PPIB_HUMAN
ID PPIB_HUMAN Reviewed; 216 AA.
AC P23284; A8K534; Q6IBH5; Q9BVK5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase B;
DE Short=PPIase B;
DE EC=5.2.1.8 {ECO:0000269|PubMed:20676357};
DE AltName: Full=CYP-S1;
DE AltName: Full=Cyclophilin B;
DE AltName: Full=Rotamase B;
DE AltName: Full=S-cyclophilin;
DE Short=SCYLP;
DE Flags: Precursor;
GN Name=PPIB; Synonyms=CYPB;
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].
RX PubMed=2040592; DOI=10.1016/s0021-9258(18)99078-2;
RA Spik G., Haendler B., Delmas O., Mariller C., Chamoux M., Maes P.,
RA Tartar A., Montreuil J., Stedman K., Kocher H.P., Keller R., Hiestand P.C.,
RA Movva N.R.;
RT "A novel secreted cyclophilin-like protein (SCYLP).";
RL J. Biol. Chem. 266:10735-10738(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Prostate, and Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-216, AND PROTEIN SEQUENCE OF 34-48.
RX PubMed=2000394; DOI=10.1073/pnas.88.5.1903;
RA Price E.R., Zydowsky L.D., Jin M., Hunter C.H., McKeon F.D., Walsh C.T.;
RT "Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl
RT isomerase with a signal sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1903-1907(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-216.
RX PubMed=1710767; DOI=10.1128/mcb.11.7.3484-3491.1991;
RA Hasel K.W., Glass J.R., Godbout M., Sutcliffe J.G.;
RT "An endoplasmic reticulum-specific cyclophilin.";
RL Mol. Cell. Biol. 11:3484-3491(1991).
RN [10]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [11]
RP PROTEIN SEQUENCE OF 52-59; 64-76; 91-101; 138-150; 164-172 AND 197-207, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP PROTEIN SEQUENCE OF 72-84 AND 159-165.
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=1530944; DOI=10.1083/jcb.116.1.113;
RA Arber S., Krause K.-H., Caroni P.;
RT "S-cyclophilin is retained intracellularly via a unique COOH-terminal
RT sequence and colocalizes with the calcium storage protein calreticulin.";
RL J. Cell Biol. 116:113-125(1992).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [15]
RP INVOLVEMENT IN OI9.
RX PubMed=19781681; DOI=10.1016/j.ajhg.2009.09.001;
RA van Dijk F.S., Nesbitt I.M., Zwikstra E.H., Nikkels P.G., Piersma S.R.,
RA Fratantoni S.A., Jimenez C.R., Huizer M., Morsman A.C., Cobben J.M.,
RA van Roij M.H., Elting M.W., Verbeke J.I., Wijnaendts L.C., Shaw N.J.,
RA Hogler W., McKeown C., Sistermans E.A., Dalton A., Meijers-Heijboer H.,
RA Pals G.;
RT "PPIB mutations cause severe osteogenesis imperfecta.";
RL Am. J. Hum. Genet. 85:521-527(2009).
RN [16]
RP INTERACTION WITH MEASLES VIRUS NUCLEOPROTEIN (MICROBIAL INFECTION), AND
RP SUBCELLULAR LOCATION (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 [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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 [18]
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 [19]
RP INTERACTION WITH DYM.
RX PubMed=21280149; DOI=10.1002/humu.21413;
RA Denais C., Dent C.L., Southgate L., Hoyle J., Dafou D., Trembath R.C.,
RA Machado R.D.;
RT "Dymeclin, the gene underlying Dyggve-Melchior-Clausen syndrome, encodes a
RT protein integral to extracellular matrix and Golgi organization and is
RT associated with protein secretion pathways critical in bone development.";
RL Hum. Mutat. 32:231-239(2011).
RN [20]
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 [21]
RP IDENTIFICATION BY MASS 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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-216.
RX PubMed=8197205; DOI=10.1073/pnas.91.11.5183;
RA Mikol V., Kallen J., Walkinshaw M.D.;
RT "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with
RT cyclophilin A and delineation of its calcineurin-binding domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5183-5186(1994).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 34-216 IN COMPLEX WITH CLGN,
RP MUTAGENESIS OF LYS-129, AND INTERACTION WITH CALR; CANX AND CLGN.
RX PubMed=20801878; DOI=10.1074/jbc.m110.160101;
RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F.,
RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.;
RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P-
RT domain.";
RL J. Biol. Chem. 285:35551-35557(2010).
RN [24]
RP VARIANT OI9 ARG-9.
RX PubMed=20089953; DOI=10.1056/nejmoa0907705;
RA Barnes A.M., Carter E.M., Cabral W.A., Weis M., Chang W., Makareeva E.,
RA Leikin S., Rotimi C.N., Eyre D.R., Raggio C.L., Marini J.C.;
RT "Lack of cyclophilin B in osteogenesis imperfecta with normal collagen
RT folding.";
RL N. Engl. J. Med. 362:521-528(2010).
CC -!- FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline
CC imidic peptide bonds in oligopeptides and may therefore assist protein
CC folding. {ECO:0000269|PubMed:20676357}.
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;
CC Evidence={ECO:0000269|PubMed:20676357};
CC -!- ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA).
CC {ECO:0000305|PubMed:20676357}.
CC -!- SUBUNIT: Interacts with DYM. Interacts with CALR, CLGN and CANX. Part
CC of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1,
CC HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1 and very small
CC amounts of ERP29, but not, or at very low levels, CALR nor CANX
CC (PubMed:12475965). {ECO:0000269|PubMed:12475965,
CC ECO:0000269|PubMed:20801878, ECO:0000269|PubMed:21280149}.
CC -!- SUBUNIT: (Microbial infection) Interacts with measles virus
CC nucleoprotein. {ECO:0000269|PubMed:20147391}.
CC -!- INTERACTION:
CC P23284; Q8N9N5: BANP; NbExp=3; IntAct=EBI-359252, EBI-744695;
CC P23284; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-359252, EBI-1210604;
CC P23284; Q7RTS9: DYM; NbExp=4; IntAct=EBI-359252, EBI-2871106;
CC P23284; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-359252, EBI-618189;
CC P23284; O43292-2: GPAA1; NbExp=3; IntAct=EBI-359252, EBI-25884370;
CC P23284; Q9NWQ4-1: GPATCH2L; NbExp=3; IntAct=EBI-359252, EBI-11959863;
CC P23284; P09017: HOXC4; NbExp=3; IntAct=EBI-359252, EBI-3923226;
CC P23284; P17066: HSPA6; NbExp=3; IntAct=EBI-359252, EBI-355106;
CC P23284; Q02363: ID2; NbExp=3; IntAct=EBI-359252, EBI-713450;
CC P23284; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-359252, EBI-743960;
CC P23284; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-359252, EBI-750750;
CC P23284; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-359252, EBI-25835523;
CC P23284; P13667: PDIA4; NbExp=2; IntAct=EBI-359252, EBI-1054653;
CC P23284; P40855: PEX19; NbExp=6; IntAct=EBI-359252, EBI-594747;
CC P23284; Q9NWS8-3: RMND1; NbExp=3; IntAct=EBI-359252, EBI-25884400;
CC P23284; O43765: SGTA; NbExp=6; IntAct=EBI-359252, EBI-347996;
CC P23284; Q96EQ0: SGTB; NbExp=4; IntAct=EBI-359252, EBI-744081;
CC P23284; Q13586: STIM1; NbExp=3; IntAct=EBI-359252, EBI-448878;
CC P23284; Q13061-2: TRDN; NbExp=3; IntAct=EBI-359252, EBI-17257686;
CC P23284; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-359252, EBI-741480;
CC P23284; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-359252, EBI-10173939;
CC P23284; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-359252, EBI-947187;
CC P23284; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-359252, EBI-12040603;
CC P23284; A0A087WZY1; NbExp=3; IntAct=EBI-359252, EBI-13387614;
CC P23284; PRO_0000037552 [Q9WMX2]; Xeno; NbExp=7; IntAct=EBI-359252, EBI-9005440;
CC PRO_0000025479; P13667: PDIA4; NbExp=3; IntAct=EBI-8771982, EBI-1054653;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:20147391}.
CC Note=(Microbial infection).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:1530944}. Melanosome {ECO:0000269|PubMed:17081065}.
CC Note=Identified by mass spectrometry in melanosome fractions from stage
CC I to stage IV (PubMed:17081065). {ECO:0000269|PubMed:17081065}.
CC -!- DISEASE: Osteogenesis imperfecta 9 (OI9) [MIM:259440]: A form of
CC osteogenesis imperfecta, a connective tissue disorder characterized by
CC low bone mass, bone fragility and susceptibility to fractures after
CC minimal trauma. Disease severity ranges from very mild forms without
CC fractures to intrauterine fractures and perinatal lethality.
CC Extraskeletal manifestations, which affect a variable number of
CC patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI9 is a severe autosomal recessive form of the disorder.
CC {ECO:0000269|PubMed:19781681, ECO:0000269|PubMed:20089953}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase B
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52150.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ppib/";
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Peptidyl-prolyl cis-trans isomerase B (PPIB);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=PPIB";
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DR EMBL; M63573; AAA36601.1; -; mRNA.
DR EMBL; AK291149; BAF83838.1; -; mRNA.
DR EMBL; CR456829; CAG33110.1; -; mRNA.
DR EMBL; AY962310; AAX44050.1; -; Genomic_DNA.
DR EMBL; AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77669.1; -; Genomic_DNA.
DR EMBL; BC001125; AAH01125.1; -; mRNA.
DR EMBL; BC008848; AAH08848.1; -; mRNA.
DR EMBL; BC020800; AAH20800.1; -; mRNA.
DR EMBL; BC032138; AAH32138.1; -; mRNA.
DR EMBL; M60857; AAA52150.1; ALT_INIT; mRNA.
DR EMBL; M60457; AAA35733.1; -; mRNA.
DR CCDS; CCDS10191.1; -.
DR PIR; A39118; CSHUB.
DR RefSeq; NP_000933.1; NM_000942.4.
DR PDB; 1CYN; X-ray; 1.85 A; A=39-216.
DR PDB; 3ICH; X-ray; 1.20 A; A=34-216.
DR PDB; 3ICI; X-ray; 1.70 A; A/B=34-216.
DR PDBsum; 1CYN; -.
DR PDBsum; 3ICH; -.
DR PDBsum; 3ICI; -.
DR AlphaFoldDB; P23284; -.
DR BMRB; P23284; -.
DR SMR; P23284; -.
DR BioGRID; 111475; 279.
DR IntAct; P23284; 119.
DR MINT; P23284; -.
DR STRING; 9606.ENSP00000300026; -.
DR BindingDB; P23284; -.
DR ChEMBL; CHEMBL2075; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB00172; Proline.
DR DrugCentral; P23284; -.
DR GlyConnect; 2943; 1 N-Linked glycan (1 site).
DR GlyGen; P23284; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P23284; -.
DR MetOSite; P23284; -.
DR PhosphoSitePlus; P23284; -.
DR SwissPalm; P23284; -.
DR BioMuta; PPIB; -.
DR DMDM; 215273869; -.
DR OGP; P23284; -.
DR REPRODUCTION-2DPAGE; IPI00646304; -.
DR SWISS-2DPAGE; P23284; -.
DR EPD; P23284; -.
DR jPOST; P23284; -.
DR MassIVE; P23284; -.
DR MaxQB; P23284; -.
DR PaxDb; P23284; -.
DR PeptideAtlas; P23284; -.
DR PRIDE; P23284; -.
DR ProteomicsDB; 54078; -.
DR TopDownProteomics; P23284; -.
DR Antibodypedia; 2584; 501 antibodies from 33 providers.
DR DNASU; 5479; -.
DR Ensembl; ENST00000300026.4; ENSP00000300026.4; ENSG00000166794.6.
DR GeneID; 5479; -.
DR KEGG; hsa:5479; -.
DR MANE-Select; ENST00000300026.4; ENSP00000300026.4; NM_000942.5; NP_000933.1.
DR UCSC; uc002and.4; human.
DR CTD; 5479; -.
DR DisGeNET; 5479; -.
DR GeneCards; PPIB; -.
DR HGNC; HGNC:9255; PPIB.
DR HPA; ENSG00000166794; Low tissue specificity.
DR MalaCards; PPIB; -.
DR MIM; 123841; gene.
DR MIM; 259440; phenotype.
DR neXtProt; NX_P23284; -.
DR OpenTargets; ENSG00000166794; -.
DR Orphanet; 216804; Osteogenesis imperfecta type 2.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA33580; -.
DR VEuPathDB; HostDB:ENSG00000166794; -.
DR eggNOG; KOG0880; Eukaryota.
DR GeneTree; ENSGT00940000158007; -.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; P23284; -.
DR OMA; GEGYPGS; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; P23284; -.
DR TreeFam; TF354259; -.
DR BioCyc; MetaCyc:HS09452-MON; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; P23284; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; P23284; -.
DR BioGRID-ORCS; 5479; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; PPIB; human.
DR EvolutionaryTrace; P23284; -.
DR GeneWiki; PPIB; -.
DR GenomeRNAi; 5479; -.
DR Pharos; P23284; Tchem.
DR PRO; PR:P23284; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P23284; protein.
DR Bgee; ENSG00000166794; Expressed in stromal cell of endometrium and 211 other tissues.
DR Genevisible; P23284; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0032991; C:protein-containing complex; ISS:CAFA.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016018; F:cyclosporin A binding; IDA: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:0070063; F:RNA polymerase binding; IPI:AgBase.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
DR GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; 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:0050821; P:protein stabilization; IMP:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 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; Direct protein sequencing; Disease variant;
KW Dwarfism; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Osteogenesis imperfecta; Reference proteome; Rotamase; S-nitrosylation;
KW Signal; Virion.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:2000394"
FT CHAIN 34..216
FT /note="Peptidyl-prolyl cis-trans isomerase B"
FT /id="PRO_0000025479"
FT DOMAIN 47..204
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOTIF 213..216
FT /note="Prevents secretion from ER"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 202
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR7"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P24369"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 9
FT /note="M -> R (in OI9; patients have white sclerae, normal
FT dentition, no rhizomelia or severe deformity of long bones;
FT dbSNP:rs137853864)"
FT /evidence="ECO:0000269|PubMed:20089953"
FT /id="VAR_063436"
FT VARIANT 60
FT /note="V -> L (in dbSNP:rs11558595)"
FT /id="VAR_047711"
FT MUTAGEN 129
FT /note="K->A: Impairs interaction with CLGN and CANX."
FT /evidence="ECO:0000269|PubMed:20801878"
FT CONFLICT 5
FT /note="S -> R (in Ref. 8; AAA52150)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="E -> D (in Ref. 3; CAG33110)"
FT /evidence="ECO:0000305"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:3ICH"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:3ICH"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:3ICH"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3ICH"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3ICH"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1CYN"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3ICH"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3ICH"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3ICH"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3ICH"
FT STRAND 197..212
FT /evidence="ECO:0007829|PDB:3ICH"
SQ SEQUENCE 216 AA; 23743 MW; 2D0410A07AA9E420 CRC64;
MLRLSERNMK VLLAAALIAG SVFFLLLPGP SAADEKKKGP KVTVKVYFDL RIGDEDVGRV
IFGLFGKTVP KTVDNFVALA TGEKGFGYKN SKFHRVIKDF MIQGGDFTRG DGTGGKSIYG
ERFPDENFKL KHYGPGWVSM ANAGKDTNGS QFFITTVKTA WLDGKHVVFG KVLEGMEVVR
KVESTKTDSR DKPLKDVIIA DCGKIEVEKP FAIAKE
