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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

  • calcium-dependent phospholipid binding Source: RGD
  • calcium ion binding Source: InterPro
  • calcium-transporting ATPase activity Source: RGD
  • peptide hormone binding Source: RGD
  • receptor tyrosine kinase binding Source: RGD

GO - Biological processi

  • blood coagulation Source: UniProtKB-KW
  • cellular response to gonadotropin-releasing hormone Source: RGD
  • cellular response to lead ion Source: RGD
  • negative regulation of blood coagulation Source: RGD
  • negative regulation of prolactin secretion Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • protein homooligomerization Source: RGD
  • regulation of flagellated sperm motility Source: RGD
  • response to calcium ion Source: RGD
  • response to thyroid hormone 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2120. Anxa5.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: RGD
  • cell projection Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • dendrite Source: RGD
  • endoplasmic reticulum Source: RGD
  • extracellular space Source: RGD
  • intercalated disc Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
  • plasma membrane Source: RGD
  • sarcolemma Source: RGD
  • synaptic vesicle Source: RGD
  • Z disc Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000674902 – 319Annexin A5Add BLAST318

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei35PhosphoserineCombined sources1
Modified residuei68N6-acetyllysineBy similarity1
Modified residuei74N6-acetyllysineBy similarity1
Modified residuei77N6-acetyllysineBy similarity1
Modified residuei95N6-acetyllysineBy similarity1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei288N6-succinyllysineBy similarity1

Post-translational modificationi

S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDbiP14668.
PRIDEiP14668.

2D gel databases

World-2DPAGE0004:P14668.

PTM databases

iPTMnetiP14668.
PhosphoSitePlusiP14668.

Interactioni

Subunit structurei

Monomer. Binds ATRX, EIF5B and DNMT1.

GO - Molecular functioni

  • receptor tyrosine kinase binding Source: RGD

Protein-protein interaction databases

BioGridi247702. 2 interactors.
IntActiP14668. 1 interactor.
MINTiMINT-4996466.
STRINGi10116.ENSRNOP00000019552.

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 26Combined sources12
Beta strandi27 – 30Combined sources4
Helixi33 – 40Combined sources8
Helixi45 – 59Combined sources15
Helixi63 – 70Combined sources8
Helixi73 – 83Combined sources11
Helixi86 – 97Combined sources12
Helixi100 – 102Combined sources3
Helixi105 – 114Combined sources10
Helixi117 – 131Combined sources15
Helixi135 – 142Combined sources8
Helixi145 – 155Combined sources11
Helixi167 – 180Combined sources14
Turni181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Helixi189 – 198Combined sources10
Helixi201 – 215Combined sources15
Helixi219 – 226Combined sources8
Helixi229 – 243Combined sources15
Helixi245 – 257Combined sources13
Beta strandi258 – 261Combined sources4
Helixi264 – 274Combined sources11
Turni275 – 278Combined sources4
Helixi279 – 290Combined sources12
Helixi294 – 301Combined sources8
Helixi304 – 314Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14668.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati21 – 81Annexin 1Add BLAST61
Repeati93 – 153Annexin 2Add BLAST61
Repeati177 – 237Annexin 3Add BLAST61
Repeati252 – 312Annexin 4Add BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi312 – 318[IL]-x-C-x-x-[DE] motifBy similarity7

Domaini

A pair of annexin repeats may form one binding site for calcium and phospholipid.
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Annexin, Repeat

Phylogenomic databases

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247702. 2 interactors.
IntActiP14668. 1 interactor.
MINTiMINT-4996466.
STRINGi10116.ENSRNOP00000019552.

PTM databases

iPTMnetiP14668.
PhosphoSitePlusiP14668.

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

eggNOGiKOG0819. Eukaryota.
ENOG410XPUN. LUCA.
HOGENOMiHOG000158803.
HOVERGENiHBG061815.
InParanoidiP14668.
KOiK16646.
PhylomeDBiP14668.

Miscellaneous databases

EvolutionaryTraceiP14668.
PROiP14668.

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...

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: November 2, 2016
This is version 151 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

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 one 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.