ID   ANXA5_MOUSE             Reviewed;         319 AA.
AC   P48036; Q3U5Q1; Q3U5X4; Q3U8K1; Q3UGV0; Q99LA1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 180.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Peritoneal cavity;
RX   PubMed=8824796; DOI=10.1006/geno.1996.0026;
RA   Rodriguez-Garcia M.I., Kozak C.A., Morgan R.O., Fernandez M.-P.;
RT   "Mouse annexin V chromosomal localization, cDNA sequence conservation, and
RT   molecular evolution.";
RL   Genomics 31:151-157(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Adachi T., Kojima K., Fukuoka S., Ogawa H., Matsumoto I.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   PubMed=9854034; DOI=10.1042/bj3370125;
RA   Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.R., Bances P.,
RA   Fernandez M.-P.;
RT   "Mouse annexin V genomic organization includes an endogenous retrovirus.";
RL   Biochem. J. 337:125-131(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [6]
RP   PROTEIN SEQUENCE OF 28-43; 62-74; 116-124; 192-199; 226-240 AND 275-283,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68 AND LYS-95, SUCCINYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-288, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P48036; Q08460: Kcnma1; NbExp=4; IntAct=EBI-1184119, EBI-1633915;
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
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:0000250|UniProtKB:P08758}.
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:0000250|UniProtKB:P08758}.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; U29396; AAC52530.1; -; mRNA.
DR   EMBL; D63423; BAA09728.1; -; mRNA.
DR   EMBL; AJ230108; CAA13092.1; -; Genomic_DNA.
DR   EMBL; AJ230110; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230111; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230114; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230116; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230118; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230119; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230120; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230121; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230122; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230123; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AJ230124; CAA13092.1; JOINED; Genomic_DNA.
DR   EMBL; AK147740; BAE28107.1; -; mRNA.
DR   EMBL; AK152185; BAE31016.1; -; mRNA.
DR   EMBL; AK153388; BAE31952.1; -; mRNA.
DR   EMBL; AK153476; BAE32026.1; -; mRNA.
DR   EMBL; BC003716; AAH03716.1; -; mRNA.
DR   CCDS; CCDS38416.1; -.
DR   RefSeq; NP_033803.1; NM_009673.2.
DR   AlphaFoldDB; P48036; -.
DR   SMR; P48036; -.
DR   BioGRID; 198111; 11.
DR   IntAct; P48036; 6.
DR   MINT; P48036; -.
DR   STRING; 10090.ENSMUSP00000029266; -.
DR   GlyGen; P48036; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P48036; -.
DR   MetOSite; P48036; -.
DR   PhosphoSitePlus; P48036; -.
DR   SwissPalm; P48036; -.
DR   REPRODUCTION-2DPAGE; IPI00317309; -.
DR   CPTAC; non-CPTAC-3687; -.
DR   CPTAC; non-CPTAC-4015; -.
DR   EPD; P48036; -.
DR   jPOST; P48036; -.
DR   MaxQB; P48036; -.
DR   PaxDb; 10090-ENSMUSP00000029266; -.
DR   PeptideAtlas; P48036; -.
DR   ProteomicsDB; 282128; -.
DR   TopDownProteomics; P48036; -.
DR   Antibodypedia; 3290; 895 antibodies from 43 providers.
DR   DNASU; 11747; -.
DR   Ensembl; ENSMUST00000029266.14; ENSMUSP00000029266.9; ENSMUSG00000027712.14.
DR   GeneID; 11747; -.
DR   KEGG; mmu:11747; -.
DR   UCSC; uc008ozj.2; mouse.
DR   AGR; MGI:106008; -.
DR   CTD; 308; -.
DR   MGI; MGI:106008; Anxa5.
DR   VEuPathDB; HostDB:ENSMUSG00000027712; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000155988; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; P48036; -.
DR   OMA; LQGNRDP; -.
DR   OrthoDB; 1500773at2759; -.
DR   PhylomeDB; P48036; -.
DR   TreeFam; TF105452; -.
DR   Reactome; R-MMU-114608; Platelet degranulation.
DR   BioGRID-ORCS; 11747; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Anxa5; mouse.
DR   PRO; PR:P48036; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P48036; Protein.
DR   Bgee; ENSMUSG00000027712; Expressed in utricle of membranous labyrinth and 271 other cell types or tissues.
DR   ExpressionAtlas; P48036; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0042995; C:cell projection; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0072563; C:endothelial microparticle; IDA:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005388; F:P-type calcium transporter activity; ISO:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR   GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0097211; P:cellular response to gonadotropin-releasing hormone; ISO:MGI.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; ISO:MGI.
DR   GO; GO:1902721; P:negative regulation of prolactin secretion; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1901317; P:regulation of flagellated sperm motility; ISO:MGI.
DR   GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR   GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR   Gene3D; 1.10.220.10; Annexin; 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; ANNEXIN; 1.
DR   PANTHER; PTHR10502:SF26; ANNEXIN A5; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00201; ANNEXINV.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; Annexin; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
DR   COMPLUYEAST-2DPAGE; P48036; -.
DR   SWISS-2DPAGE; P48036; -.
DR   Genevisible; P48036; MM.
PE   1: Evidence at protein level;
KW   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:0000250|UniProtKB:P14668"
FT   CHAIN           2..319
FT                   /note="Annexin A5"
FT                   /id="PRO_0000067488"
FT   REPEAT          13..84
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          85..156
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          168..240
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          244..315
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   MOTIF           312..318
FT                   /note="[IL]-x-C-x-x-[DE] motif"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P14668"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         74
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   MOD_RES         77
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   MOD_RES         95
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   MOD_RES         288
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08758"
FT   CONFLICT        142
FT                   /note="D -> G (in Ref. 4; BAE28107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="A -> G (in Ref. 5; AAH03716)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="K -> N (in Ref. 4; BAE31952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="G -> S (in Ref. 4; BAE32026)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   319 AA;  35752 MW;  55055BAF2E1C36B7 CRC64;
     MATRGTVTDF PGFDGRADAE VLRKAMKGLG TDEDSILNLL TSRSNAQRQE IAQEFKTLFG
     RDLVDDLKSE LTGKFEKLIV AMMKPSRLYD AYELKHALKG AGTDEKVLTE IIASRTPEEL
     SAIKQVYEEE YGSNLEDDVV GDTSGYYQRM LVVLLQANRD PDTAIDDAQV ELDAQALFQA
     GELKWGTDEE KFITIFGTRS VSHLRRVFDK YMTISGFQIE ETIDRETSGN LEQLLLAVVK
     SIRSIPAYLA ETLYYAMKGA GTDDHTLIRV VVSRSEIDLF NIRKEFRKNF ATSLYSMIKG
     DTSGDYKKAL LLLCGGEDD
//