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P48036

- ANXA5_MOUSE

UniProt

P48036 - ANXA5_MOUSE

Protein

Annexin A5

Gene

Anxa5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. negative regulation of coagulation Source: InterPro
    3. response to organic substance Source: MGI

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:106008. Anxa5.

    Subcellular locationi

    GO - Cellular componenti

    1. endothelial microparticle Source: BHF-UCL
    2. external side of plasma membrane Source: MGI
    3. extracellular vesicular exosome Source: Ensembl
    4. intracellular Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 319318Annexin A5PRO_0000067488Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei68 – 681N6-acetyllysine1 Publication
    Modified residuei74 – 741N6-acetyllysineBy similarity
    Modified residuei77 – 771N6-acetyllysineBy similarity
    Modified residuei95 – 951N6-acetyllysine1 Publication
    Modified residuei99 – 991N6-acetyllysineBy similarity
    Modified residuei288 – 2881N6-succinyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP48036.
    PaxDbiP48036.
    PRIDEiP48036.

    2D gel databases

    COMPLUYEAST-2DPAGEP48036.
    REPRODUCTION-2DPAGEIPI00317309.
    SWISS-2DPAGEP48036.

    PTM databases

    PhosphoSiteiP48036.

    Expressioni

    Gene expression databases

    BgeeiP48036.
    CleanExiMM_ANXA5.
    GenevestigatoriP48036.

    Interactioni

    Subunit structurei

    Monomer. Binds ATRX and EIF5B By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Kcnma1Q084604EBI-1184119,EBI-1633915

    Protein-protein interaction databases

    BioGridi198111. 2 interactions.
    IntActiP48036. 6 interactions.
    MINTiMINT-1869281.

    Structurei

    3D structure databases

    ProteinModelPortaliP48036.
    SMRiP48036. Positions 2-319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati22 – 8261Annexin 1Add
    BLAST
    Repeati94 – 15461Annexin 2Add
    BLAST
    Repeati178 – 23861Annexin 3Add
    BLAST
    Repeati253 – 31361Annexin 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.
    GeneTreeiENSGT00740000115434.
    HOGENOMiHOG000158803.
    HOVERGENiHBG061815.
    InParanoidiP48036.
    KOiK16646.
    OMAiWNKTLAN.
    OrthoDBiEOG74XS72.
    PhylomeDBiP48036.
    TreeFamiTF105452.

    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.

    P48036-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATRGTVTDF PGFDGRADAE VLRKAMKGLG TDEDSILNLL TSRSNAQRQE    50
    IAQEFKTLFG RDLVDDLKSE LTGKFEKLIV AMMKPSRLYD AYELKHALKG 100
    AGTDEKVLTE IIASRTPEEL SAIKQVYEEE YGSNLEDDVV GDTSGYYQRM 150
    LVVLLQANRD PDTAIDDAQV ELDAQALFQA GELKWGTDEE KFITIFGTRS 200
    VSHLRRVFDK YMTISGFQIE ETIDRETSGN LEQLLLAVVK SIRSIPAYLA 250
    ETLYYAMKGA GTDDHTLIRV VVSRSEIDLF NIRKEFRKNF ATSLYSMIKG 300
    DTSGDYKKAL LLLCGGEDD 319
    Length:319
    Mass (Da):35,752
    Last modified:February 1, 1996 - v1
    Checksum:i55055BAF2E1C36B7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti142 – 1421D → G in BAE28107. (PubMed:16141072)Curated
    Sequence conflicti157 – 1571A → G in AAH03716. (PubMed:15489334)Curated
    Sequence conflicti284 – 2841K → N in BAE31952. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001G → S in BAE32026. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29396 mRNA. Translation: AAC52530.1.
    D63423 mRNA. Translation: BAA09728.1.
    AJ230108
    , AJ230110, AJ230111, AJ230114, AJ230116, AJ230118, AJ230119, AJ230120, AJ230121, AJ230122, AJ230123, AJ230124 Genomic DNA. Translation: CAA13092.1.
    AK147740 mRNA. Translation: BAE28107.1.
    AK152185 mRNA. Translation: BAE31016.1.
    AK153388 mRNA. Translation: BAE31952.1.
    AK153476 mRNA. Translation: BAE32026.1.
    BC003716 mRNA. Translation: AAH03716.1.
    CCDSiCCDS38416.1.
    RefSeqiNP_033803.1. NM_009673.2.
    XP_006535439.1. XM_006535376.1.
    UniGeneiMm.1620.

    Genome annotation databases

    EnsembliENSMUST00000029266; ENSMUSP00000029266; ENSMUSG00000027712.
    GeneIDi11747.
    KEGGimmu:11747.
    UCSCiuc008ozj.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U29396 mRNA. Translation: AAC52530.1 .
    D63423 mRNA. Translation: BAA09728.1 .
    AJ230108
    , AJ230110 , AJ230111 , AJ230114 , AJ230116 , AJ230118 , AJ230119 , AJ230120 , AJ230121 , AJ230122 , AJ230123 , AJ230124 Genomic DNA. Translation: CAA13092.1 .
    AK147740 mRNA. Translation: BAE28107.1 .
    AK152185 mRNA. Translation: BAE31016.1 .
    AK153388 mRNA. Translation: BAE31952.1 .
    AK153476 mRNA. Translation: BAE32026.1 .
    BC003716 mRNA. Translation: AAH03716.1 .
    CCDSi CCDS38416.1.
    RefSeqi NP_033803.1. NM_009673.2.
    XP_006535439.1. XM_006535376.1.
    UniGenei Mm.1620.

    3D structure databases

    ProteinModelPortali P48036.
    SMRi P48036. Positions 2-319.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198111. 2 interactions.
    IntActi P48036. 6 interactions.
    MINTi MINT-1869281.

    PTM databases

    PhosphoSitei P48036.

    2D gel databases

    COMPLUYEAST-2DPAGE P48036.
    REPRODUCTION-2DPAGE IPI00317309.
    SWISS-2DPAGE P48036.

    Proteomic databases

    MaxQBi P48036.
    PaxDbi P48036.
    PRIDEi P48036.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029266 ; ENSMUSP00000029266 ; ENSMUSG00000027712 .
    GeneIDi 11747.
    KEGGi mmu:11747.
    UCSCi uc008ozj.2. mouse.

    Organism-specific databases

    CTDi 308.
    MGIi MGI:106008. Anxa5.

    Phylogenomic databases

    eggNOGi NOG281174.
    GeneTreei ENSGT00740000115434.
    HOGENOMi HOG000158803.
    HOVERGENi HBG061815.
    InParanoidi P48036.
    KOi K16646.
    OMAi WNKTLAN.
    OrthoDBi EOG74XS72.
    PhylomeDBi P48036.
    TreeFami TF105452.

    Miscellaneous databases

    NextBioi 279485.
    PROi P48036.
    SOURCEi Search...

    Gene expression databases

    Bgeei P48036.
    CleanExi MM_ANXA5.
    Genevestigatori P48036.

    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. "Mouse annexin V chromosomal localization, cDNA sequence conservation, and molecular evolution."
      Rodriguez-Garcia M.I., Kozak C.A., Morgan R.O., Fernandez M.-P.
      Genomics 31:151-157(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peritoneal cavity.
    2. Adachi T., Kojima K., Fukuoka S., Ogawa H., Matsumoto I.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Mouse annexin V genomic organization includes an endogenous retrovirus."
      Rodriguez-Garcia M.I., Morgan R.O., Fernandez M.R., Bances P., Fernandez M.-P.
      Biochem. J. 337:125-131(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
      Tissue: Liver.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Mammary gland.
    6. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 28-43; 62-74; 116-124; 192-199; 226-240 AND 275-283, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68 AND LYS-95, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiANXA5_MOUSE
    AccessioniPrimary (citable) accession number: P48036
    Secondary accession number(s): Q3U5Q1
    , Q3U5X4, Q3U8K1, Q3UGV0, Q99LA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3