(data stored in SCRATCH zone)

SWISSPROT: ANXA8_HUMAN

ID   ANXA8_HUMAN             Reviewed;         327 AA.
AC   P13928; A6NDE6; A6NLM1; B4DKI1; B4DTC9; Q5T2P8; Q5VTM4; Q6GMY3;
AC   Q9BT34;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   08-MAY-2019, entry version 183.
DE   RecName: Full=Annexin A8 {ECO:0000312|HGNC:HGNC:546};
DE   AltName: Full=Annexin VIII {ECO:0000303|PubMed:1313714};
DE   AltName: Full=Annexin-8 {ECO:0000303|PubMed:2530088};
DE   AltName: Full=Vascular anticoagulant-beta {ECO:0000303|PubMed:2530088};
DE            Short=VAC-beta {ECO:0000303|PubMed:2530088};
GN   Name=ANXA8 {ECO:0000312|HGNC:HGNC:546}; Synonyms=ANX8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND
RP   ALA-177.
RC   TISSUE=Placenta;
RX   PubMed=2530088; DOI=10.1111/j.1432-1033.1989.tb15082.x;
RA   Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H.,
RA   Reutelingsperger C.P.M.;
RT   "Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding
RT   protein that inhibits coagulation and phospholipase A2 activity. Its
RT   molecular cloning, expression and comparison with VAC-alpha.";
RL   Eur. J. Biochem. 185:63-71(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1313714;
RA   Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L.,
RA   Trujillo J.M., Stass S.A.;
RT   "Specific expression of the annexin VIII gene in acute promyelocytic
RT   leukemia.";
RL   Blood 79:1802-1810(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Cervix, and Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ALA-177.
RC   TISSUE=Lung, and Pancreas;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), AND CALCIUM-BINDING SITES.
RX   PubMed=15644210; DOI=10.1016/j.jmb.2004.11.015;
RA   Rety S., Sopkova-de Oliveira Santos J., Dreyfuss L., Blondeau K.,
RA   Hofbauerova K., Raguenes-Nicol C., Kerboeuf D., Renouard M.,
RA   Russo-Marie F., Lewit-Bentley A.;
RT   "The crystal structure of annexin A8 is similar to that of annexin
RT   A3.";
RL   J. Mol. Biol. 345:1131-1139(2005).
CC   -!- FUNCTION: This protein is an anticoagulant protein that acts as an
CC       indirect inhibitor of the thromboplastin-specific complex, which
CC       is involved in the blood coagulation cascade.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P13928-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P13928-2; Sequence=VSP_056397, VSP_056398;
CC         Note=No experimental confirmation available.;
CC       Name=3;
CC         IsoId=P13928-3; Sequence=VSP_057805;
CC         Note=No experimental confirmation available.;
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC       calcium and phospholipid.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
DR   EMBL; X16662; CAA34650.1; -; mRNA.
DR   EMBL; M81844; AAB46383.1; -; mRNA.
DR   EMBL; AK296573; BAG59193.1; -; mRNA.
DR   EMBL; AK300158; BAG61941.1; -; mRNA.
DR   EMBL; AL391137; CAI12203.1; -; Genomic_DNA.
DR   EMBL; AL591684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004376; AAH04376.1; -; mRNA.
DR   EMBL; BC073755; AAH73755.1; -; mRNA.
DR   CCDS; CCDS73121.1; -. [P13928-3]
DR   CCDS; CCDS73122.1; -. [P13928-1]
DR   PIR; S06476; LUHU8.
DR   RefSeq; NP_001035173.1; NM_001040084.2. [P13928-1]
DR   RefSeq; NP_001092315.2; NM_001098845.2.
DR   RefSeq; NP_001258631.1; NM_001271702.1.
DR   RefSeq; NP_001258632.1; NM_001271703.1. [P13928-3]
DR   PDB; 1W3W; X-ray; 1.99 A; A=1-327.
DR   PDB; 1W45; X-ray; 2.51 A; A/B=1-327.
DR   PDBsum; 1W3W; -.
DR   PDBsum; 1W45; -.
DR   SMR; P13928; -.
DR   BioGrid; 575558; 9.
DR   BioGrid; 608549; 9.
DR   IntAct; P13928; 7.
DR   MINT; P13928; -.
DR   iPTMnet; P13928; -.
DR   PhosphoSitePlus; P13928; -.
DR   SwissPalm; P13928; -.
DR   BioMuta; ANXA8; -.
DR   DMDM; 215274181; -.
DR   EPD; P13928; -.
DR   jPOST; P13928; -.
DR   MaxQB; P13928; -.
DR   PaxDb; P13928; -.
DR   PeptideAtlas; P13928; -.
DR   PRIDE; P13928; -.
DR   ProteomicsDB; 52998; -.
DR   ProteomicsDB; 64350; -.
DR   DNASU; 244; -.
DR   Ensembl; ENST00000577813; ENSP00000463244; ENSG00000265190. [P13928-2]
DR   Ensembl; ENST00000583911; ENSP00000463091; ENSG00000265190. [P13928-3]
DR   Ensembl; ENST00000585281; ENSP00000462880; ENSG00000265190. [P13928-1]
DR   GeneID; 653145; -.
DR   GeneID; 728113; -.
DR   KEGG; hsa:653145; -.
DR   KEGG; hsa:728113; -.
DR   UCSC; uc001jev.5; human. [P13928-1]
DR   CTD; 653145; -.
DR   CTD; 728113; -.
DR   DisGeNET; 653145; -.
DR   DisGeNET; 728113; -.
DR   GeneCards; ANXA8; -.
DR   HGNC; HGNC:546; ANXA8.
DR   HPA; HPA045246; -.
DR   HPA; HPA047451; -.
DR   MIM; 602396; gene.
DR   neXtProt; NX_P13928; -.
DR   OpenTargets; ENSG00000265190; -.
DR   PharmGKB; PA134881914; -.
DR   PharmGKB; PA24836; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   eggNOG; ENOG410XPUN; LUCA.
DR   GeneTree; ENSGT00940000161044; -.
DR   HOGENOM; HOG000158803; -.
DR   InParanoid; P13928; -.
DR   KO; K17096; -.
DR   OrthoDB; 856254at2759; -.
DR   PhylomeDB; P13928; -.
DR   TreeFam; TF105452; -.
DR   ChiTaRS; ANXA8; human.
DR   EvolutionaryTrace; P13928; -.
DR   PRO; PR:P13928; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000265190; Expressed in 77 organ(s), highest expression level in vagina.
DR   ExpressionAtlas; P13928; baseline and differential.
DR   Genevisible; P13928; HS.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR   GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:UniProtKB.
DR   GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB.
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   PROSITE; PS00223; ANNEXIN; 4.
PE   1: Evidence at protein level;
DR   PRODOM; Q9BT34.
DR   SWISS-2DPAGE; Q9BT34.
KW   3D-structure; Alternative splicing; Annexin; Blood coagulation;
KW   Calcium; Calcium/phospholipid-binding; Complete proteome; Hemostasis;
KW   Metal-binding; Polymorphism; Reference proteome; Repeat.
FT   CHAIN         1    327       Annexin A8.
FT                                /FTId=PRO_0000067503.
FT   REPEAT       30     90       Annexin 1.
FT   REPEAT      102    162       Annexin 2.
FT   REPEAT      187    247       Annexin 3.
FT   REPEAT      262    322       Annexin 4.
FT   METAL       266    266       Calcium; via carbonyl oxygen.
FT   METAL       268    268       Calcium; via carbonyl oxygen.
FT   METAL       270    270       Calcium; via carbonyl oxygen.
FT   METAL       310    310       Calcium.
FT   VAR_SEQ       8     69       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057805.
FT   VAR_SEQ     138    141       DYGS -> GQQG (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056397.
FT   VAR_SEQ     142    327       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_056398.
FT   VARIANT       6      6       S -> A (in dbSNP:rs3870786).
FT                                {ECO:0000269|PubMed:2530088}.
FT                                /FTId=VAR_000604.
FT   VARIANT     177    177       G -> A (in dbSNP:rs3013886).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:2530088}.
FT                                /FTId=VAR_030630.
FT   CONFLICT     32     32       K -> Q (in Ref. 3; BAG59193 and 4;
FT                                CAI12203). {ECO:0000305}.
FT   CONFLICT     58     58       Q -> T (in Ref. 2; AAB46383).
FT                                {ECO:0000305}.
FT   CONFLICT     83     83       F -> L (in Ref. 2; AAB46383).
FT                                {ECO:0000305}.
FT   CONFLICT    157    157       R -> S (in Ref. 2; AAB46383).
FT                                {ECO:0000305}.
FT   CONFLICT    313    314       GD -> RY (in Ref. 2; AAB46383).
FT                                {ECO:0000305}.
FT   HELIX        24     34       {ECO:0000244|PDB:1W3W}.
FT   STRAND       35     38       {ECO:0000244|PDB:1W3W}.
FT   HELIX        41     48       {ECO:0000244|PDB:1W3W}.
FT   HELIX        53     67       {ECO:0000244|PDB:1W3W}.
FT   HELIX        71     78       {ECO:0000244|PDB:1W3W}.
FT   HELIX        81     91       {ECO:0000244|PDB:1W3W}.
FT   HELIX        96    107       {ECO:0000244|PDB:1W3W}.
FT   STRAND      108    110       {ECO:0000244|PDB:1W3W}.
FT   HELIX       113    122       {ECO:0000244|PDB:1W3W}.
FT   HELIX       125    139       {ECO:0000244|PDB:1W3W}.
FT   HELIX       143    150       {ECO:0000244|PDB:1W3W}.
FT   HELIX       153    163       {ECO:0000244|PDB:1W3W}.
FT   STRAND      167    170       {ECO:0000244|PDB:1W45}.
FT   HELIX       176    191       {ECO:0000244|PDB:1W3W}.
FT   STRAND      193    195       {ECO:0000244|PDB:1W3W}.
FT   HELIX       198    207       {ECO:0000244|PDB:1W3W}.
FT   HELIX       210    224       {ECO:0000244|PDB:1W3W}.
FT   HELIX       228    235       {ECO:0000244|PDB:1W3W}.
FT   HELIX       238    252       {ECO:0000244|PDB:1W3W}.
FT   HELIX       254    266       {ECO:0000244|PDB:1W3W}.
FT   STRAND      267    270       {ECO:0000244|PDB:1W3W}.
FT   HELIX       273    283       {ECO:0000244|PDB:1W3W}.
FT   TURN        284    286       {ECO:0000244|PDB:1W3W}.
FT   HELIX       288    299       {ECO:0000244|PDB:1W3W}.
FT   HELIX       303    310       {ECO:0000244|PDB:1W3W}.
FT   HELIX       313    323       {ECO:0000244|PDB:1W3W}.
SQ   SEQUENCE   327 AA;  36881 MW;  5DBBDBB6E723C298 CRC64;
     MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA
     KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL
     ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL
     QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL
     EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG
     KTLSSMIMED TSGDYKNALL SLVGSDP
//

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