ANXA5_MOUSE
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 03-AUG-2022, entry version 171.
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, Pancreas,
RC 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; 9.
DR IntAct; P48036; 6.
DR MINT; P48036; -.
DR STRING; 10090.ENSMUSP00000029266; -.
DR iPTMnet; P48036; -.
DR PhosphoSitePlus; P48036; -.
DR SwissPalm; P48036; -.
DR COMPLUYEAST-2DPAGE; P48036; -.
DR REPRODUCTION-2DPAGE; IPI00317309; -.
DR SWISS-2DPAGE; P48036; -.
DR CPTAC; non-CPTAC-3687; -.
DR CPTAC; non-CPTAC-4015; -.
DR EPD; P48036; -.
DR jPOST; P48036; -.
DR MaxQB; P48036; -.
DR PaxDb; P48036; -.
DR PeptideAtlas; P48036; -.
DR PRIDE; P48036; -.
DR ProteomicsDB; 282128; -.
DR TopDownProteomics; P48036; -.
DR Antibodypedia; 3290; 788 antibodies from 43 providers.
DR DNASU; 11747; -.
DR Ensembl; ENSMUST00000029266; ENSMUSP00000029266; ENSMUSG00000027712.
DR GeneID; 11747; -.
DR KEGG; mmu:11747; -.
DR UCSC; uc008ozj.2; mouse.
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; KVKAIWA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P48036; -.
DR TreeFam; TF105452; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 11747; 3 hits in 72 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 268 other tissues.
DR ExpressionAtlas; P48036; baseline and differential.
DR Genevisible; P48036; MM.
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; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; 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: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; -; 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 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
