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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//