ANXA5_HUMAN
ID ANXA5_HUMAN Reviewed; 320 AA.
AC P08758; D3DNW7; Q6FHB3; Q6FI16; Q8WV69; Q9UDH9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Annexin A5;
DE AltName: Full=Anchorin CII;
DE AltName: Full=Annexin V;
DE AltName: Full=Annexin-5;
DE AltName: Full=Calphobindin I;
DE Short=CPB-I;
DE AltName: Full=Endonexin II;
DE AltName: Full=Lipocortin V;
DE AltName: Full=Placental anticoagulant protein 4;
DE Short=PP4;
DE AltName: Full=Placental anticoagulant protein I;
DE Short=PAP-I;
DE AltName: Full=Thromboplastin inhibitor;
DE AltName: Full=Vascular anticoagulant-alpha;
DE Short=VAC-alpha;
GN Name=ANXA5; Synonyms=ANX5, ENX2, PP4;
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=2964863; DOI=10.1021/bi00399a011;
RA Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.;
RT "Primary structure of human placental anticoagulant protein.";
RL Biochemistry 26:8087-8092(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-320.
RX PubMed=2963810; DOI=10.1093/oxfordjournals.jbchem.a122165;
RA Iwasaki A., Suda M., Nakao H., Nagoya T., Saino Y., Arai K., Mizoguchi T.,
RA Sato F., Yoshizaki H., Hirata M., Miyata T., Shidara Y., Murata M.,
RA Maki M.;
RT "Structure and expression of cDNA for an inhibitor of blood coagulation
RT isolated from human placenta: a new lipocortin-like protein.";
RL J. Biochem. 102:1261-1273(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2455636; DOI=10.1111/j.1432-1033.1988.tb14139.x;
RA Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G., Stratowa C.,
RA Hauptmann R.;
RT "Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-
RT dependent phospholipid-binding protein.";
RL Eur. J. Biochem. 174:585-592(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2967291; DOI=10.1016/s0021-9258(18)68438-8;
RA Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T.;
RT "Cloning and expression of cDNA for human endonexin II, a Ca2+ and
RT phospholipid binding protein.";
RL J. Biol. Chem. 263:8037-8043(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2968983; DOI=10.1016/s0021-9258(18)38041-4;
RA Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
RA Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
RA Hession C., Frey A.Z., Wallner B.P.;
RT "Five distinct calcium and phospholipid binding proteins share homology
RT with lipocortin I.";
RL J. Biol. Chem. 263:10799-10811(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2967495; DOI=10.1073/pnas.85.11.3708;
RA Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F.,
RA Kuepper H.;
RT "Characterization of cDNA encoding human placental anticoagulant protein
RT (PP4): homology with the lipocortin family.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=7958998; DOI=10.1016/0378-1119(94)90157-0;
RA Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T.;
RT "The gene encoding human annexin V has a TATA-less promoter with a high G+C
RT content.";
RL Gene 149:253-260(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8034319; DOI=10.1006/geno.1994.1201;
RA Cookson B.T., Engelhardt S., Smith C., Bamford H.A., Prochazka M.,
RA Tait J.F.;
RT "Organization of the human annexin V (ANX5) gene.";
RL Genomics 20:463-467(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [12]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, Ovary, 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 [14]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2532007; DOI=10.1042/bj2630929;
RA Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H.,
RA Cavadore J.-C., Conard J., Russo-Marie F., Lederer F.;
RT "A 32 kDa lipocortin from human mononuclear cells appears to be identical
RT with the placental inhibitor of blood coagulation.";
RL Biochem. J. 263:929-935(1989).
RN [15]
RP PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
RL Submitted (JAN-2005) to UniProtKB.
RN [16]
RP PROTEIN SEQUENCE OF 21-31; 93-108; 176-188 AND 304-319, AND INTERACTION
RP WITH HBV.
RX PubMed=8249278; DOI=10.1006/viro.1993.1628;
RA Hertogs K., Leenders W.P., Depla E., De Bruin W.C., Meheus L.,
RA Raymackers J., Moshage H., Yap S.H.;
RT "Endonexin II, present on human liver plasma membranes, is a specific
RT binding protein of small hepatitis B virus (HBV) envelope protein.";
RL Virology 197:549-557(1993).
RN [17]
RP PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
RX PubMed=2957692; DOI=10.1073/pnas.84.17.6078;
RA Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T.;
RT "Structural and functional characterization of endonexin II, a calcium- and
RT phospholipid-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987).
RN [18]
RP PROTEIN SEQUENCE OF 85-93.
RC TISSUE=Placenta;
RX PubMed=2974032; DOI=10.1016/s0021-9258(18)37335-6;
RA Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
RA de Haen C.;
RT "Sedimentation equilibrium analysis of five lipocortin-related
RT phospholipase A2 inhibitors from human placenta. Evidence against a
RT mechanistically relevant association between enzyme and inhibitor.";
RL J. Biol. Chem. 263:18657-18663(1988).
RN [19]
RP PROTEIN SEQUENCE OF 152-161 AND 246-260.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y.,
RA Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by a
RT proteomics survey.";
RL Mol. Cell 23:607-618(2006).
RN [21]
RP INVOLVEMENT IN RPRGL3.
RX PubMed=17339269; DOI=10.1093/hmg/ddm017;
RA Bogdanova N., Horst J., Chlystun M., Croucher P.J., Nebel A., Bohring A.,
RA Todorova A., Schreiber S., Gerke V., Krawczak M., Markoff A.;
RT "A common haplotype of the annexin A5 (ANXA5) gene promoter is associated
RT with recurrent pregnancy loss.";
RL Hum. Mol. Genet. 16:573-578(2007).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-79 AND LYS-97,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 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 [25]
RP S-NITROSYLATION, AND DOMAIN.
RX PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
RA Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L., Fox P.L.;
RT "Target-selective protein S-nitrosylation by sequence motif recognition.";
RL Cell 159:623-634(2014).
RN [26]
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 [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [29]
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 [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP 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 [31]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=2147412; DOI=10.1002/j.1460-2075.1990.tb07605.x;
RA Huber R., Roemisch J., Paques E.-P.;
RT "The crystal and molecular structure of human annexin V, an anticoagulant
RT protein that binds to calcium and membranes.";
RL EMBO J. 9:3867-3874(1990).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2148156; DOI=10.1016/0014-5793(90)81428-q;
RA Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P.;
RT "The calcium binding sites in human annexin V by crystal structure analysis
RT at 2.0-A resolution. Implications for membrane binding and calcium channel
RT activity.";
RL FEBS Lett. 275:15-21(1990).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1311770; DOI=10.1016/0022-2836(92)90984-r;
RA Huber R., Berendes R., Burger A., Schneider M., Karshikov A., Luecke H.,
RA Roemisch J., Paques E.-P.;
RT "Crystal and molecular structure of human annexin V after refinement.
RT Implications for structure, membrane binding and ion channel formation of
RT the annexin family of proteins.";
RL J. Mol. Biol. 223:683-704(1992).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9398511; DOI=10.1006/jmbi.1997.1375;
RA Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M.;
RT "Crystal structure of annexin V with its ligand K-201 as a calcium channel
RT activity inhibitor.";
RL J. Mol. Biol. 274:16-20(1997).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9435213; DOI=10.1073/pnas.95.2.455;
RA Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L.;
RT "Residue-specific bioincorporation of non-natural, biologically active
RT amino acids into proteins as possible drug carriers: structure and
RT stability of the per-thiaproline mutant of annexin V.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998).
CC -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC indirect inhibitor of the thromboplastin-specific complex, which is
CC involved in the blood coagulation cascade.
CC -!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity). Interacts with
CC hepatitis B virus (HBV). {ECO:0000250, ECO:0000269|PubMed:8249278}.
CC -!- INTERACTION:
CC P08758; O15499: GSC2; NbExp=3; IntAct=EBI-296601, EBI-19954058;
CC P08758; P04792: HSPB1; NbExp=3; IntAct=EBI-296601, EBI-352682;
CC P08758; Q96CV9: OPTN; NbExp=3; IntAct=EBI-296601, EBI-748974;
CC P08758; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-296601, EBI-717399;
CC P08758; O76024: WFS1; NbExp=3; IntAct=EBI-296601, EBI-720609;
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
CC -!- DISEASE: Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: A common
CC complication of pregnancy, resulting in spontaneous abortion before the
CC fetus has reached viability. The term includes all miscarriages from
CC the time of conception until 24 weeks of gestation. Recurrent pregnancy
CC loss is defined as 3 or more consecutive spontaneous abortions.
CC {ECO:0000269|PubMed:17339269}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18366; AAA35570.1; -; mRNA.
DR EMBL; D00172; BAA00122.1; -; mRNA.
DR EMBL; X12454; CAA30985.1; -; mRNA.
DR EMBL; J03745; AAA52386.1; -; mRNA.
DR EMBL; M21731; AAA36166.1; -; mRNA.
DR EMBL; M19384; AAB59545.1; -; mRNA.
DR EMBL; U01691; AAB40047.1; -; Genomic_DNA.
DR EMBL; U01681; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01682; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01683; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01685; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01686; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01687; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01689; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U01690; AAB40047.1; JOINED; Genomic_DNA.
DR EMBL; U05770; AAB60648.1; -; Genomic_DNA.
DR EMBL; U05760; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05761; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05762; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05764; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05765; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05766; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05767; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05768; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; U05769; AAB60648.1; JOINED; Genomic_DNA.
DR EMBL; AK312644; BAG35528.1; -; mRNA.
DR EMBL; CR536522; CAG38759.1; -; mRNA.
DR EMBL; CR541842; CAG46640.1; -; mRNA.
DR EMBL; AC096730; AAY40954.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05257.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05258.1; -; Genomic_DNA.
DR EMBL; BC001429; AAH01429.1; -; mRNA.
DR EMBL; BC004993; AAH04993.1; -; mRNA.
DR EMBL; BC012804; AAH12804.1; -; mRNA.
DR EMBL; BC012822; AAH12822.1; -; mRNA.
DR EMBL; BC018671; AAH18671.1; -; mRNA.
DR CCDS; CCDS3720.1; -.
DR PIR; D29250; AQHUP.
DR RefSeq; NP_001145.1; NM_001154.3.
DR PDB; 1ANW; X-ray; 2.40 A; A/B=2-320.
DR PDB; 1ANX; X-ray; 1.90 A; A/B/C=2-320.
DR PDB; 1AVH; X-ray; 2.30 A; A/B=1-320.
DR PDB; 1AVR; X-ray; 2.30 A; A=1-320.
DR PDB; 1HAK; X-ray; 3.00 A; A/B=1-320.
DR PDB; 1HVD; X-ray; 2.00 A; A=2-320.
DR PDB; 1HVE; X-ray; 2.30 A; A=2-320.
DR PDB; 1HVF; X-ray; 2.00 A; A=2-320.
DR PDB; 1HVG; X-ray; 3.00 A; A=2-320.
DR PDB; 1SAV; X-ray; 2.50 A; A=1-320.
DR PDB; 2XO2; X-ray; 2.80 A; A=1-320.
DR PDB; 2XO3; X-ray; 2.30 A; A=1-320.
DR PDB; 6K22; X-ray; 2.75 A; A=2-320.
DR PDB; 6K25; X-ray; 2.40 A; A=2-320.
DR PDBsum; 1ANW; -.
DR PDBsum; 1ANX; -.
DR PDBsum; 1AVH; -.
DR PDBsum; 1AVR; -.
DR PDBsum; 1HAK; -.
DR PDBsum; 1HVD; -.
DR PDBsum; 1HVE; -.
DR PDBsum; 1HVF; -.
DR PDBsum; 1HVG; -.
DR PDBsum; 1SAV; -.
DR PDBsum; 2XO2; -.
DR PDBsum; 2XO3; -.
DR PDBsum; 6K22; -.
DR PDBsum; 6K25; -.
DR AlphaFoldDB; P08758; -.
DR SMR; P08758; -.
DR BioGRID; 106805; 164.
DR IntAct; P08758; 52.
DR MINT; P08758; -.
DR STRING; 9606.ENSP00000296511; -.
DR DrugBank; DB03981; 1,4-Dideoxy-5-Dehydro-O2-Sulfo-Glucuronic Acid.
DR DrugBank; DB03935; 1,4-Dideoxy-O2-Sulfo-Glucuronic Acid.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00591; Fluocinolone acetonide.
DR DrugBank; DB02929; K201 free base.
DR DrugBank; DB02497; L-Alpha-Glycerophosphorylserine.
DR DrugBank; DB02846; L-thioproline.
DR DrugBank; DB03959; N,O6-Disulfo-Glucosamine.
DR DrugBank; DB03484; sn-glycero-3-phosphoethanolamine.
DR TCDB; 1.A.31.1.7; the annexin (annexin) family.
DR iPTMnet; P08758; -.
DR MetOSite; P08758; -.
DR PhosphoSitePlus; P08758; -.
DR SwissPalm; P08758; -.
DR BioMuta; ANXA5; -.
DR DMDM; 113960; -.
DR OGP; P08758; -.
DR REPRODUCTION-2DPAGE; IPI00329801; -.
DR REPRODUCTION-2DPAGE; P08758; -.
DR EPD; P08758; -.
DR jPOST; P08758; -.
DR MassIVE; P08758; -.
DR PaxDb; P08758; -.
DR PeptideAtlas; P08758; -.
DR PRIDE; P08758; -.
DR ProteomicsDB; 52165; -.
DR TopDownProteomics; P08758; -.
DR Antibodypedia; 3290; 788 antibodies from 43 providers.
DR DNASU; 308; -.
DR Ensembl; ENST00000296511.10; ENSP00000296511.5; ENSG00000164111.15.
DR GeneID; 308; -.
DR KEGG; hsa:308; -.
DR MANE-Select; ENST00000296511.10; ENSP00000296511.5; NM_001154.4; NP_001145.1.
DR CTD; 308; -.
DR DisGeNET; 308; -.
DR GeneCards; ANXA5; -.
DR HGNC; HGNC:543; ANXA5.
DR HPA; ENSG00000164111; Low tissue specificity.
DR MalaCards; ANXA5; -.
DR MIM; 131230; gene.
DR MIM; 614391; phenotype.
DR neXtProt; NX_P08758; -.
DR OpenTargets; ENSG00000164111; -.
DR PharmGKB; PA24833; -.
DR VEuPathDB; HostDB:ENSG00000164111; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000155988; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; P08758; -.
DR OMA; KVKAIWA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P08758; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P08758; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P08758; -.
DR BioGRID-ORCS; 308; 12 hits in 1086 CRISPR screens.
DR ChiTaRS; ANXA5; human.
DR EvolutionaryTrace; P08758; -.
DR GeneWiki; Annexin_A5; -.
DR GenomeRNAi; 308; -.
DR Pharos; P08758; Tbio.
DR PRO; PR:P08758; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P08758; protein.
DR Bgee; ENSG00000164111; Expressed in stromal cell of endometrium and 209 other tissues.
DR ExpressionAtlas; P08758; baseline and differential.
DR Genevisible; P08758; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072563; C:endothelial microparticle; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
DR GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002392; ANX5.
DR PANTHER; PTHR10502:SF26; PTHR10502:SF26; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00201; ANNEXINV.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Annexin; Blood coagulation; Calcium;
KW Calcium/phospholipid-binding; Direct protein sequencing; Hemostasis;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW S-nitrosylation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2963810,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..320
FT /note="Annexin A5"
FT /id="PRO_0000067487"
FT REPEAT 15..86
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 87..158
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 170..242
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 246..317
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOTIF 314..319
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000305|PubMed:25417112"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48036"
FT MOD_RES 70
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 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:16916647"
FT MOD_RES 290
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48036"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CONFLICT 135
FT /note="S -> L (in Ref. 10; CAG38759)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="I -> T (in Ref. 13; AAH18671)"
FT /evidence="ECO:0000305"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:1ANX"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 47..61
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1ANX"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1ANX"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1ANX"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1ANX"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:1ANX"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:1ANX"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6K25"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:1ANX"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:1ANX"
SQ SEQUENCE 320 AA; 35937 MW; 45E14E3964BA4D1A CRC64;
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE
ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF
QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI
KGDTSGDYKK ALLLLCGEDD
