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P24551

- ANXA1_RODSP

UniProt

P24551 - ANXA1_RODSP

Protein

Annexin A1

Gene

ANXA1

Organism
Rodentia sp.
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity By similarity.By similarity

    GO - Molecular functioni

    1. calcium-dependent phospholipid binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. phospholipase A2 inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Phospholipase A2 inhibitor

    Keywords - Ligandi

    Calcium, Calcium/phospholipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Annexin A1
    Alternative name(s):
    Annexin I
    Annexin-1
    Calpactin II
    Calpactin-2
    Lipocortin I
    Gene namesi
    Name:ANXA1
    Synonyms:ANX1
    OrganismiRodentia sp.
    Taxonomic identifieri69158 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaunclassified Rodentia

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Cell projectioncilium By similarity. Basolateral cell membrane By similarity
    Note: Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium. Found in the cytoplasm of type II pneumocytes and alveolar macrophages.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: UniProtKB-SubCell
    2. cilium Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 346345Annexin A1PRO_0000067465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei5 – 51Phosphoserine; by TRPM7By similarity
    Cross-linki19 – 19Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity
    Modified residuei21 – 211Phosphotyrosine; by EGFRBy similarity
    Modified residuei27 – 271Phosphoserine; by PKCBy similarity
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei312 – 3121N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein

    Interactioni

    Subunit structurei

    Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP24551.
    SMRiP24551. Positions 2-344.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati51 – 11161Annexin 1Add
    BLAST
    Repeati123 – 18361Annexin 2Add
    BLAST
    Repeati207 – 26761Annexin 3Add
    BLAST
    Repeati282 – 34261Annexin 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

    HOVERGENiHBG061815.

    Family and domain databases

    Gene3Di1.10.220.10. 4 hits.
    InterProiIPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002388. AnnexinI.
    [Graphical view]
    PfamiPF00191. Annexin. 4 hits.
    [Graphical view]
    PRINTSiPR00196. ANNEXIN.
    PR00197. ANNEXINI.
    SMARTiSM00335. ANX. 4 hits.
    [Graphical view]
    PROSITEiPS00223. ANNEXIN. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24551-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMVSEFINQ ACYLEKQEQE YIEIVKSYKG GPAHAVSPYP SFDPSSDVAA    50
    LHKGIMVNGV DEATILDLLT KRYNAQRHHL KAVYIQETGE PLDETLKKAL 100
    TGHIQELLLA MIKTPAQFDG NELRAAMKAV GTDEETLIEI LWTRSNQQIR 150
    EITSVYREEL KKDIAKYQTS DTSGEFRDAL LALAKGNRCE DMSVNQDIAD 200
    TDARALYQAA ERRNGTDVNV FNTILTTKKY PHLRNKFQNY RKYTEEDMKK 250
    ALDIELKGQI EKCLTTIAKC GTSTPAFFAE KLYEAMKGAG TRHKTLIRIM 300
    VSRSEIDSDQ IKVFYQKKYG VPLCQAILDE TKGAYEKILV ALEGGN 346
    Length:346
    Mass (Da):39,053
    Last modified:January 23, 2007 - v3
    Checksum:i99930C41B682D12F
    GO

    Sequence databases

    PIRiS13044. LUJP1.

    Cross-referencesi

    Sequence databases

    PIRi S13044. LUJP1.

    3D structure databases

    ProteinModelPortali P24551.
    SMRi P24551. Positions 2-344.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG061815.

    Family and domain databases

    Gene3Di 1.10.220.10. 4 hits.
    InterProi IPR001464. Annexin.
    IPR018502. Annexin_repeat.
    IPR018252. Annexin_repeat_CS.
    IPR002388. AnnexinI.
    [Graphical view ]
    Pfami PF00191. Annexin. 4 hits.
    [Graphical view ]
    PRINTSi PR00196. ANNEXIN.
    PR00197. ANNEXINI.
    SMARTi SM00335. ANX. 4 hits.
    [Graphical view ]
    PROSITEi PS00223. ANNEXIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges."
      Robitzki A., Schroeder H.C., Ugarkovic D., Gramzow M., Fritsche U., Batel R., Mueller W.E.G.
      Biochem. J. 271:415-420(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Duret L.
      Unpublished observations (FEB-1996)
      Cited for: DOUBTS ON BIOLOGICAL SOURCE OF PROTEIN.
    3. Mueller W.E.G.
      Unpublished observations (APR-1996)
      Cited for: AGREEMENT WITH RODENT CONTAMINATION.

    Entry informationi

    Entry nameiANXA1_RODSP
    AccessioniPrimary (citable) accession number: P24551
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to originate from the sponge Geodia cydonium, but, on the basis of phylogenetic studies (1 Publication) it seems very probable that the DNA sequence coding for this protein comes from a rodent as agreed by the original authors ().1 Publication

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3