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P20073 (ANXA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A7
Alternative name(s):
Annexin VII
Annexin-7
Synexin
Gene names
Name:ANXA7
Synonyms:ANX7, SNX
ORF Names:OK/SW-cl.95
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.

Subunit structure

Interacts with PDCD6. Ref.10

Tissue specificity

Isoform 1 is expressed in brain, heart and skeletal muscle. Isoform 2 is more abundant in liver, lung, kidney, spleen, fibroblasts and placenta. Ref.9

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.

Sequence caution

The sequence CAI52483.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular water homeostasis

Inferred from electronic annotation. Source: Ensembl

epithelial cell differentiation

Inferred from expression pattern PubMed 21492153. Source: UniProt

hemostasis

Inferred from electronic annotation. Source: Ensembl

membrane fusion

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to salt stress

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from expression pattern PubMed 21531385. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

nuclear envelope

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10672515. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-dependent protein binding

Inferred from physical interaction PubMed 12445460. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20073-1)

Also known as: Annexin VIIb;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20073-2)

Also known as: Annexin VIIa;

The sequence of this isoform differs from the canonical sequence as follows:
     146-167: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Annexin A7
PRO_0000067499

Regions

Repeat5 – 951
Repeat10 – 1452
Repeat16 – 2053
Repeat189 – 25466Annexin 1
Repeat266 – 32661Annexin 2
Repeat349 – 40961Annexin 3
Repeat425 – 48561Annexin 4
Region1 – 143143Repeat-rich region
Region5 – 20163 X 5 AA tandem repeats of G-Y-P-P-X

Amino acid modifications

Modified residue2331N6-acetyllysine Ref.11

Natural variations

Alternative sequence146 – 16722Missing in isoform 2.
VSP_011843
Natural variant4411R → Q.
Corresponds to variant rs3750575 [ dbSNP | Ensembl ].
VAR_048253

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Annexin VIIb) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: BFC688479D8CC2A0

FASTA48852,739
        10         20         30         40         50         60 
MSYPGYPPTG YPPFPGYPPA GQESSFPPSG QYPYPSGFPP MGGGAYPQVP SSGYPGAGGY 

        70         80         90        100        110        120 
PAPGGYPAPG GYPGAPQPGG APSYPGVPPG QGFGVPPGGA GFSGYPQPPS QSYGGGPAQV 

       130        140        150        160        170        180 
PLPGGFPGGQ MPSQYPGGQP TYPSQINTDS FSSYPVFSPV SLDYSSEPAT VTQVTQGTIR 

       190        200        210        220        230        240 
PAANFDAIRD AEILRKAMKG FGTDEQAIVD VVANRSNDQR QKIKAAFKTS YGKDLIKDLK 

       250        260        270        280        290        300 
SELSGNMEEL ILALFMPPTY YDAWSLRKAM QGAGTQERVL IEILCTRTNQ EIREIVRCYQ 

       310        320        330        340        350        360 
SEFGRDLEKD IRSDTSGHFE RLLVSMCQGN RDENQSINHQ MAQEDAQRLY QAGEGRLGTD 

       370        380        390        400        410        420 
ESCFNMILAT RSFPQLRATM EAYSRMANRD LLSSVSREFS GYVESGLKTI LQCALNRPAF 

       430        440        450        460        470        480 
FAERLYYAMK GAGTDDSTLV RIVVTRSEID LVQIKQMFAQ MYQKTLGTMI AGDTSGDYRR 


LLLAIVGQ 

« Hide

Isoform 2 (Annexin VIIa) [UniParc].

Checksum: 09A6760729D45FCD
Show »

FASTA46650,316

References

« Hide 'large scale' references
[1]"Calcium channel activity of purified human synexin and structure of the human synexin gene."
Burns A.L., Magendzo K., Shirvan A., Srivastava M., Rojas E., Alijani M.R., Pollard H.B.
Proc. Natl. Acad. Sci. U.S.A. 86:3798-3802(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
[2]"Divergent structure of the human synexin (annexin VII) gene and assignment to chromosome 10."
Shirvan A., Srivastava M., Wang M.G., Cultraro C., Magendzo K., McBride O.W., Pollard H.B., Burns A.L.
Biochemistry 33:6888-6901(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon adenocarcinoma.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"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. expand/collapse author list , 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].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 2).
Tissue: Pancreas.
[9]"Alternative splicing of human synexin mRNA in brain, cardiac, and skeletal muscle alters the unique N-terminal domain."
Magendzo K., Shirvan A., Cultraro C., Srivastava M., Pollard H.B., Burns A.L.
J. Biol. Chem. 266:3228-3232(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 145-166 (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Fibroblast.
[10]"Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDCD6.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04543 mRNA. Translation: AAA36616.1.
AB062429 mRNA. Translation: BAB93492.1.
BT007187 mRNA. Translation: AAP35851.1.
CR407686 mRNA. Translation: CAG28614.1.
AL512656, AL353731 Genomic DNA. Translation: CAI15290.1.
AL512656, AL353731 Genomic DNA. Translation: CAI15291.1.
AL353731 Genomic DNA. Translation: CAI52483.1. Sequence problems.
AL353731, AL512656 Genomic DNA. Translation: CAI52484.1.
AL353731, AL512656 Genomic DNA. Translation: CAI52485.1.
CH471083 Genomic DNA. Translation: EAW54493.1.
CH471083 Genomic DNA. Translation: EAW54494.1.
BC002632 mRNA. Translation: AAH02632.1.
PIRLUHU7. A54467.
RefSeqNP_001147.1. NM_001156.3.
NP_004025.1. NM_004034.2.
UniGeneHs.631827.

3D structure databases

ProteinModelPortalP20073.
SMRP20073. Positions 174-488.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106807. 114 interactions.
IntActP20073. 114 interactions.
MINTMINT-4999305.
STRING9606.ENSP00000362010.

PTM databases

PhosphoSiteP20073.

Polymorphism databases

DMDM215274186.

2D gel databases

REPRODUCTION-2DPAGEIPI00002460.

Proteomic databases

PaxDbP20073.
PRIDEP20073.

Protocols and materials databases

DNASU310.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372919; ENSP00000362010; ENSG00000138279. [P20073-1]
ENST00000372921; ENSP00000362012; ENSG00000138279. [P20073-2]
GeneID310.
KEGGhsa:310.
UCSCuc001jtz.2. human. [P20073-1]
uc001jua.2. human. [P20073-2]

Organism-specific databases

CTD310.
GeneCardsGC10M075135.
HGNCHGNC:545. ANXA7.
HPACAB004312.
MIM186360. gene.
neXtProtNX_P20073.
PharmGKBPA24835.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267770.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP20073.
KOK17095.
OMAFSQMYQK.
OrthoDBEOG74XS72.
PhylomeDBP20073.
TreeFamTF105452.

Gene expression databases

ArrayExpressP20073.
BgeeP20073.
CleanExHS_ANXA7.
GenevestigatorP20073.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR013286. AnnexinVII.
[Graphical view]
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR01871. ANNEXINVII.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA7. human.
GeneWikiANXA7.
GenomeRNAi310.
NextBio1253.
PROP20073.
SOURCESearch...

Entry information

Entry nameANXA7_HUMAN
AccessionPrimary (citable) accession number: P20073
Secondary accession number(s): Q5F2H3, Q5T0M6, Q5T0M7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM