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Protein

Annexin A5

Gene

Anxa5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: RGD
  2. calcium ion binding Source: InterPro
  3. peptide hormone binding Source: RGD
  4. receptor tyrosine kinase binding Source: RGD

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. negative regulation of blood coagulation Source: RGD
  3. positive regulation of apoptotic process Source: RGD
  4. protein homooligomerization Source: RGD
  5. regulation of sperm motility Source: RGD
  6. response to calcium ion Source: RGD
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Calcium/phospholipid-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Anxa5
Synonyms:Anx5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2120. Anxa5.

Subcellular locationi

GO - Cellular componenti

  1. cell projection Source: RGD
  2. cytoplasm Source: RGD
  3. extracellular space Source: RGD
  4. intercalated disc Source: RGD
  5. nucleus Source: RGD
  6. plasma membrane Source: RGD
  7. sarcolemma Source: RGD
  8. Z disc Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 319318Annexin A5PRO_0000067490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei68 – 681N6-acetyllysineBy similarity
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei95 – 951N6-acetyllysineBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei288 – 2881N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP14668.
PRIDEiP14668.

2D gel databases

World-2DPAGE0004:P14668.

PTM databases

PhosphoSiteiP14668.

Expressioni

Gene expression databases

GenevestigatoriP14668.

Interactioni

Subunit structurei

Monomer. Binds ATRX, EIF5B and DNMT1.

Protein-protein interaction databases

BioGridi247702. 2 interactions.
IntActiP14668. 1 interaction.
MINTiMINT-4996466.
STRINGi10116.ENSRNOP00000019552.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2612Combined sources
Beta strandi27 – 304Combined sources
Helixi33 – 408Combined sources
Helixi45 – 5915Combined sources
Helixi63 – 708Combined sources
Helixi73 – 8311Combined sources
Helixi86 – 9712Combined sources
Helixi100 – 1023Combined sources
Helixi105 – 11410Combined sources
Helixi117 – 13115Combined sources
Helixi135 – 1428Combined sources
Helixi145 – 15511Combined sources
Helixi167 – 18014Combined sources
Turni181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Helixi189 – 19810Combined sources
Helixi201 – 21515Combined sources
Helixi219 – 2268Combined sources
Helixi229 – 24315Combined sources
Helixi245 – 25713Combined sources
Beta strandi258 – 2614Combined sources
Helixi264 – 27411Combined sources
Turni275 – 2784Combined sources
Helixi279 – 29012Combined sources
Helixi294 – 3018Combined sources
Helixi304 – 31411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14668.
SMRiP14668. Positions 2-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14668.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati21 – 8161Annexin 1Add
BLAST
Repeati93 – 15361Annexin 2Add
BLAST
Repeati177 – 23761Annexin 3Add
BLAST
Repeati252 – 31261Annexin 4Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the annexin family.Curated
Contains 4 annexin repeats.Curated

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiNOG281174.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP14668.
KOiK16646.
PhylomeDBiP14668.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
PANTHERiPTHR10502:SF26. PTHR10502:SF26. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14668-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRGTVTDF SGFDGRADAE VLRKAMKGLG TDEDSILNLL TARSNAQRQQ
60 70 80 90 100
IAEEFKTLFG RDLVNDMKSE LTGKFEKLIV ALMKPSRLYD AYELKHALKG
110 120 130 140 150
AGTDEKVLTE IIASRTPEEL RAIKQAYEEE YGSNLEDDVV GDTSGYYQRM
160 170 180 190 200
LVVLLQANRD PDTAIDDAQV ELDAQALFQA GELKWGTDEE KFITILGTRS
210 220 230 240 250
VSHLRRVFDK YMTISGFQIE ETIDRETSGN LENLLLAVVK SIRSIPAYLA
260 270 280 290 300
ETLYYAMKGA GTDDHTLIRV IVSRSEIDLF NIRKEFRKNF ATSLYSMIKG
310
DTSGDYKKAL LLLCGGEDD
Length:319
Mass (Da):35,745
Last modified:January 23, 2007 - v3
Checksum:i3B5D3AFDE8C3F32C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21730 mRNA. Translation: AAA41512.1.
D42137 Genomic DNA. Translation: BAA07708.1.
PIRiC29250. LURT5.
RefSeqiNP_037264.1. NM_013132.1.
UniGeneiRn.3318.

Genome annotation databases

GeneIDi25673.
KEGGirno:25673.
UCSCiRGD:2120. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21730 mRNA. Translation: AAA41512.1.
D42137 Genomic DNA. Translation: BAA07708.1.
PIRiC29250. LURT5.
RefSeqiNP_037264.1. NM_013132.1.
UniGeneiRn.3318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14668.
SMRiP14668. Positions 2-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247702. 2 interactions.
IntActiP14668. 1 interaction.
MINTiMINT-4996466.
STRINGi10116.ENSRNOP00000019552.

PTM databases

PhosphoSiteiP14668.

2D gel databases

World-2DPAGE0004:P14668.

Proteomic databases

PaxDbiP14668.
PRIDEiP14668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25673.
KEGGirno:25673.
UCSCiRGD:2120. rat.

Organism-specific databases

CTDi308.
RGDi2120. Anxa5.

Phylogenomic databases

eggNOGiNOG281174.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP14668.
KOiK16646.
PhylomeDBiP14668.

Miscellaneous databases

EvolutionaryTraceiP14668.
NextBioi607615.
PROiP14668.

Gene expression databases

GenevestigatoriP14668.

Family and domain databases

Gene3Di1.10.220.10. 4 hits.
InterProiIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
PANTHERiPTHR10502:SF26. PTHR10502:SF26. 1 hit.
PfamiPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSiPR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTiSM00335. ANX. 4 hits.
[Graphical view]
PROSITEiPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiANXA5_RAT
AccessioniPrimary (citable) accession number: P14668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.