UniProt: A0A1V4JZG2

Database: UniProt
Entry: A0A1V4JZG2_PATFA

LinkDB:  A0A1V4JZG2_PATFA 
Original site:  A0A1V4JZG2_PATFA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (2)   
   SMART (2)   
All databases (17)   

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ID   A0A1V4JZG2_PATFA        Unreviewed;       749 AA.
AC   A0A1V4JZG2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|RuleBase:RU362102};
GN   Name=PLA2G4A {ECO:0000313|EMBL:OPJ77534.1};
GN   ORFNames=AV530_019785 {ECO:0000313|EMBL:OPJ77534.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ77534.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ77534.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ77534.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ77534.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU362102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. {ECO:0000256|RuleBase:RU362102}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ77534.1}.
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DR   EMBL; LSYS01005418; OPJ77534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4JZG2; -.
DR   STRING; 372326.A0A1V4JZG2; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd04036; C2_cPLA2; 1.
DR   CDD; cd07200; cPLA2_Grp-IVA; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR041847; C2_cPLA2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF13; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU362102};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362102};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU00555,
KW   ECO:0000256|RuleBase:RU362102};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648}.
FT   DOMAIN          6..124
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          138..740
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
FT   REGION          432..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  85129 MW;  422129D963D58C4B CRC64;
     MSIIDPYQHI VVEHQYSHIF TVTVRKATNV TKGAFGDMLD TPDPYVELFI PSAPDCRKRT
     KHFNNDVNPV WDETFEFILD PNQDNILEVT LMDANYVMDE TLGTSTFPIS SLKLGEKKEV
     QLTFNDVTEM TLELSLEVCS STDLRFSMAL CDEEKKFRQQ RKENIMHSMK SFLGEENSKN
     LTSSRDVPVI AVLGSGGGFR AMVGFAGVMK ALYESGVLDC ATYVAGLSGS TWYMSTLYSH
     PDFPEKGPKE INQELMNSVS HNPLLLLTPQ KVKRYIEALW NKKSSGQPVT FTDIFGMLIG
     ETLIHNRMDT TLSDMKEKIS HAQCALPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
     TFMSPDLFGS KFFMGTVVKK YNENPLHFLM GVWGSAFSIL FNRVLGVSNS QNKGPTMEEE
     LENIRLKHLI SNDSSDSEDE SQHPKGTENT EANQEYQNSS QESWVQRMLM ALVGDSALFN
     TREGRAGKVH NFMLGLNLNS CYPLSPLADL LSQESVEEDE LDAAVADPDE FERIYEPLDV
     KSKKIHIVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEI LLAEKWAKMN
     KLPFPKIDPN VFDREGLKEC YVFKPKDTSS EKDCPTIIHF VLANINFRKY KAPGVPRETQ
     EEKDFADFDI FDDPNTPFST FNFQYPNEAF KRLHDLMEFN TLNNIDVIKQ AMMESIEYRK
     ENPSRCSVSL SSVEARRFFN KTNLNNNLT
//

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