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Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CBP-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha)

 ANXA5_BOVIN             Reviewed;         321 AA.
P81287; Q3ZCH7; Q5E9B9;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 114.
RecName: Full=Annexin A5;
AltName: Full=Anchorin CII;
AltName: Full=Annexin V;
AltName: Full=Annexin-5;
AltName: Full=Calphobindin I;
Short=CBP-I;
AltName: Full=Endonexin II;
AltName: Full=Lipocortin V;
AltName: Full=Placental anticoagulant protein 4;
AltName: Full=Placental anticoagulant protein I;
Short=PAP-I;
AltName: Full=Thromboplastin inhibitor;
AltName: Full=Vascular anticoagulant-alpha;
Short=VAC-alpha;
Name=ANXA5; Synonyms=ANX5;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-37 AND
LYS-126.
STRAIN=Hereford; TISSUE=Mammary gland;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-321, ACETYLATION AT ALA-2, AND VARIANTS SER-37
AND LYS-126.
TISSUE=Brain;
PubMed=1420335; DOI=10.1016/0167-4838(92)90040-K;
Learmonth M.P., Howell S.A., Harris A.C.M., Amess B., Patel Y.,
Giambanco I., Bianchi R., Pula G., Ceccarelli P., Donato R.,
Green B.N., Aitken A.;
"Novel isoforms of CaBP 33/37 (annexin V) from mammalian brain:
structural and phosphorylation differences that suggest distinct
biological roles.";
Biochim. Biophys. Acta 1160:76-83(1992).
-!- FUNCTION: This protein is an anticoagulant protein that acts as an
indirect inhibitor of the thromboplastin-specific complex, which
is involved in the blood coagulation cascade.
-!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity).
{ECO:0000250}.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000250|UniProtKB:P08758}.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BT021001; AAX09018.1; -; mRNA.
EMBL; BC102235; AAI02236.1; -; mRNA.
PIR; S27214; S27214.
UniGene; Bt.49277; -.
ProteinModelPortal; P81287; -.
SMR; P81287; -.
IntAct; P81287; 1.
STRING; 9913.ENSBTAP00000028988; -.
iPTMnet; P81287; -.
PaxDb; P81287; -.
PeptideAtlas; P81287; -.
PRIDE; P81287; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P81287; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0016021; C:integral component of membrane; IDA:AgBase.
GO; GO:0005622; C:intracellular; ISS:AgBase.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
GO; GO:0008201; F:heparin binding; IDA:AgBase.
GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
GO; GO:0051283; P:negative regulation of sequestering of calcium ion; IDA:AgBase.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR002392; ANX5.
PANTHER; PTHR10502:SF26; PTHR10502:SF26; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00201; ANNEXINV.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
Acetylation; Annexin; Blood coagulation; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Hemostasis; Isopeptide bond; Polymorphism;
Reference proteome; Repeat; S-nitrosylation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1420335}.
CHAIN 2 321 Annexin A5.
/FTId=PRO_0000067486.
REPEAT 24 84 Annexin 1.
REPEAT 96 156 Annexin 2.
REPEAT 180 240 Annexin 3.
REPEAT 255 315 Annexin 4.
MOTIF 314 320 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:1420335}.
MOD_RES 70 70 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 79 79 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 101 101 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08758}.
MOD_RES 290 290 N6-succinyllysine.
{ECO:0000250|UniProtKB:P48036}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P08758}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08758}.
VARIANT 37 37 T -> S. {ECO:0000269|PubMed:1420335,
ECO:0000269|Ref.2}.
VARIANT 126 126 E -> K. {ECO:0000269|PubMed:1420335,
ECO:0000269|Ref.2}.
CONFLICT 135 135 S -> T (in Ref. 2; AAI02236).
{ECO:0000305}.
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


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E0259h ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant 96T
U0259h CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prote 96T
E0259h ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prot 96T
U0259r CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattus norv 96T
E0259b ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
U0259b CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,T 96T
E0259m ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I 96T
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