ANXA8_RABIT
ID ANXA8_RABIT Reviewed; 327 AA.
AC O97529;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Annexin A8;
DE AltName: Full=Annexin VIII;
DE AltName: Full=Annexin-8;
GN Name=ANXA8;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng W., Tsao F.H.C.;
RL Submitted (JUL-1997) 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; AF012745; AAD01508.1; -; mRNA.
DR RefSeq; NP_001075488.1; NM_001082019.1.
DR AlphaFoldDB; O97529; -.
DR SMR; O97529; -.
DR STRING; 9986.ENSOCUP00000012199; -.
DR GeneID; 100008655; -.
DR KEGG; ocu:100008655; -.
DR CTD; 653145; -.
DR eggNOG; KOG0819; Eukaryota.
DR InParanoid; O97529; -.
DR OrthoDB; 856254at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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_0000231029"
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; 36680 MW; 1815B77B6BE50AB7 CRC64;
MAWWKAWVEQ EGVTVKGSPH FNPVPDAETL YKAMKGIGTN EQAIIDVLTR RSSAQRQQIA
KSFKAQFGSD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL
ASRTKNQLQE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV TGFVDPGLAL
QDAQDLYAAG EKICGTDEMK FITILCTRSA RHLMRVFEEY EKIANKSIED SIKSETHGSL
EEAMLTIVKC TRNLHCYFAE RLHYAMKGAG TLDGTLIRNI VSRSEIDLNL IKGHYKKMYG
KTLSSMIMED TSGDYKNALL SLVGSDP