ID   ANXA8_RAT               Reviewed;         327 AA.
AC   Q4FZU6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Annexin A8;
DE   AltName: Full=Annexin VIII;
DE   AltName: Full=Annexin-8;
GN   Name=Anxa8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-56; 101-107 AND 234-249, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
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.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC099106; AAH99106.1; -; mRNA.
DR   RefSeq; NP_001026824.1; NM_001031654.1.
DR   AlphaFoldDB; Q4FZU6; -.
DR   SMR; Q4FZU6; -.
DR   STRING; 10116.ENSRNOP00000027464; -.
DR   iPTMnet; Q4FZU6; -.
DR   PhosphoSitePlus; Q4FZU6; -.
DR   PaxDb; Q4FZU6; -.
DR   PRIDE; Q4FZU6; -.
DR   Ensembl; ENSRNOT00000082186; ENSRNOP00000069969; ENSRNOG00000060949.
DR   GeneID; 306283; -.
DR   KEGG; rno:306283; -.
DR   UCSC; RGD:1307719; rat.
DR   CTD; 653145; -.
DR   RGD; 1307719; Anxa8.
DR   eggNOG; KOG0819; Eukaryota.
DR   GeneTree; ENSGT00940000161044; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   InParanoid; Q4FZU6; -.
DR   OMA; RCTRNIR; -.
DR   OrthoDB; 856254at2759; -.
DR   PhylomeDB; Q4FZU6; -.
DR   TreeFam; TF105452; -.
DR   PRO; PR:Q4FZU6; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000060949; Expressed in lung and 15 other tissues.
DR   Genevisible; Q4FZU6; RN.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0031902; C:late endosome membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:RGD.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:RGD.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:RGD.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:RGD.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0016197; P:endosomal transport; ISO:RGD.
DR   GO; GO:0007032; P:endosome organization; ISO:RGD.
DR   GO; GO:1900138; P:negative regulation of phospholipase A2 activity; ISO:RGD.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; ISO:RGD.
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   1: Evidence at protein level;
KW   Annexin; Blood coagulation; Calcium; Calcium/phospholipid-binding;
KW   Direct protein sequencing; Hemostasis; Metal-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..327
FT                   /note="Annexin A8"
FT                   /id="PRO_0000277887"
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;  36706 MW;  9E999F1D872A00E2 CRC64;
     MAWWKAWVEQ EGVSVKGSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNVQRQQIA
     KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL
     ASRTKNQLRE IMKAYEEDYG STLEEDIQGD TSGYLERILV CLLQGCRDDV SGFVDPGLAL
     QDAQDLHAAG EKILGTDEMK FITILCTRSA THLMRVFEEY EKIANKSIED SIKSETHGSL
     EEAMLTVVKC TRNVHSYFAE RLYYAMKGAG TLDGTLIRNI VSRSEIDLNL IKSQFQKMYG
     KTLSSMIMGD TSGYYKTALL NLVGTDL