ANXA5_BOVIN
ID ANXA5_BOVIN Reviewed; 321 AA.
AC P81287; Q3ZCH7; Q5E9B9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 132.
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 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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-37 AND LYS-126.
RC STRAIN=Hereford; TISSUE=Mammary gland;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-321, ACETYLATION AT ALA-2, AND VARIANTS SER-37 AND
RP LYS-126.
RC TISSUE=Brain;
RX PubMed=1420335; DOI=10.1016/0167-4838(92)90040-k;
RA Learmonth M.P., Howell S.A., Harris A.C.M., Amess B., Patel Y.,
RA Giambanco I., Bianchi R., Pula G., Ceccarelli P., Donato R., Green B.N.,
RA Aitken A.;
RT "Novel isoforms of CaBP 33/37 (annexin V) from mammalian brain: structural
RT and phosphorylation differences that suggest distinct biological roles.";
RL Biochim. Biophys. Acta 1160:76-83(1992).
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 -!- 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; BT021001; AAX09018.1; -; mRNA.
DR EMBL; BC102235; AAI02236.1; -; mRNA.
DR PIR; S27214; S27214.
DR AlphaFoldDB; P81287; -.
DR SMR; P81287; -.
DR IntAct; P81287; 1.
DR STRING; 9913.ENSBTAP00000028988; -.
DR ChEMBL; CHEMBL3308974; -.
DR iPTMnet; P81287; -.
DR PaxDb; P81287; -.
DR PeptideAtlas; P81287; -.
DR PRIDE; P81287; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; P81287; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
DR GO; GO:0005622; C:intracellular anatomical structure; ISS:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IDA:AgBase.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
DR GO; GO:0051283; P:negative regulation of sequestering of calcium ion; IDA:AgBase.
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; Reference proteome; Repeat; S-nitrosylation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1420335"
FT CHAIN 2..321
FT /note="Annexin A5"
FT /id="PRO_0000067486"
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..320
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:0000269|PubMed:1420335"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08758"
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:0000250|UniProtKB:P08758"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08758"
FT VARIANT 37
FT /note="T -> S"
FT /evidence="ECO:0000269|PubMed:1420335, ECO:0000269|Ref.2"
FT VARIANT 126
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:1420335, ECO:0000269|Ref.2"
FT CONFLICT 135
FT /note="S -> T (in Ref. 2; AAI02236)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 36089 MW; 18EC336E6A935251 CRC64;
MAQVLRGTVA DFPGFDERAD AETLRKAMKG LGTDEETILT LLTSRSNAQR QEIAVAFKTL
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTDEKVL TEIIASRTPE
ELRAIEQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDARIDEA QVEQDAQALF
QAGELKWGTD EEKFITIFGT RSVSHLRRVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVVVSRSEID LYNIRKEFRK NFGTSLYSMI
KGDTSGDYKK ALLLLCGGED D
