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ANXA2_CEREL
ID   ANXA2_CEREL             Reviewed;         339 AA.
AC   Q2Q1M6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Annexin A2;
DE   AltName: Full=Annexin-2;
GN   Name=ANXA2; Synonyms=ANX2;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=17131158; DOI=10.1007/s00438-006-0193-x;
RA   Molnar A., Gyurjan I., Korpos E., Borsy A., Steger V., Buzas Z., Kiss I.,
RA   Zomborszky Z., Papp P., Deak F., Orosz L.;
RT   "Identification of differentially expressed genes in the developing antler
RT   of red deer Cervus elaphus.";
RL   Mol. Genet. Genomics 277:237-248(2007).
CC   -!- FUNCTION: Calcium-regulated membrane-binding protein whose affinity for
CC       calcium is greatly enhanced by anionic phospholipids. It binds two
CC       calcium ions with high affinity. May be involved in heat-stress
CC       response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces
CC       PCSK9 protein levels via a translational mechanism but also competes
CC       with LDLR for binding with PCSK9. {ECO:0000250|UniProtKB:P07355}.
CC   -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC       heavy chains of ANXA2/p36 (By similarity). Interacts with ATP1B1 (By
CC       similarity). Interacts with DYSF (By similarity). Interacts with COCH.
CC       Interacts (via repeat Annexin 1) with PCSK9 (via the C-terminal
CC       domain); the interaction inhibits the degradation of LDLR. Interacts
CC       with CEACAM1 (via the cytoplasmic domain); this interaction is
CC       regulated by phosphorylation of CEACAM1 (By similarity). Interacts with
CC       APPL2 and APPL1; targets APPL2 to endosomes and acting in parallel to
CC       RAB5A (By similarity). Interacts with S100A4 (By similarity).
CC       {ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07355,
CC       ECO:0000250|UniProtKB:P07356, ECO:0000250|UniProtKB:Q6TEQ7}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=In the lamina beneath the plasma
CC       membrane. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed strongly in velvet antler reserve
CC       mesenchyme. {ECO:0000269|PubMed:17131158}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- PTM: ISGylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids with
CC       actin and the cytoskeleton and be involved with exocytosis.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86 of
CC       September 2007;
CC       URL="https://web.expasy.org/spotlight/back_issues/086";
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DR   EMBL; DQ239920; ABB77206.1; -; mRNA.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0004859; F:phospholipase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.10.220.10; -; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR002389; ANX2.
DR   PANTHER; PTHR10502:SF18; PTHR10502:SF18; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00198; ANNEXINII.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   2: Evidence at transcript level;
KW   Acetylation; Annexin; Basement membrane; Calcium;
KW   Calcium/phospholipid-binding; Extracellular matrix; Isopeptide bond;
KW   Phosphoprotein; Repeat; Secreted; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P04272"
FT   CHAIN           2..339
FT                   /note="Annexin A2"
FT                   /id="PRO_0000288685"
FT   REPEAT          33..104
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          105..176
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          189..261
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          265..336
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REGION          2..24
FT                   /note="S100A10-binding site"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04272"
FT   MOD_RES         24
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P07355"
FT   MOD_RES         26
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P07355"
FT   MOD_RES         49
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07356"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07356"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07355"
FT   MOD_RES         199
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P07356"
FT   MOD_RES         227
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P07356"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07355"
FT   CROSSLNK        49
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P07355"
SQ   SEQUENCE   339 AA;  38621 MW;  A22C3DA3F6829FEF CRC64;
     MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL
     TNRSNEQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
     LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDIV SDTSGDFRKL MVALAKGRRA
     EDGSVIDYEL IDQDARDLYD AGVKXKXTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM
     LESIKKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
     LKIRSEFKKK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
 
 
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