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