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ANXA3_BOVIN
ID   ANXA3_BOVIN             Reviewed;         323 AA.
AC   Q3SWX7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Annexin A3;
DE   AltName: Full=Annexin III;
DE   AltName: Full=Annexin-3;
GN   Name=ANXA3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant
CC       properties. Also cleaves the cyclic bond of inositol 1,2-cyclic
CC       phosphate to form inositol 1-phosphate (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; BC104614; AAI04615.1; -; mRNA.
DR   RefSeq; NP_001030402.1; NM_001035325.1.
DR   AlphaFoldDB; Q3SWX7; -.
DR   SMR; Q3SWX7; -.
DR   STRING; 9913.ENSBTAP00000042843; -.
DR   PaxDb; Q3SWX7; -.
DR   PeptideAtlas; Q3SWX7; -.
DR   PRIDE; Q3SWX7; -.
DR   GeneID; 518050; -.
DR   KEGG; bta:518050; -.
DR   CTD; 306; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   InParanoid; Q3SWX7; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
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; IPR002390; ANX3.
DR   PANTHER; PTHR10502:SF25; PTHR10502:SF25; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00199; ANNEXINIII.
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; Calcium; Calcium/phospholipid-binding;
KW   Phospholipase A2 inhibitor; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P12429"
FT   CHAIN           2..323
FT                   /note="Annexin A3"
FT                   /id="PRO_0000236217"
FT   REPEAT          18..89
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          90..161
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          173..245
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          249..320
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P12429"
FT   MOD_RES         177
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35639"
FT   MOD_RES         267
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14669"
SQ   SEQUENCE   323 AA;  36140 MW;  04A4CDB623A5A54A CRC64;
     MASIWVGKRG TIRDYAGFNP SVDAEAIRKA IRGIGTDEKT LISILTERTN AQRLLIAKEY
     QALCGKELKD DLKGDLSGHF KHLMVALVTP PAVFDAKQLK KSMKGMGTNE DALIEILTTR
     TSKQMQEIGH AYYTAYKKSL GDEISSETSG DFRKALLILA NGRRDESLKV DEQLARKDAQ
     ILYNAGEKRW GTDEDAFTNI LCLRSFPQLK LTFDEYRNIS QKDIEDSIKG ELSGHFEDLL
     LAIVRCARNT PAFLAERLYR ALKGAGTDEF TLNRIMVSRS EIDLLDIRAE FKKLSGYSLY
     SAIKSDTSGD YEITLLKICG GDD
 
 
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