ANXA8_MOUSE
ID ANXA8_MOUSE Reviewed; 327 AA.
AC O35640; Q8K2N9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Annexin A8;
DE AltName: Full=Annexin VIII;
DE AltName: Full=Annexin-8;
GN Name=Anxa8; Synonyms=Anx8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RX PubMed=9434938; DOI=10.1007/s003359900671;
RA Fernandez M.-P., Copeland N.G., Gilbert D.J., Jenkins N.A., Morgan R.O.;
RT "The genetic origin of mouse annexin VIII.";
RL Mamm. Genome 9:8-14(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AJ002390; CAA05364.1; -; mRNA.
DR EMBL; BC030407; AAH30407.1; -; mRNA.
DR CCDS; CCDS26932.1; -.
DR RefSeq; NP_001268774.1; NM_001281845.1.
DR RefSeq; NP_038501.2; NM_013473.4.
DR AlphaFoldDB; O35640; -.
DR SMR; O35640; -.
DR STRING; 10090.ENSMUSP00000022519; -.
DR iPTMnet; O35640; -.
DR PhosphoSitePlus; O35640; -.
DR MaxQB; O35640; -.
DR PaxDb; O35640; -.
DR PeptideAtlas; O35640; -.
DR PRIDE; O35640; -.
DR ProteomicsDB; 296049; -.
DR DNASU; 11752; -.
DR Ensembl; ENSMUST00000022519; ENSMUSP00000022519; ENSMUSG00000021950.
DR GeneID; 11752; -.
DR KEGG; mmu:11752; -.
DR UCSC; uc007taj.2; mouse.
DR CTD; 653145; -.
DR MGI; MGI:1201374; Anxa8.
DR VEuPathDB; HostDB:ENSMUSG00000021950; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000161044; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; O35640; -.
DR OMA; RCTRNIR; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; O35640; -.
DR TreeFam; TF105452; -.
DR BioGRID-ORCS; 11752; 1 hit in 75 CRISPR screens.
DR PRO; PR:O35640; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35640; protein.
DR Bgee; ENSMUSG00000021950; Expressed in tail skin and 137 other tissues.
DR ExpressionAtlas; O35640; baseline and differential.
DR Genevisible; O35640; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISO:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
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 1: Evidence at protein 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_0000067504"
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"
FT CONFLICT 14
FT /note="S -> T (in Ref. 1; CAA05364)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> L (in Ref. 1; CAA05364)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="N -> D (in Ref. 1; CAA05364)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="I -> F (in Ref. 1; CAA05364)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="K -> R (in Ref. 1; CAA05364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 36724 MW; 56DB9CFAFA8C2B21 CRC64;
MAWWKAWVEQ EGVSVKGSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNVQRQQIA
KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYSYEAK ELHDAMKGLG TKEGVIIEIL
ASRTKNQLRE IMKAYEEDYG STLEEDIQGD TSGYLERILV CLLQGSRDDV SGFVDPGLVL
QDAQALHEAG EKIMGTDEMK FITILCTRSA THLMRVFEEY EKIANKCIED SIKSETHGSL
EEAMLTVVKC TRNVHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKGQFKKMYG
KTLSSMIMAD TSGYYKTALL NLVGTDL
