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Database: UniProt
Entry: F6TFZ5_XENTR
LinkDB: F6TFZ5_XENTR
Original site: F6TFZ5_XENTR 
ID   F6TFZ5_XENTR            Unreviewed;       856 AA.
AC   F6TFZ5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Phospholipase A2 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
DE            EC=3.1.1.4 {ECO:0000256|ARBA:ARBA00013278, ECO:0000256|RuleBase:RU362102};
GN   Name=pla2g4f {ECO:0000313|Ensembl:ENSXETP00000000594,
GN   ECO:0000313|RefSeq:XP_002932885.3,
GN   ECO:0000313|Xenbase:XB-GENE-6042177};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000000594};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000000594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000000594};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000000594}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_002932885.3}
RP   IDENTIFICATION.
RC   STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002932885.3};
RC   TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002932885.3};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC       calcium binding. {ECO:0000256|RuleBase:RU362102}.
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DR   RefSeq; XP_002932885.3; XM_002932839.5.
DR   Ensembl; ENSXETT00000000594; ENSXETP00000000594; ENSXETG00000000299.
DR   KEGG; xtr:100497525; -.
DR   AGR; Xenbase:XB-GENE-6042177; -.
DR   Xenbase; XB-GENE-6042177; pla2g4f.
DR   eggNOG; KOG1028; Eukaryota.
DR   eggNOG; KOG1325; Eukaryota.
DR   HOGENOM; CLU_011663_0_0_1; -.
DR   OMA; PFEVLHQ; -.
DR   TreeFam; TF325228; -.
DR   Reactome; R-XTR-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-XTR-1482801; Acyl chain remodelling of PS.
DR   Reactome; R-XTR-1482839; Acyl chain remodelling of PE.
DR   Reactome; R-XTR-1482922; Acyl chain remodelling of PI.
DR   Reactome; R-XTR-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-XTR-1483115; Hydrolysis of LPC.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Bgee; ENSXETG00000000299; Expressed in blastula and 10 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   CDD; cd04036; C2_cPLA2; 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; IPR040723; cPLA2_C2.
DR   InterPro; IPR002642; LysoPLipase_cat_dom.
DR   PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR   PANTHER; PTHR10728:SF22; CYTOSOLIC PHOSPHOLIPASE A2 ZETA; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF18695; cPLA2_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:UP000008143}.
FT   DOMAIN          32..150
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          308..856
FT                   /note="PLA2c"
FT                   /evidence="ECO:0000259|PROSITE:PS51210"
SQ   SEQUENCE   856 AA;  96833 MW;  B35C11A2B1D1A66A CRC64;
     MFQAVVTRFS SRALPALAAV LLRRNERGEK EARRERRPKS WRKEVHPYYN LSVTVLGAKN
     IHGADLLSKA DCYVQLRLPT ASPLASRTAV VYNSSDPEWN ETFKYRIHGA VKNILELTLY
     DRDVVLDDKL SSVVFDIGHI KPGHSSKRVF KLGPKESLEV EFSLEKSKEP PTQIITNGVL
     VAHPCLCVHG NIHRGGDLNS PRGNQMLQLS MPGSYEKQIC TPFSSLSSQE QGAPFVFHAD
     KDIAPQLNVH LLKTVRLGEN DLDPELEKQI LLVGESSVPV SSLPEGKEQG INLQLSKDHS
     LEMNVTTEED NRELDIRLGF ELSLGEREYL EKRKKVAARC LQEVLKLDST SSVNEVPVVA
     VLGSGGGTRA MTSFYGSLLG LQELKLLDSV TYISGVSGST WCMSTLYEDP DWSQKSVQDP
     ISRARKSVTA SKSGAFSAER LKRCTQELIA MEKDGHMVNF TDLWGLVIEY FLHQKENPAK
     LSDQQACVSK SQNPYPIYAG VNVRVDINGG DFAEWCEFTP HEVGFRKYGA FVRTEDCGSE
     FFMGHLIHRR KEPKICYLQG IWGSAFAANL DEIWAHAAGT GIRWLSSLTD AIRVIDDCRK
     LHWRDSSRLK TRLVMPGGFV SNMFQEIFKS RFTAGEWYNF TRGLYLYKDY LGVREFLAWK
     GTHLDAFPNQ LTPMEESLYL VDGGFSINSP FPLVLQPERD VDVILSFNYS WGAPFEVLHL
     TSTYCRERGI PFPEITLTNE DEKQPKECYV FMDHNNPRAP IVLHFPMVNN TFRTFIEPGV
     ERKTEEEKLN GEVDLTGKES PFRTKNFTYE PQHFDRLVAV NRYNVLNSRE QIAAALKAAV
     ARRKDKSTKL PSKKHM
//
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