ID   ANXA8_BOVIN             Reviewed;         327 AA.
AC   Q95L54;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Annexin A8;
DE   AltName: Full=Annexin VIII;
DE   AltName: Full=Annexin-8;
GN   Name=ANXA8;
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 [MRNA].
RA   White A.H., Wallis G.A.;
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; AF417637; AAL13308.1; -; mRNA.
DR   EMBL; BT021645; AAX46492.1; -; mRNA.
DR   EMBL; BT021646; AAX46493.1; -; mRNA.
DR   EMBL; BC113321; AAI13322.1; -; mRNA.
DR   RefSeq; NP_776666.1; NM_174241.2.
DR   RefSeq; XP_005226585.1; XM_005226528.3.
DR   AlphaFoldDB; Q95L54; -.
DR   SMR; Q95L54; -.
DR   STRING; 9913.ENSBTAP00000043804; -.
DR   PaxDb; Q95L54; -.
DR   PeptideAtlas; Q95L54; -.
DR   PRIDE; Q95L54; -.
DR   Ensembl; ENSBTAT00000046510; ENSBTAP00000043804; ENSBTAG00000018499.
DR   GeneID; 281627; -.
DR   KEGG; bta:281627; -.
DR   CTD; 728113; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018499; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000161044; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; Q95L54; -.
DR   OMA; RCTRNIR; -.
DR   OrthoDB; 856254at2759; -.
DR   TreeFam; TF105452; -.
DR   Proteomes; UP000009136; Chromosome 28.
DR   Bgee; ENSBTAG00000018499; Expressed in oviduct epithelium and 98 other tissues.
DR   ExpressionAtlas; Q95L54; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IBA:GO_Central.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IBA:GO_Central.
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; IPR009115; ANX8.
DR   PANTHER; PTHR10502:SF133; PTHR10502:SF133; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR01808; ANNEXINVIII.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   2: Evidence at transcript level;
KW   Annexin; Blood coagulation; Calcium; Calcium/phospholipid-binding;
KW   Hemostasis; Metal-binding; Reference proteome; Repeat.
FT   CHAIN           1..327
FT                   /note="Annexin A8"
FT                   /id="PRO_0000231028"
FT   REPEAT          21..92
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          93..164
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          177..249
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          253..324
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   BINDING         266
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   327 AA;  36787 MW;  2EB178E13738CF22 CRC64;
     MAWWKAWVEQ EGVSVKGSPH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNAQRQQIA
     KSFKAQFGKD LIETLKSELS GKFERLIIAL MYPPYRYEAK ELYDAMKGIG TKEGVIIEIL
     ASRTKNQLQE IMKAYEEDYG SNLEEDIKAD TSGYLERILV CLLQGSRDDL SGYVDPGLAL
     QDAQDLYAAG EKICGTDEMK FITILCTRSA THLMRVFEEY EKIANKSIED SIKSETHGSL
     EEAMLTVVKC TRNLHGYFAE RLYFAMKGAG TLDGTLIRNI VSRSEIDLNL IKNQFKKMYG
     KTLSSMIMED TSGDYKNALL NLVGSDL