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P14668

- ANXA5_RAT

UniProt

P14668 - ANXA5_RAT

Protein

Annexin A5

Gene

Anxa5

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: RGD
    5. 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

    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

    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. 1 interaction.
    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 – 2612
    Beta strandi27 – 304
    Helixi33 – 408
    Helixi45 – 5915
    Helixi63 – 708
    Helixi73 – 8311
    Helixi86 – 9712
    Helixi100 – 1023
    Helixi105 – 11410
    Helixi117 – 13115
    Helixi135 – 1428
    Helixi145 – 15511
    Helixi167 – 18014
    Turni181 – 1833
    Beta strandi184 – 1863
    Helixi189 – 19810
    Helixi201 – 21515
    Helixi219 – 2268
    Helixi229 – 24315
    Helixi245 – 25713
    Beta strandi258 – 2614
    Helixi264 – 27411
    Turni275 – 2784
    Helixi279 – 29012
    Helixi294 – 3018
    Helixi304 – 31411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MALRGTVTDF SGFDGRADAE VLRKAMKGLG TDEDSILNLL TARSNAQRQQ    50
    IAEEFKTLFG RDLVNDMKSE LTGKFEKLIV ALMKPSRLYD AYELKHALKG 100
    AGTDEKVLTE IIASRTPEEL RAIKQAYEEE YGSNLEDDVV GDTSGYYQRM 150
    LVVLLQANRD PDTAIDDAQV ELDAQALFQA GELKWGTDEE KFITILGTRS 200
    VSHLRRVFDK YMTISGFQIE ETIDRETSGN LENLLLAVVK SIRSIPAYLA 250
    ETLYYAMKGA GTDDHTLIRV IVSRSEIDLF NIRKEFRKNF ATSLYSMIKG 300
    DTSGDYKKAL LLLCGGEDD 319
    Length:319
    Mass (Da):35,745
    Last modified:January 23, 2007 - v3
    Checksum:i3B5D3AFDE8C3F32C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21730 mRNA. Translation: AAA41512.1 .
    D42137 Genomic DNA. Translation: BAA07708.1 .
    PIRi C29250. LURT5.
    RefSeqi NP_037264.1. NM_013132.1.
    UniGenei Rn.3318.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8A X-ray 1.90 A 2-319 [» ]
    1A8B X-ray 1.90 A 2-319 [» ]
    1BC0 X-ray 2.00 A 1-319 [» ]
    1BC1 X-ray 2.05 A 1-319 [» ]
    1BC3 X-ray 1.95 A 1-319 [» ]
    1BCW X-ray 2.10 A 1-319 [» ]
    1BCY X-ray 1.95 A 1-319 [» ]
    1BCZ X-ray 2.20 A 1-319 [» ]
    1G5N X-ray 1.90 A 2-319 [» ]
    1N41 X-ray 2.10 A 1-319 [» ]
    1N42 X-ray 2.10 A 1-319 [» ]
    1N44 X-ray 3.00 A 1-319 [» ]
    2H0K X-ray 2.76 A/B 2-319 [» ]
    2H0L X-ray 2.59 A 2-319 [» ]
    2H0M X-ray 2.26 A 1-318 [» ]
    2IE6 X-ray 1.83 A 2-319 [» ]
    2IE7 X-ray 1.75 A 2-319 [» ]
    2RAN X-ray 1.89 A 2-317 [» ]
    ProteinModelPortali P14668.
    SMRi P14668. Positions 2-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247702. 1 interaction.
    IntActi P14668. 1 interaction.
    MINTi MINT-4996466.
    STRINGi 10116.ENSRNOP00000019552.

    PTM databases

    PhosphoSitei P14668.

    2D gel databases

    World-2DPAGE 0004:P14668.

    Proteomic databases

    PaxDbi P14668.
    PRIDEi P14668.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25673.
    KEGGi rno:25673.
    UCSCi RGD:2120. rat.

    Organism-specific databases

    CTDi 308.
    RGDi 2120. Anxa5.

    Phylogenomic databases

    eggNOGi NOG281174.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P14668.
    KOi K16646.
    PhylomeDBi P14668.

    Miscellaneous databases

    EvolutionaryTracei P14668.
    NextBioi 607615.
    PROi P14668.

    Gene expression databases

    Genevestigatori P14668.

    Family and domain databases

    Gene3Di 1.10.220.10. 4 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR015473. Annexins_V.
    IPR002392. AnnexinV.
    [Graphical view ]
    PANTHERi PTHR10502:SF26. PTHR10502:SF26. 1 hit.
    Pfami PF00191. Annexin. 4 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00201. ANNEXINV.
    SMARTi SM00335. ANX. 4 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 133 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