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P14668 (ANXA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. 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 A5
Alternative name(s):
Anchorin CII
Annexin V
Annexin-5
Calphobindin I
Short name=CBP-I
Endonexin II
Lipocortin V
Placental anticoagulant protein 4
Short name=PP4
Placental anticoagulant protein I
Short name=PAP-I
Thromboplastin inhibitor
Vascular anticoagulant-alpha
Short name=VAC-alpha
Gene names
Name:Anxa5
Synonyms:Anx5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subunit structure

Monomer. Binds ATRX, EIF5B and DNMT1.

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 processBlood coagulation
Hemostasis
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of blood coagulation

Inferred from direct assay PubMed 20684318. Source: RGD

positive regulation of apoptotic process

Inferred from direct assay PubMed 15537503. Source: RGD

protein homooligomerization

Inferred from direct assay PubMed 12401794. Source: RGD

regulation of sperm motility

Inferred from direct assay PubMed 20684318. Source: RGD

response to calcium ion

Inferred from direct assay Ref.5. Source: RGD

   Cellular_componentZ disc

Inferred from direct assay PubMed 7585827. Source: RGD

cell projection

Inferred from direct assay PubMed 1833446. Source: RGD

cytoplasm

Inferred from direct assay PubMed 1833446. Source: RGD

extracellular space

Inferred from direct assay PubMed 11271515. Source: RGD

intercalated disc

Inferred from direct assay PubMed 1833446. Source: RGD

nucleus

Inferred from direct assay PubMed 9723888. Source: RGD

plasma membrane

Inferred from direct assay PubMed 1833446. Source: RGD

sarcolemma

Inferred from direct assay PubMed 1833446. Source: RGD

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 12401794PubMed 2307675. Source: RGD

peptide hormone binding

Inferred from direct assay PubMed 1386737. Source: RGD

protein binding

Inferred from physical interaction Ref.4. Source: RGD

receptor tyrosine kinase binding

Inferred from physical interaction PubMed 10329451. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 319318Annexin A5
PRO_0000067490

Regions

Repeat21 – 8161Annexin 1
Repeat93 – 15361Annexin 2
Repeat177 – 23761Annexin 3
Repeat252 – 31261Annexin 4

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue681N6-acetyllysine By similarity
Modified residue741N6-acetyllysine By similarity
Modified residue771N6-acetyllysine By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue991N6-acetyllysine By similarity
Modified residue2881N6-succinyllysine By similarity

Secondary structure

............................................... 319
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14668 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3B5D3AFDE8C3F32C

FASTA31935,745
        10         20         30         40         50         60 
MALRGTVTDF SGFDGRADAE VLRKAMKGLG TDEDSILNLL TARSNAQRQQ IAEEFKTLFG 

        70         80         90        100        110        120 
RDLVNDMKSE LTGKFEKLIV ALMKPSRLYD AYELKHALKG AGTDEKVLTE IIASRTPEEL 

       130        140        150        160        170        180 
RAIKQAYEEE YGSNLEDDVV GDTSGYYQRM LVVLLQANRD PDTAIDDAQV ELDAQALFQA 

       190        200        210        220        230        240 
GELKWGTDEE KFITILGTRS VSHLRRVFDK YMTISGFQIE ETIDRETSGN LENLLLAVVK 

       250        260        270        280        290        300 
SIRSIPAYLA ETLYYAMKGA GTDDHTLIRV IVSRSEIDLF NIRKEFRKNF ATSLYSMIKG 

       310 
DTSGDYKKAL LLLCGGEDD 

« Hide

References

[1]"Five distinct calcium and phospholipid binding proteins share homology with lipocortin I."
Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T., Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L., Hession C., Frey A.Z., Wallner B.P.
J. Biol. Chem. 263:10799-10811(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of rat annexin V gene and molecular diversity of its transcripts."
Imai Y., Kohsaka S.
Eur. J. Biochem. 232:327-334(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Wistar.
[3]Lubec G., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-16; 150-159; 192-199; 259-269 AND 289-299, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[4]"Molecular cloning and characterization of annexin V-binding proteins with highly hydrophilic peptide structure."
Ohsawa K., Imai Y., Ito D., Kohsaka S.
J. Neurochem. 67:89-97(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF5B AND DNMT1.
[5]"Rat annexin V crystal structure: Ca(2+)-induced conformational changes."
Concha N.O., Head J.F., Kaetzel M.A., Dedman J.R., Seaton B.A.
Science 261:1321-1324(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]"Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V."
Swairjo M.A., Concha N.O., Kaetzel M.A., Dedman J.R., Seaton B.A.
Nat. Struct. Biol. 2:968-974(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
Tissue: Kidney.
[7]"Mutational and crystallographic analyses of interfacial residues in annexin V suggest direct interactions with phospholipid membrane components."
Campos B., Mo Y.D., Mealy T.R., Li C.W., Swairjo M.A., Balch C., Head J.F., Retzinger G., Dedman J.R., Seaton B.A.
Biochemistry 37:8004-8010(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-320.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21730 mRNA. Translation: AAA41512.1.
D42137 Genomic DNA. Translation: BAA07708.1.
PIRLURT5. C29250.
RefSeqNP_037264.1. NM_013132.1.
UniGeneRn.3318.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8AX-ray1.90A2-319[»]
1A8BX-ray1.90A2-319[»]
1BC0X-ray2.00A1-319[»]
1BC1X-ray2.05A1-319[»]
1BC3X-ray1.95A1-319[»]
1BCWX-ray2.10A1-319[»]
1BCYX-ray1.95A1-319[»]
1BCZX-ray2.20A1-319[»]
1G5NX-ray1.90A2-319[»]
1N41X-ray2.10A1-319[»]
1N42X-ray2.10A1-319[»]
1N44X-ray3.00A1-319[»]
2H0KX-ray2.76A/B2-319[»]
2H0LX-ray2.59A2-319[»]
2H0MX-ray2.26A1-318[»]
2IE6X-ray1.83A2-319[»]
2IE7X-ray1.75A2-319[»]
2RANX-ray1.89A2-317[»]
ProteinModelPortalP14668.
SMRP14668. Positions 2-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247702. 1 interaction.
IntActP14668. 1 interaction.
MINTMINT-4996466.
STRING10116.ENSRNOP00000019552.

PTM databases

PhosphoSiteP14668.

2D gel databases

World-2DPAGE0004:P14668.

Proteomic databases

PaxDbP14668.
PRIDEP14668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25673.
KEGGrno:25673.
UCSCRGD:2120. rat.

Organism-specific databases

CTD308.
RGD2120. Anxa5.

Phylogenomic databases

eggNOGNOG281174.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP14668.
KOK16646.
PhylomeDBP14668.

Gene expression databases

GenevestigatorP14668.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
PANTHERPTHR10502:SF26. PTHR10502:SF26. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14668.
NextBio607615.
PROP14668.

Entry information

Entry nameANXA5_RAT
AccessionPrimary (citable) accession number: P14668
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 3 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