ID   ANXA8_PANTR             Reviewed;         327 AA.
AC   A5A6L7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Annexin A8;
DE   AltName: Full=Annexin-8;
GN   Name=ANXA8;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
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; AB222145; BAF62390.1; -; mRNA.
DR   RefSeq; NP_001092012.1; NM_001098542.1.
DR   AlphaFoldDB; A5A6L7; -.
DR   SMR; A5A6L7; -.
DR   STRING; 9598.ENSPTRP00000058077; -.
DR   PaxDb; A5A6L7; -.
DR   GeneID; 450881; -.
DR   CTD; 728113; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   InParanoid; A5A6L7; -.
DR   Proteomes; UP000002277; Unplaced.
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_0000295283"
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;  36904 MW;  E29829F3894594BE CRC64;
     MAWWKAWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA
     KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKSLG TKEGVIIEIL
     ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL
     QDAHDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL
     EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG
     KTLSSMIMED TSGDYKNALL SLVGSDP