ID H0VT58_CAVPO Unreviewed; 795 AA.
AC H0VT58;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
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=PLA2G4B {ECO:0000313|Ensembl:ENSCPOP00000013838.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000013838.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000013838.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000013838.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000256|ARBA:ARBA00023922};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000256|ARBA:ARBA00023922};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
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|ARBA:ARBA00023422};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000256|ARBA:ARBA00023422};
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 EMBL; AAKN02015908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013014224.1; XM_013158770.1.
DR AlphaFoldDB; H0VT58; -.
DR STRING; 10141.ENSCPOP00000013838; -.
DR Ensembl; ENSCPOT00000015502.3; ENSCPOP00000013838.3; ENSCPOG00000015353.4.
DR VEuPathDB; HostDB:ENSCPOG00000015353; -.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR eggNOG; KOG2508; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; H0VT58; -.
DR OMA; ECHAFSD; -.
DR TreeFam; TF325228; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000015353; Expressed in cerebellum and 13 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:0047498; F:calcium-dependent phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IEA:Ensembl.
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:SF32; CYTOSOLIC PHOSPHOLIPASE A2 BETA; 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:UP000005447}.
FT DOMAIN 1..123
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 258..795
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 795 AA; 90463 MW; 55E026B736516C15 CRC64;
MVSCRYHQGQ LRRKVKVPGT CLFIVRVLQA HGLPSKDLMS PSDCYVTLWL PTASSHRLRT
RTVKNSRDPV WNQTFRFRIH SQLKNILELK VFDQDLCTKD DAVLSVLFDA GTLQAGEFQR
QSFSLNTEGE MQLEVEFRLQ SLTDCAECLV SNGILVAREL SCLYVQLKEV GDREGSERRV
QLVVPGACEG MQEASKGTSS FLFHCLASWE QELSIHLQDD PQEQLKVPLQ TLPSGQLVKL
VFPTSQEPML RVELKKEEGP RELAVRLGSG PCTEEQAFLN RRKQVVATAL KQALQLDRDL
QEDEIPVVAI MATGGGIRAM TSLYGQLAGL KELGLLDCIS YITGASGSTW ALANLYEDPE
WSQKDLARPT ELLKTQVTKS KLGVLAPSKL WRYKQELAER TRLGHPPCFT NLWALINEAL
LHDGPHDHRL SDQREALSRG QNPLPIYCAL NTKEQSLTTF EFGEWCEFSP FEVGFPKYGA
FIPSELFGSE FFMGRLVKQL PESRICFLEG IWSNLYAANL QDSLYWSSDP SQFWDRWAQD
RANLDKEQVP HVKMEEPPTA AGRIAEFFTD LLTRRPLAQA THNFLHGLHF HKDYFHHPHF
STWKATKLDG FPNQLTPTEP HLCLLDVGYL INTSCLPLLQ PTRDVDLILS LDYNLHGAFQ
QLQLLDHFCK EQGIPFPHIS PSPEEQSHPQ ECHAFCDPTQ PEAPIVLHFP LVNDSFQEYS
APGVRRTPEE KAAGEVELSS TSSPYHYTKV TYSPEDTDKL LHLTRYNICN NRKQLLEALR
QAVQRRQLRR QHRPQ
//
