13915.1; -; mRNA.
DR EMBL; BC073992; AAH73992.1; -; mRNA.
DR EMBL; BC093076; AAH93076.1; -; mRNA.
DR EMBL; BC106030; AAI06031.1; -; mRNA.
DR EMBL; BC137057; AAI37058.1; -; mRNA.
DR EMBL; BC137058; AAI37059.1; -; mRNA.
DR CCDS; CCDS5494.1; -. [P62937-1]
DR CCDS; CCDS75592.1; -. [P62937-2]
DR PIR; A94496; CSHUA.
DR RefSeq; NP_001287910.1; NM_001300981.1. [P62937-2]
DR RefSeq; NP_066953.1; NM_021130.4. [P62937-1]
DR PDB; 1AK4; X-ray; 2.36 A; A/B=1-165.
DR PDB; 1AWQ; X-ray; 1.58 A; A=2-165.
DR PDB; 1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165.
DR PDB; 1AWS; X-ray; 2.55 A; A=2-165.
DR PDB; 1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165.
DR PDB; 1AWU; X-ray; 2.34 A; A=2-165.
DR PDB; 1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165.
DR PDB; 1BCK; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWA; X-ray; 2.10 A; A=1-165.
DR PDB; 1CWB; X-ray; 2.20 A; A=1-165.
DR PDB; 1CWC; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWF; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWH; X-ray; 1.86 A; A=1-165.
DR PDB; 1CWI; X-ray; 1.90 A; A=1-165.
DR PDB; 1CWJ; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWK; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWL; X-ray; 1.80 A; A=1-165.
DR PDB; 1CWM; X-ray; 2.00 A; A=1-165.
DR PDB; 1CWO; X-ray; 1.86 A; A=1-165.
DR PDB; 1FGL; X-ray; 1.80 A; A=1-165.
DR PDB; 1M63; X-ray; 2.80 A; C/G=1-165.
DR PDB; 1M9C; X-ray; 2.00 A; A/B=1-165.
DR PDB; 1M9D; X-ray; 1.90 A; A/B=1-165.
DR PDB; 1M9E; X-ray; 1.72 A; A/B=1-164.
DR PDB; 1M9F; X-ray; 1.73 A; A/B=1-165.
DR PDB; 1M9X; X-ray; 1.70 A; A/B/E/F=1-165.
DR PDB; 1M9Y; X-ray; 1.90 A; A/B/E/F=1-165.
DR PDB; 1MF8; X-ray; 3.10 A; C=1-165.
DR PDB; 1MIK; X-ray; 1.76 A; A=1-165.
DR PDB; 1NMK; X-ray; 2.10 A; A/B=1-165.
DR PDB; 1OCA; NMR; -; A=1-165.
DR PDB; 1RMH; X-ray; 2.40 A; A/B=2-165.
DR PDB; 1VBS; X-ray; 2.00 A; A=1-165.
DR PDB; 1VBT; X-ray; 2.30 A; A/B=1-165.
DR PDB; 1W8L; X-ray; 1.80 A; A=2-165.
DR PDB; 1W8M; X-ray; 1.65 A; A=2-165.
DR PDB; 1W8V; X-ray; 1.70 A; A=2-165.
DR PDB; 1YND; X-ray; 1.60 A; A/B=1-165.
DR PDB; 1ZKF; X-ray; 2.55 A; A/B=1-165.
DR PDB; 2ALF; X-ray; 1.90 A; A=2-165.
DR PDB; 2CPL; X-ray; 1.63 A; A=1-165.
DR PDB; 2CYH; X-ray; 1.64 A; A=2-165.
DR PDB; 2MS4; NMR; -; A=1-165.
DR PDB; 2MZU; NMR; -; A=1-165.
DR PDB; 2N0T; NMR; -; A=1-165.
DR PDB; 2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 2X25; X-ray; 1.20 A; B=2-165.
DR PDB; 2X2A; X-ray; 1.40 A; A/B=1-165.
DR PDB; 2X2C; X-ray; 2.41 A; K/M/O/Q/S=1-165.
DR PDB; 2X2D; X-ray; 1.95 A; B/C=1-165.
DR PDB; 2XGY; X-ray; 1.80 A; B=1-165.
DR PDB; 3CYH; X-ray; 1.90 A; A=2-165.
DR PDB; 3CYS; NMR; -; A=1-165.
DR PDB; 3K0M; X-ray; 1.25 A; A=1-165.
DR PDB; 3K0N; X-ray; 1.39 A; A=1-165.
DR PDB; 3K0O; X-ray; 1.55 A; A=1-165.
DR PDB; 3K0P; X-ray; 1.65 A; A=1-165.
DR PDB; 3K0Q; X-ray; 2.32 A; A=1-165.
DR PDB; 3K0R; X-ray; 2.42 A; A=1-165.
DR PDB; 3ODI; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 3ODL; X-ray; 2.31 A; A/C/E/G/I/K/M/O/Q/S=1-165.
DR PDB; 3RDD; X-ray; 2.14 A; A=1-165.
DR PDB; 4CYH; X-ray; 2.10 A; A=2-165.
DR PDB; 4IPZ; X-ray; 1.67 A; A=1-165.
DR PDB; 4N1M; X-ray; 1.15 A; A=1-165.
DR PDB; 4N1N; X-ray; 1.50 A; A=1-165.
DR PDB; 4N1O; X-ray; 1.75 A; A=1-165.
DR PDB; 4N1P; X-ray; 1.90 A; A=1-165.
DR PDB; 4N1Q; X-ray; 1.65 A; A=1-165.
DR PDB; 4N1R; X-ray; 1.80 A; A=1-165.
DR PDB; 4N1S; X-ray; 1.47 A; A=1-165.
DR PDB; 4YUG; X-ray; 1.48 A; A=1-165.
DR PDB; 4YUH; X-ray; 1.34 A; A=1-165.
DR PDB; 4YUI; X-ray; 1.38 A; A=1-165.
DR PDB; 4YUJ; X-ray; 1.42 A; A=1-165.
DR PDB; 4YUK; X-ray; 1.48 A; A=1-165.
DR PDB; 4YUL; X-ray; 1.42 A; A=1-165.
DR PDB; 4YUM; X-ray; 1.50 A; A=1-165.
DR PDB; 4YUN; X-ray; 1.58 A; A=1-165.
DR PDB; 4YUO; X-ray; 1.20 A; A=1-165.
DR PDB; 4YUP; X-ray; 1.75 A; A=1-165.
DR PDB; 5CYH; X-ray; 2.10 A; A=2-165.
DR PDB; 5F66; X-ray; 1.15 A; A=1-165.
DR PDB; 5FJB; EM; 9.00 A; C=2-165.
DR PDB; 5KUL; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUN; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUO; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUQ; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUR; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUS; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUU; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUV; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUW; X-ray; 1.70 A; A=2-165.
DR PDB; 5KUZ; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV0; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV1; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV2; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV3; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV4; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV5; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV6; X-ray; 1.70 A; A=2-165.
DR PDB; 5KV7; X-ray; 1.70 A; A=2-165.
DR PDB; 5LUD; X-ray; 1.25 A; A=1-165.
DR PDB; 5NOQ; X-ray; 1.60 A; A=1-165.
DR PDB; 5NOR; X-ray; 1.80 A; A=1-165.
DR PDB; 5NOS; X-ray; 1.35 A; A=1-165.
DR PDB; 5NOT; X-ray; 1.45 A; A=1-165.
DR PDB; 5NOU; X-ray; 1.30 A; A=1-165.
DR PDB; 5NOV; X-ray; 2.00 A; A=1-165.
DR PDB; 5NOW; X-ray; 1.48 A; A=1-165.
DR PDB; 5NOX; X-ray; 1.49 A; A=1-165.
DR PDB; 5NOY; X-ray; 1.43 A; A=1-165.
DR PDB; 5NOZ; X-ray; 1.61 A; A=1-165.
DR PDB; 5T9U; X-ray; 2.30 A; A/B/C/D=1-164.
DR PDB; 5T9W; X-ray; 2.00 A; A=2-165.
DR PDB; 5T9Z; X-ray; 1.40 A; A=2-164.
DR PDB; 5TA2; X-ray; 1.48 A; A=2-164.
DR PDB; 5TA4; X-ray; 1.50 A; A=2-165.
DR PDB; 5WC7; X-ray; 1.43 A; A=1-165.
DR PDB; 6BTA; X-ray; 1.50 A; A=1-165.
DR PDB; 6GJI; X-ray; 1.60 A; A=1-165.
DR PDB; 6GJJ; X-ray; 1.38 A; A=1-165.
DR PDB; 6GJL; X-ray; 1.16 A; A=1-165.
DR PDB; 6GJM; X-ray; 1.35 A; A=1-165.
DR PDB; 6GJN; X-ray; 1.70 A; A=1-165.
DR PDB; 6GJP; X-ray; 1.94 A; A=1-165.
DR PDB; 6GJR; X-ray; 1.69 A; A=1-165.
DR PDB; 6GJY; X-ray; 1.29 A; A=1-165.
DR PDB; 6GS6; X-ray; 1.16 A; A=1-165.
DR PDB; 6I42; X-ray; 1.38 A; A=2-165.
DR PDB; 6U5C; X-ray; 1.62 A; A=1-165.
DR PDB; 6U5D; X-ray; 1.65 A; A=1-165.
DR PDB; 6U5E; X-ray; 1.56 A; A=1-165.
DR PDB; 6U5G; EM; 2.50 A; A=1-165.
DR PDB; 6X3R; X-ray; 1.80 A; A=1-165.
DR PDB; 6X3Y; X-ray; 1.40 A; A=1-165.
DR PDB; 6X4M; X-ray; 1.50 A; A=1-165.
DR PDB; 6X4N; X-ray; 1.51 A; A=1-165.
DR PDB; 6X4O; X-ray; 1.50 A; A=1-165.
DR PDB; 6X4P; X-ray; 1.50 A; A=1-165.
DR PDB; 6X4Q; X-ray; 1.80 A; A=1-165.
DR PDB; 6Y9V; EM; 6.90 A; J=2-165.
DR PDB; 6Y9W; EM; 4.10 A; J=2-165.
DR PDB; 6Y9X; EM; 4.40 A; J=2-165.
DR PDB; 6Y9Y; EM; 6.10 A; J=2-165.
DR PDB; 6Y9Z; EM; 4.80 A; J=2-165.
DR PDB; 6ZDJ; EM; 5.80 A; J=2-165.
DR PDB; 7ABT; X-ray; 1.31 A; A=2-164.
DR PDBsum; 1AK4; -.
DR PDBsum; 1AWQ; -.
DR PDBsum; 1AWR; -.
DR PDBsum; 1AWS; -.
DR PDBsum; 1AWT; -.
DR PDBsum; 1AWU; -.
DR PDBsum; 1AWV; -.
DR PDBsum; 1BCK; -.
DR PDBsum; 1CWA; -.
DR PDBsum; 1CWB; -.
DR PDBsum; 1CWC; -.
DR PDBsum; 1CWF; -.
DR PDBsum; 1CWH; -.
DR PDBsum; 1CWI; -.
DR PDBsum; 1CWJ; -.
DR PDBsum; 1CWK; -.
DR PDBsum; 1CWL; -.
DR PDBsum; 1CWM; -.
DR PDBsum; 1CWO; -.
DR PDBsum; 1FGL; -.
DR PDBsum; 1M63; -.
DR PDBsum; 1M9C; -.
DR PDBsum; 1M9D; -.
DR PDBsum; 1M9E; -.
DR PDBsum; 1M9F; -.
DR PDBsum; 1M9X; -.
DR PDBsum; 1M9Y; -.
DR PDBsum; 1MF8; -.
DR PDBsum; 1MIK; -.
DR PDBsum; 1NMK; -.
DR PDBsum; 1OCA; -.
DR PDBsum; 1RMH; -.
DR PDBsum; 1VBS; -.
DR PDBsum; 1VBT; -.
DR PDBsum; 1W8L; -.
DR PDBsum; 1W8M; -.
DR PDBsum; 1W8V; -.
DR PDBsum; 1YND; -.
DR PDBsum; 1ZKF; -.
DR PDBsum; 2ALF; -.
DR PDBsum; 2CPL; -.
DR PDBsum; 2CYH; -.
DR PDBsum; 2MS4; -.
DR PDBsum; 2MZU; -.
DR PDBsum; 2N0T; -.
DR PDBsum; 2RMA; -.
DR PDBsum; 2RMB; -.
DR PDBsum; 2X25; -.
DR PDBsum; 2X2A; -.
DR PDBsum; 2X2C; -.
DR PDBsum; 2X2D; -.
DR PDBsum; 2XGY; -.
DR PDBsum; 3CYH; -.
DR PDBsum; 3CYS; -.
DR PDBsum; 3K0M; -.
DR PDBsum; 3K0N; -.
DR PDBsum; 3K0O; -.
DR PDBsum; 3K0P; -.
DR PDBsum; 3K0Q; -.
DR PDBsum; 3K0R; -.
DR PDBsum; 3ODI; -.
DR PDBsum; 3ODL; -.
DR PDBsum; 3RDD; -.
DR PDBsum; 4CYH; -.
DR PDBsum; 4IPZ; -.
DR PDBsum; 4N1M; -.
DR PDBsum; 4N1N; -.
DR PDBsum; 4N1O; -.
DR PDBsum; 4N1P; -.
DR PDBsum; 4N1Q; -.
DR PDBsum; 4N1R; -.
DR PDBsum; 4N1S; -.
DR PDBsum; 4YUG; -.
DR PDBsum; 4YUH; -.
DR PDBsum; 4YUI; -.
DR PDBsum; 4YUJ; -.
DR PDBsum; 4YUK; -.
DR PDBsum; 4YUL; -.
DR PDBsum; 4YUM; -.
DR PDBsum; 4YUN; -.
DR PDBsum; 4YUO; -.
DR PDBsum; 4YUP; -.
DR PDBsum; 5CYH; -.
DR PDBsum; 5F66; -.
DR PDBsum; 5FJB; -.
DR PDBsum; 5KUL; -.
DR PDBsum; 5KUN; -.
DR PDBsum; 5KUO; -.
DR PDBsum; 5KUQ; -.
DR PDBsum; 5KUR; -.
DR PDBsum; 5KUS; -.
DR PDBsum; 5KUU; -.
DR PDBsum; 5KUV; -.
DR PDBsum; 5KUW; -.
DR PDBsum; 5KUZ; -.
DR PDBsum; 5KV0; -.
DR PDBsum; 5KV1; -.
DR PDBsum; 5KV2; -.
DR PDBsum; 5KV3; -.
DR PDBsum; 5KV4; -.
DR PDBsum; 5KV5; -.
DR PDBsum; 5KV6; -.
DR PDBsum; 5KV7; -.
DR PDBsum; 5LUD; -.
DR PDBsum; 5NOQ; -.
DR PDBsum; 5NOR; -.
DR PDBsum; 5NOS; -.
DR PDBsum; 5NOT; -.
DR PDBsum; 5NOU; -.
DR PDBsum; 5NOV; -.
DR PDBsum; 5NOW; -.
DR PDBsum; 5NOX; -.
DR PDBsum; 5NOY; -.
DR PDBsum; 5NOZ; -.
DR PDBsum; 5T9U; -.
DR PDBsum; 5T9W; -.
DR PDBsum; 5T9Z; -.
DR PDBsum; 5TA2; -.
DR PDBsum; 5TA4; -.
DR PDBsum; 5WC7; -.
DR PDBsum; 6BTA; -.
DR PDBsum; 6GJI; -.
DR PDBsum; 6GJJ; -.
DR PDBsum; 6GJL; -.
DR PDBsum; 6GJM; -.
DR PDBsum; 6GJN; -.
DR PDBsum; 6GJP; -.
DR PDBsum; 6GJR; -.
DR PDBsum; 6GJY; -.
DR PDBsum; 6GS6; -.
DR PDBsum; 6I42; -.
DR PDBsum; 6U5C; -.
DR PDBsum; 6U5D; -.
DR PDBsum; 6U5E; -.
DR PDBsum; 6U5G; -.
DR PDBsum; 6X3R; -.
DR PDBsum; 6X3Y; -.
DR PDBsum; 6X4M; -.
DR PDBsum; 6X4N; -.
DR PDBsum; 6X4O; -.
DR PDBsum; 6X4P; -.
DR PDBsum; 6X4Q; -.
DR PDBsum; 6Y9V; -.
DR PDBsum; 6Y9W; -.
DR PDBsum; 6Y9X; -.
DR PDBsum; 6Y9Y; -.
DR PDBsum; 6Y9Z; -.
DR PDBsum; 6ZDJ; -.
DR PDBsum; 7ABT; -.
DR AlphaFoldDB; P62937; -.
DR BMRB; P62937; -.
DR SMR; P62937; -.
DR BioGRID; 111474; 296.
DR CORUM; P62937; -.
DR DIP; DIP-6080N; -.
DR IntAct; P62937; 138.
DR MINT; P62937; -.
DR STRING; 9606.ENSP00000419425; -.
DR BindingDB; P62937; -.
DR ChEMBL; CHEMBL1949; -.
DR DrugBank; DB01742; (3r)-1-Acetyl-3-Methylpiperidine.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00091; Cyclosporine.
DR DrugBank; DB02419; Ethyl Oxo(Piperidin-1-Yl)Acetate.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB03393; Sanglifehrin A.
DR DrugCentral; P62937; -.
DR GuidetoPHARMACOLOGY; 2751; -.
DR GlyGen; P62937; 2 sites, 2 O-linked glycans (1 site).
DR iPTMnet; P62937; -.
DR MetOSite; P62937; -.
DR PhosphoSitePlus; P62937; -.
DR SwissPalm; P62937; -.
DR BioMuta; PPIA; -.
DR DMDM; 51702775; -.
DR DOSAC-COBS-2DPAGE; P62937; -.
DR OGP; P62937; -.
DR REPRODUCTION-2DPAGE; IPI00419585; -.
DR REPRODUCTION-2DPAGE; P62937; -.
DR SWISS-2DPAGE; P62937; -.
DR UCD-2DPAGE; P62937; -.
DR EPD; P62937; -.
DR jPOST; P62937; -.
DR MassIVE; P62937; -.
DR PaxDb; P62937; -.
DR PeptideAtlas; P62937; -.
DR PRIDE; P62937; -.
DR ProteomicsDB; 57455; -. [P62937-1]
DR ProteomicsDB; 62564; -.
DR TopDownProteomics; P62937-1; -. [P62937-1]
DR ABCD; P62937; 2 sequenced antibodies.
DR Antibodypedia; 13466; 671 antibodies from 44 providers.
DR DNASU; 5478; -.
DR Ensembl; ENST00000355968.10; ENSP00000430817.1; ENSG00000196262.15. [P62937-2]
DR Ensembl; ENST00000468812.6; ENSP00000419425.1; ENSG00000196262.15. [P62937-1]
DR Ensembl; ENST00000489459.5; ENSP00000427976.1; ENSG00000196262.15. [P62937-2]
DR Ensembl; ENST00000677022.1; ENSP00000504216.1; ENSG00000196262.15. [P62937-2]
DR Ensembl; ENST00000677107.1; ENSP00000504735.1; ENSG00000196262.15. [P62937-2]
DR Ensembl; ENST00000678789.1; ENSP00000503804.1; ENSG00000196262.15. [P62937-2]
DR Ensembl; ENST00000678805.1; ENSP00000502945.1; ENSG00000196262.15. [P62937-2]
DR GeneID; 5478; -.
DR KEGG; hsa:5478; -.
DR MANE-Select; ENST00000468812.6; ENSP00000419425.1; NM_021130.5; NP_066953.1.
DR UCSC; uc064djo.1; human. [P62937-1]
DR CTD; 5478; -.
DR DisGeNET; 5478; -.
DR GeneCards; PPIA; -.
DR HGNC; HGNC:9253; PPIA.
DR HPA; ENSG00000196262; Low tissue specificity.
DR MIM; 123840; gene.
DR neXtProt; NX_P62937; -.
DR OpenTargets; ENSG00000196262; -.
DR PharmGKB; PA33574; -.
DR VEuPathDB; HostDB:ENSG00000196262; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00950000183087; -.
DR HOGENOM; CLU_012062_38_0_1; -.
DR InParanoid; P62937; -.
DR OMA; MRAPIVN; -.
DR PhylomeDB; P62937; -.
DR TreeFam; TF316719; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; P62937; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-162585; Uncoating of the HIV Virion.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
DR Reactome; R-HSA-164516; Minus-strand DNA synthesis.
DR Reactome; R-HSA-164525; Plus-strand DNA synthesis.
DR Reactome; R-HSA-173107; Binding and entry of HIV virion.
DR Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-2025928; Calcineurin activates NFAT.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; P62937; -.
DR BioGRID-ORCS; 5478; 548 hits in 1053 CRISPR screens.
DR ChiTaRS; PPIA; human.
DR EvolutionaryTrace; P62937; -.
DR GeneWiki; Peptidylprolyl_isomerase_A; -.
DR GenomeRNAi; 5478; -.
DR Pharos; P62937; Tclin.
DR PRO; PR:P62937; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P62937; protein.
DR Bgee; ENSG00000196262; Expressed in ventricular zone and 178 other tissues.
DR ExpressionAtlas; P62937; baseline and differential.
DR Genevisible; P62937; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0016018; F:cyclosporin A binding; IDA:UniProtKB.
DR GO; GO:1904399; F:heparan sulfate binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
DR GO; GO:0046790; F:virion binding; NAS:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0060352; P:cell adhesion molecule production; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0042118; P:endothelial cell activation; IDA:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IMP:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IMP:UniProtKB.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0061944; P:negative regulation of protein K48-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:1903901; P:negative regulation of viral life cycle; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:2001233; P:regulation of apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0045069; P:regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Host-virus interaction; Isomerase;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Rotamase;
KW Secreted; Ubl conjugation.
FT CHAIN 1..165
FT /note="Peptidyl-prolyl cis-trans isomerase A"
FT /id="PRO_0000423240"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:25489052, ECO:0000269|PubMed:7657784,
FT ECO:0000269|Ref.11, ECO:0000269|Ref.12,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..165
FT /note="Peptidyl-prolyl cis-trans isomerase A, N-terminally
FT processed"
FT /id="PRO_0000064115"
FT DOMAIN 7..163
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="N-acetylvaline; partial; in Peptidyl-prolyl cis-
FT trans isomerase A, N-terminally processed"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20364129,
FT ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17742"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 28
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..60
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_056050"
FT MUTAGEN 55
FT /note="R->A: Loss of peptidyl-prolyl cis-trans isomerase
FT activity. No loss of its interaction with BSG/CD147 or its
FT ability to induce leukocyte chemotaxis. No effect on its
FT interaction with MAP3K5/ASK1. Loss of its ability to
FT negatively regulate oxidative stress-induced apoptosis
FT mediated by MAP3K5/ASK1. Reduced interaction with TARDBP.
FT No loss of interaction with influenza A virus matrix
FT protein 1 or its ability to inhibit viral replication."
FT /evidence="ECO:0000269|PubMed:19207730,
FT ECO:0000269|PubMed:21245143, ECO:0000269|PubMed:25678563,
FT ECO:0000269|PubMed:26095851"
FT MUTAGEN 60
FT /note="F->A: Loss of ability to stimulate MAPK/ERK
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:11943775"
FT MUTAGEN 69
FT /note="R->A: No effect on peptidyl-prolyl cis-trans
FT isomerase activity. Reduced interaction with BSG/CD147 and
FT ability to induce leukocyte chemotaxis."
FT /evidence="ECO:0000269|PubMed:21245143"
FT MUTAGEN 70
FT /note="H->A: No effect on peptidyl-prolyl cis-trans
FT isomerase activity. Reduced interaction with BSG/CD147 and
FT ability to induce leukocyte chemotaxis."
FT /evidence="ECO:0000269|PubMed:21245143"
FT MUTAGEN 107
FT /note="T->A: No effect on peptidyl-prolyl cis-trans
FT isomerase activity. Reduced interaction with BSG/CD147 and
FT ability to induce leukocyte chemotaxis."
FT /evidence="ECO:0000269|PubMed:21245143"
FT MUTAGEN 113
FT /note="F->A: Reduced ability to stimulate MAPK/ERK
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:11943775"
FT MUTAGEN 121
FT /note="W->A: 200-fold decrease of sensitivity to CsA.
FT Reduced ability to stimulate MAPK/ERK phosphorylation."
FT /evidence="ECO:0000269|PubMed:11943775,
FT ECO:0000269|PubMed:2001362"
FT MUTAGEN 121
FT /note="W->E: Loss of peptidyl-prolyl cis-trans isomerase
FT activity."
FT /evidence="ECO:0000269|PubMed:20676357"
FT MUTAGEN 121
FT /note="W->F: 75-fold decrease of sensitivity to CsA."
FT /evidence="ECO:0000269|PubMed:2001362"
FT MUTAGEN 121
FT /note="W->H: No effect on peptidyl-prolyl cis-trans
FT isomerase activity."
FT /evidence="ECO:0000269|PubMed:20676357"
FT MUTAGEN 125
FT /note="K->Q: Acetylation-mimetic mutant; no effect on its
FT interaction with TARDBP."
FT /evidence="ECO:0000269|PubMed:25678563"
FT MUTAGEN 125
FT /note="K->R: Loss of acetylation and interaction with
FT TARDBP."
FT /evidence="ECO:0000269|PubMed:25678563"
FT MUTAGEN 126
FT /note="H->A: Loss of peptidyl-prolyl cis-trans isomerase
FT activity and interaction with HCV NS5A. Loss of ability to
FT stimulate MAPK/ERK phosphorylation."
FT /evidence="ECO:0000269|PubMed:11943775,
FT ECO:0000269|PubMed:21593166"
FT CONFLICT 89
FT /note="I -> T (in Ref. 8; AAH05982)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="N -> I (in Ref. 8; AAH07104)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> D (in Ref. 4; CAG32988)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:4N1M"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:4N1M"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:4N1M"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4N1M"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4N1M"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2MS4"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4YUI"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6I42"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:7ABT"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:4N1M"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4N1M"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:4N1M"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4N1M"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:4N1M"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3K0O"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2MS4"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:4N1M"
SQ SEQUENCE 165 AA; 18012 MW; 9B2E637A555E4434 CRC64;
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE
