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P79134 (ANXA6_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A6
Alternative name(s):
Annexin VI
Annexin-6
Gene names
Name:ANXA6
Synonyms:ANX6
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May associate with CD21. May regulate the release of Ca2+ from intracellular stores.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity.

Domain

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Post-translational modification

Phosphorylated in response to growth factor stimulation By similarity.

Miscellaneous

Seems to bind one calcium ion with high affinity.

Sequence similarities

Belongs to the annexin family.

Contains 8 annexin repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbiomineral tissue development

Inferred from direct assay PubMed 18597635. Source: AgBase

calcium ion import

Inferred from mutant phenotype PubMed 18597635. Source: AgBase

calcium ion transport

Inferred from sequence or structural similarity. Source: AgBase

growth plate cartilage chondrocyte differentiation

Inferred from direct assay PubMed 11696438. Source: AgBase

regulation of muscle contraction

Inferred from sequence or structural similarity. Source: AgBase

   Cellular_componentchromaffin granule membrane

Inferred from direct assay PubMed 1911746. Source: AgBase

cytoplasm

Inferred from direct assay PubMed 1423665. Source: AgBase

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from mutant phenotype PubMed 1423665. Source: AgBase

integral component of membrane

Traceable author statement PubMed 21672540. Source: AgBase

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 21672540. Source: AgBase

membrane-bounded vesicle

Inferred from direct assay PubMed 18597635. Source: AgBase

mitochondrial crista

Inferred from direct assay PubMed 7875306. Source: AgBase

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: AgBase

plasma membrane

Inferred from direct assay PubMed 15226301. Source: AgBase

stress fiber

Inferred from mutant phenotype PubMed 1423665. Source: AgBase

   Molecular_functionactin filament binding

Inferred from physical interaction PubMed 1423665. Source: AgBase

calcium channel activity

Inferred from mutant phenotype PubMed 18597635. Source: AgBase

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 1423665. Source: AgBase

calcium-dependent protein binding

Inferred from physical interaction PubMed 1423665PubMed 15226301PubMed 1911746. Source: AgBase

chondroitin sulfate binding

Inferred from direct assay PubMed 9545337. Source: AgBase

enzyme binding

Inferred from physical interaction PubMed 21672540. Source: AgBase

heparin binding

Inferred from direct assay PubMed 9545337. Source: AgBase

identical protein binding

Inferred from mutant phenotype PubMed 1911746. Source: AgBase

receptor activity

Inferred from direct assay PubMed 21672540. Source: AgBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 673672Annexin A6
PRO_0000067493

Regions

Repeat29 – 8961Annexin 1
Repeat101 – 16161Annexin 2
Repeat185 – 24561Annexin 3
Repeat260 – 32061Annexin 4
Repeat372 – 43261Annexin 5
Repeat444 – 50461Annexin 6
Repeat533 – 59361Annexin 7
Repeat608 – 66861Annexin 8

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue301Phosphotyrosine By similarity
Modified residue631N6-acetyllysine By similarity
Modified residue681N6-acetyllysine By similarity
Modified residue751N6-acetyllysine By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue2011Phosphotyrosine By similarity
Modified residue3061N6-acetyllysine By similarity
Modified residue3701N6-acetyllysine By similarity
Modified residue4181N6-acetyllysine By similarity
Modified residue4831N6-acetyllysine By similarity
Modified residue6201N6-acetyllysine By similarity

Experimental info

Sequence conflict1411D → E in AAB47570. Ref.2
Sequence conflict1811V → L in AAB47570. Ref.2
Sequence conflict3911A → T in AAB47570. Ref.2
Sequence conflict4841S → T in AAB47570. Ref.2
Sequence conflict5581H → D in AAB47570. Ref.2
Sequence conflict5671I → V in AAB47570. Ref.2
Sequence conflict6181D → E in AAB47570. Ref.2

Secondary structure

......................................................................................... 673
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P79134 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: AC85A55BEFDF236B

FASTA67375,907
        10         20         30         40         50         60 
MAKPAQGAKY RGSIRDFPDF NPSQDAETLY NAMKGFGSDK EAILELITSR SNRQRQEICQ 

        70         80         90        100        110        120 
NYKSLYGKDL IADLKYELTG KFERLIVGLM RPPAYADAKE IKDAISGIGT DEKCLIEILA 

       130        140        150        160        170        180 
SRTNEQIHQL VAAYKDAYER DLEADITGDT SGHFRKMLVV LLQGTREEDD VVSEDLVQQD 

       190        200        210        220        230        240 
VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK 

       250        260        270        280        290        300 
LMLAVVKCIR STAEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS 

       310        320        330        340        350        360 
LYSMIKNDTS GEYKKTLLKL CGGDDDAAGQ FFPEAAQVAY QMWELSAVAR VELKGTVRPA 

       370        380        390        400        410        420 
GDFNPDADAK ALRKAMKGLG TDEDTIIDII AHRSNAQRQQ IRQTFKSHFG RDLMADLKSE 

       430        440        450        460        470        480 
LSGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKALIE ILATRTNAEI QAINKAYKED 

       490        500        510        520        530        540 
YHKSLEDALS SDTSGHFKRI LISLATGNRE EGGEDRERAR EDAQVAAEIL EIADTTSGDK 

       550        560        570        580        590        600 
SSLETRFMMI LCTRSYPHLR RVFQEFIKMT NYDVEHTIKK EMSGDVRDVF VAIVQSVKNK 

       610        620        630        640        650        660 
PLFFADKLYK SMKGAGTDEK TLTRIMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGH 

       670 
FLKALLAICG GED 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[2]Comera C., Creutz C.E.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-673.
Tissue: Liver.
[3]"Crystal structure of bovine annexin VI in a calcium-bound state."
Avila-Sakar A.J., Creutz C.E., Kretsinger R.H.
Biochim. Biophys. Acta 1387:103-116(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 56-673 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC151391 mRNA. Translation: AAI51392.1.
U87539 mRNA. Translation: AAB47570.1.
RefSeqNP_001096694.1. NM_001103224.1.
XP_005209618.1. XM_005209561.1.
UniGeneBt.5267.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVCX-ray2.90A46-673[»]
ProteinModelPortalP79134.
SMRP79134. Positions 10-671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000019719.

Proteomic databases

PaxDbP79134.
PRIDEP79134.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000019719; ENSBTAP00000019719; ENSBTAG00000014809.
GeneID327685.
KEGGbta:327685.

Organism-specific databases

CTD309.

Phylogenomic databases

eggNOGNOG267770.
GeneTreeENSGT00740000115434.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP79134.
KOK17094.
OMAEKSLYSM.
OrthoDBEOG74XS72.
TreeFamTF105452.

Family and domain databases

Gene3D1.10.220.10. 8 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002393. AnnexinVI.
[Graphical view]
PfamPF00191. Annexin. 8 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00202. ANNEXINVI.
SMARTSM00335. ANX. 8 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP79134.
NextBio20810150.

Entry information

Entry nameANXA6_BOVIN
AccessionPrimary (citable) accession number: P79134
Secondary accession number(s): A7YY61
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references