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Annexin A8 (Annexin VIII) (Annexin-8) (Vascular anticoagulant-beta) (VAC-beta)

 ANXA8_HUMAN             Reviewed;         327 AA.
P13928; A6NDE6; A6NLM1; B4DKI1; B4DTC9; Q5T2P8; Q5VTM4; Q6GMY3;
Q9BT34;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
16-JAN-2019, entry version 180.
RecName: Full=Annexin A8 {ECO:0000312|HGNC:HGNC:546};
AltName: Full=Annexin VIII {ECO:0000303|PubMed:1313714};
AltName: Full=Annexin-8 {ECO:0000303|PubMed:2530088};
AltName: Full=Vascular anticoagulant-beta {ECO:0000303|PubMed:2530088};
Short=VAC-beta {ECO:0000303|PubMed:2530088};
Name=ANXA8 {ECO:0000312|HGNC:HGNC:546}; Synonyms=ANX8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND
ALA-177.
TISSUE=Placenta;
PubMed=2530088; DOI=10.1111/j.1432-1033.1989.tb15082.x;
Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H.,
Reutelingsperger C.P.M.;
"Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding
protein that inhibits coagulation and phospholipase A2 activity. Its
molecular cloning, expression and comparison with VAC-alpha.";
Eur. J. Biochem. 185:63-71(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1313714;
Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L.,
Trujillo J.M., Stass S.A.;
"Specific expression of the annexin VIII gene in acute promyelocytic
leukemia.";
Blood 79:1802-1810(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Cervix, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-177.
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), AND CALCIUM-BINDING SITES.
PubMed=15644210; DOI=10.1016/j.jmb.2004.11.015;
Rety S., Sopkova-de Oliveira Santos J., Dreyfuss L., Blondeau K.,
Hofbauerova K., Raguenes-Nicol C., Kerboeuf D., Renouard M.,
Russo-Marie F., Lewit-Bentley A.;
"The crystal structure of annexin A8 is similar to that of annexin
A3.";
J. Mol. Biol. 345:1131-1139(2005).
-!- FUNCTION: This protein is an anticoagulant protein that acts as an
indirect inhibitor of the thromboplastin-specific complex, which
is involved in the blood coagulation cascade.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P13928-1; Sequence=Displayed;
Name=2;
IsoId=P13928-2; Sequence=VSP_056397, VSP_056398;
Note=No experimental confirmation available.;
Name=3;
IsoId=P13928-3; Sequence=VSP_057805;
Note=No experimental confirmation available.;
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; X16662; CAA34650.1; -; mRNA.
EMBL; M81844; AAB46383.1; -; mRNA.
EMBL; AK296573; BAG59193.1; -; mRNA.
EMBL; AK300158; BAG61941.1; -; mRNA.
EMBL; AL391137; CAI12203.1; -; Genomic_DNA.
EMBL; AL591684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004376; AAH04376.1; -; mRNA.
EMBL; BC073755; AAH73755.1; -; mRNA.
CCDS; CCDS73121.1; -. [P13928-3]
CCDS; CCDS73122.1; -. [P13928-1]
PIR; S06476; LUHU8.
RefSeq; NP_001035173.1; NM_001040084.2. [P13928-1]
RefSeq; NP_001092315.2; NM_001098845.2.
RefSeq; NP_001258631.1; NM_001271702.1.
RefSeq; NP_001258632.1; NM_001271703.1. [P13928-3]
UniGene; Hs.535306; -.
UniGene; Hs.705389; -.
UniGene; Hs.744068; -.
PDB; 1W3W; X-ray; 1.99 A; A=1-327.
PDB; 1W45; X-ray; 2.51 A; A/B=1-327.
PDBsum; 1W3W; -.
PDBsum; 1W45; -.
ProteinModelPortal; P13928; -.
SMR; P13928; -.
BioGrid; 575558; 9.
BioGrid; 608549; 9.
IntAct; P13928; 7.
MINT; P13928; -.
STRING; 9606.ENSP00000341674; -.
iPTMnet; P13928; -.
PhosphoSitePlus; P13928; -.
BioMuta; ANXA8; -.
DMDM; 215274181; -.
EPD; P13928; -.
jPOST; P13928; -.
MaxQB; P13928; -.
PaxDb; P13928; -.
PeptideAtlas; P13928; -.
PRIDE; P13928; -.
ProteomicsDB; 52998; -.
ProteomicsDB; 64350; -.
DNASU; 244; -.
Ensembl; ENST00000577813; ENSP00000463244; ENSG00000265190. [P13928-2]
Ensembl; ENST00000583911; ENSP00000463091; ENSG00000265190. [P13928-3]
Ensembl; ENST00000585281; ENSP00000462880; ENSG00000265190. [P13928-1]
GeneID; 653145; -.
GeneID; 728113; -.
KEGG; hsa:653145; -.
KEGG; hsa:728113; -.
UCSC; uc001jev.5; human. [P13928-1]
CTD; 653145; -.
CTD; 728113; -.
DisGeNET; 653145; -.
DisGeNET; 728113; -.
EuPathDB; HostDB:ENSG00000265190.6; -.
GeneCards; ANXA8; -.
HGNC; HGNC:546; ANXA8.
HPA; HPA045246; -.
HPA; HPA047451; -.
MIM; 602396; gene.
neXtProt; NX_P13928; -.
OpenTargets; ENSG00000265190; -.
PharmGKB; PA134881914; -.
PharmGKB; PA24836; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00940000161044; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P13928; -.
KO; K17096; -.
OrthoDB; 856254at2759; -.
PhylomeDB; P13928; -.
TreeFam; TF105452; -.
ChiTaRS; ANXA8; human.
EvolutionaryTrace; P13928; -.
PRO; PR:P13928; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000265190; Expressed in 77 organ(s), highest expression level in vagina.
CleanEx; HS_ANXA8; -.
ExpressionAtlas; P13928; baseline and differential.
Genevisible; P13928; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
GO; GO:1900138; P:negative regulation of phospholipase A2 activity; IDA:UniProtKB.
GO; GO:1900004; P:negative regulation of serine-type endopeptidase activity; IDA:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR037104; Annexin_sf.
InterPro; IPR009115; ANX8.
PANTHER; PTHR10502:SF133; PTHR10502:SF133; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR01808; ANNEXINVIII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Annexin; Blood coagulation;
Calcium; Calcium/phospholipid-binding; Complete proteome; Hemostasis;
Metal-binding; Polymorphism; Reference proteome; Repeat.
CHAIN 1 327 Annexin A8.
/FTId=PRO_0000067503.
REPEAT 30 90 Annexin 1.
REPEAT 102 162 Annexin 2.
REPEAT 187 247 Annexin 3.
REPEAT 262 322 Annexin 4.
METAL 266 266 Calcium; via carbonyl oxygen.
METAL 268 268 Calcium; via carbonyl oxygen.
METAL 270 270 Calcium; via carbonyl oxygen.
METAL 310 310 Calcium.
VAR_SEQ 8 69 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057805.
VAR_SEQ 138 141 DYGS -> GQQG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056397.
VAR_SEQ 142 327 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056398.
VARIANT 6 6 S -> A (in dbSNP:rs3870786).
{ECO:0000269|PubMed:2530088}.
/FTId=VAR_000604.
VARIANT 177 177 G -> A (in dbSNP:rs3013886).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2530088}.
/FTId=VAR_030630.
CONFLICT 32 32 K -> Q (in Ref. 3; BAG59193 and 4;
CAI12203). {ECO:0000305}.
CONFLICT 58 58 Q -> T (in Ref. 2; AAB46383).
{ECO:0000305}.
CONFLICT 83 83 F -> L (in Ref. 2; AAB46383).
{ECO:0000305}.
CONFLICT 157 157 R -> S (in Ref. 2; AAB46383).
{ECO:0000305}.
CONFLICT 313 314 GD -> RY (in Ref. 2; AAB46383).
{ECO:0000305}.
HELIX 24 34 {ECO:0000244|PDB:1W3W}.
STRAND 35 38 {ECO:0000244|PDB:1W3W}.
HELIX 41 48 {ECO:0000244|PDB:1W3W}.
HELIX 53 67 {ECO:0000244|PDB:1W3W}.
HELIX 71 78 {ECO:0000244|PDB:1W3W}.
HELIX 81 91 {ECO:0000244|PDB:1W3W}.
HELIX 96 107 {ECO:0000244|PDB:1W3W}.
STRAND 108 110 {ECO:0000244|PDB:1W3W}.
HELIX 113 122 {ECO:0000244|PDB:1W3W}.
HELIX 125 139 {ECO:0000244|PDB:1W3W}.
HELIX 143 150 {ECO:0000244|PDB:1W3W}.
HELIX 153 163 {ECO:0000244|PDB:1W3W}.
STRAND 167 170 {ECO:0000244|PDB:1W45}.
HELIX 176 191 {ECO:0000244|PDB:1W3W}.
STRAND 193 195 {ECO:0000244|PDB:1W3W}.
HELIX 198 207 {ECO:0000244|PDB:1W3W}.
HELIX 210 224 {ECO:0000244|PDB:1W3W}.
HELIX 228 235 {ECO:0000244|PDB:1W3W}.
HELIX 238 252 {ECO:0000244|PDB:1W3W}.
HELIX 254 266 {ECO:0000244|PDB:1W3W}.
STRAND 267 270 {ECO:0000244|PDB:1W3W}.
HELIX 273 283 {ECO:0000244|PDB:1W3W}.
TURN 284 286 {ECO:0000244|PDB:1W3W}.
HELIX 288 299 {ECO:0000244|PDB:1W3W}.
HELIX 303 310 {ECO:0000244|PDB:1W3W}.
HELIX 313 323 {ECO:0000244|PDB:1W3W}.
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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E0259m ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I 96T
E0259b ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
E0259r ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattu 96T
E0259r