P13928 (ANXA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Annexin A8

Alternative name(s):
Annexin VIII
Annexin-8
Vascular anticoagulant-beta
Short name=VAC-beta

Gene names

Name:	ANXA8
Synonyms:	ANX8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Coding sequence diversity	Polymorphism
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding Metal-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 327

327

Annexin A8

PRO_0000067503

Regions

Repeat

30 – 90

61

Annexin 1

Repeat

102 – 162

61

Annexin 2

Repeat

187 – 247

61

Annexin 3

Repeat

262 – 322

61

Annexin 4

Sites

Metal binding

266

1

Calcium; via carbonyl oxygen

Metal binding

268

1

Calcium; via carbonyl oxygen

Metal binding

270

1

Calcium; via carbonyl oxygen

Metal binding

310

1

Calcium

Natural variations

Natural variant

6

1

S → A. Ref.1

VAR_000604

Natural variant

177

1

G → A. Ref.1 Ref.4
Corresponds to variant rs3013886 [ dbSNP | Ensembl ].

VAR_030630

Experimental info

Sequence conflict

58

1

Q → T in AAB46383. Ref.2

Sequence conflict

83

1

F → L in AAB46383. Ref.2

Sequence conflict

157

1

R → S in AAB46383. Ref.2

Sequence conflict

313 – 314

2

GD → RY in AAB46383. Ref.2

Secondary structure

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327

Helix Strand Turn

Details...

Helix

24 – 34

11

Beta strand

35 – 38

4

Helix

41 – 48

8

Helix

53 – 67

15

Helix

71 – 78

8

Helix

81 – 91

11

Helix

96 – 107

12

Beta strand

108 – 110

3

Helix

113 – 122

10

Helix

125 – 139

15

Helix

143 – 150

8

Helix

153 – 163

11

Beta strand

167 – 170

4

Helix

176 – 191

16

Beta strand

193 – 195

3

Helix

198 – 207

10

Helix

210 – 224

15

Helix

228 – 235

8

Helix

238 – 252

15

Helix

254 – 266

13

Beta strand

267 – 270

4

Helix

273 – 283

11

Turn

284 – 286

3

Helix

288 – 299

12

Helix

303 – 310

8

Helix

313 – 323

11

Sequences

	Sequence		Length	Mass (Da)
	P13928 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 5DBBDBB6E723C298	FASTA	327	36,881
	10 20 30 40 50 60 MAWWKSWIEQ EGVTVKSSSH FNPDPDAETL YKAMKGIGTN EQAIIDVLTK RSNTQRQQIA 70 80 90 100 110 120 KSFKAQFGKD LTETLKSELS GKFERLIVAL MYPPYRYEAK ELHDAMKGLG TKEGVIIEIL 130 140 150 160 170 180 ASRTKNQLRE IMKAYEEDYG SSLEEDIQAD TSGYLERILV CLLQGSRDDV SSFVDPGLAL 190 200 210 220 230 240 QDAQDLYAAG EKIRGTDEMK FITILCTRSA THLLRVFEEY EKIANKSIED SIKSETHGSL 250 260 270 280 290 300 EEAMLTVVKC TQNLHSYFAE RLYYAMKGAG TRDGTLIRNI VSRSEIDLNL IKCHFKKMYG 310 320 KTLSSMIMED TSGDYKNALL SLVGSDP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Hauptmann R., Maurer-Fogy I., Krystek E., Bodo G., Andree H., Reutelingsperger C.P.M. Eur. J. Biochem. 185:63-71(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-6 AND ALA-177. Tissue: Placenta.
[2]	"Specific expression of the annexin VIII gene in acute promyelocytic leukemia." Chang K.S., Wang G., Freireich E.J., Daly M., Naylor S.L., Trujillo J.M., Stass S.A. Blood 79:1802-1810(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-177. Tissue: Lung and Pancreas.
[5]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]	"The crystal structure of annexin A8 is similar to that of annexin A3." 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. J. Mol. Biol. 345:1131-1139(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS), CALCIUM-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16662 mRNA. Translation: CAA34650.1.
M81844 mRNA. Translation: AAB46383.1.
AL591684 Genomic DNA. Translation: CAH72203.1.
BC004376 mRNA. Translation: AAH04376.1.
BC073755 mRNA. Translation: AAH73755.1.

IPI

IPI00872295.

PIR

LUHU8. S06476.

RefSeq

NP_001035173.1. NM_001040084.2.
NP_001258631.1. NM_001271702.1.
NP_001258632.1. NM_001271703.1.
NP_001621.2. NM_001630.2.

UniGene

Hs.535306.
Hs.705389.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W3W	X-ray	1.99	A	1-327	[»]
1W45	X-ray	2.51	A/B	1-327	[»]

ProteinModelPortal

P13928.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13928. 2 interactions.

MINT

MINT-1892975.

STRING

9606.ENSP00000341674.

PTM databases

PhosphoSite

P13928.

Proteomic databases

PaxDb

P13928.

PRIDE

P13928.

Protocols and materials databases

DNASU

244.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344416; ENSP00000341674; ENSG00000165390.
ENST00000585281; ENSP00000462880; ENSG00000265190.

GeneID

244.
653145.

KEGG

hsa:244.
hsa:653145.

Organism-specific databases

CTD

244.
653145.

GeneCards

GC10P048255.

HGNC

HGNC:546. ANXA8.

MIM

602396. gene.

neXtProt

NX_P13928.

PharmGKB

PA24836.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG267770.

HOGENOM

HOG000158803.

HOVERGEN

HBG061815.

InParanoid

P13928.

OMA

PHFNPDP.

Gene expression databases

ArrayExpress

P13928.

Bgee

P13928.

CleanEx

HS_ANXA8.

Genevestigator

P13928.

GermOnline

ENSG00000186807. Homo sapiens.

Family and domain databases

Gene3D

1.10.220.10. 4 hits.

InterPro

IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR009115. AnnexinVIII.
[Graphical view]

PANTHER

PTHR10502. PTHR10502. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR01808. ANNEXINVIII.

SMART

SM00335. ANX. 4 hits.
[Graphical view]

SUPFAM

SSF47874. Annexin. 1 hit.

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P13928.

NextBio

972.

SOURCE

Search...

Entry information

Entry name

ANXA8_HUMAN

Accession

Primary (citable) accession number: P13928
Secondary accession number(s): A6NLM1 , Q5VTM4, Q6GMY3, Q9BT34

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.