Annexin A7

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.[5][6]

AliasesANXA7, ANX7, SNX, SYNEXIN, annexin A7
End73,414,076 bp[1]
Quick facts ANXA7, Identifiers ...
ANXA7
Identifiers
AliasesANXA7, ANX7, SNX, SYNEXIN, annexin A7
External IDsOMIM: 186360; MGI: 88031; HomoloGene: 36149; GeneCards: ANXA7; OMA:ANXA7 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001156
NM_004034
NM_001320879
NM_001320880

NM_001110794
NM_009674
NM_001374757

RefSeq (protein)

NP_001147
NP_001307808
NP_001307809
NP_004025

NP_001104264
NP_033804
NP_001361686

Location (UCSC)Chr 10: 73.38 – 73.41 MbChr 14: 20.51 – 20.53 Mb
PubMed search[3][4]
Wikidata
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Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in two mRNA transcripts of 2.0 and 2.4 kb which are predicted to generate two protein isoforms differing in their N-terminal domain. The alternative splicing event is tissue specific and the mRNA containing the cassette exon is prevalent in brain, heart and skeletal muscle. The transcripts also differ in their 3'-non coding regions by the use of two alternative poly(A) signals. The selection of poly(A) signals is independent of the mRNA splicing pattern. ~Annexin VII encodes a protein with a molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.[6]

Function

Suppresses tumor[7] and tumorigenesis and metastasis.[8]

Interactions

ANXA7 has been shown to interact with ALG2[9] and SRI.[10]

References

Further reading

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