ID G3QDN8_GORGO Unreviewed; 781 AA.
AC G3QDN8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:ENSGGOP00000000362.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000362.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000000362.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000000362.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000000362.2}
RP IDENTIFICATION.
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=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; CABD030095711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030095720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3QDN8; -.
DR STRING; 9593.ENSGGOP00000000362; -.
DR Ensembl; ENSGGOT00000000371.3; ENSGGOP00000000362.2; ENSGGOG00000011737.3.
DR GeneTree; ENSGT01030000234606; -.
DR InParanoid; G3QDN8; -.
DR OMA; ECHAFSD; -.
DR Proteomes; UP000001519; Chromosome 15.
DR Bgee; ENSGGOG00000011737; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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:UP000001519}.
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 246..781
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 781 AA; 87947 MW; FCC42B388136D299 CRC64;
MAVAEVSRTC LLTVRVLQAH RLPSKDLVTP SDCYVTLWLP TACSHRLQTR TVKNSSSPVW
NQSFHFRIHR QLKNVVELKV FDQDLVTGDD PVLSVLFDAG TLRAGEFRRE SFSLSPQGEG
CLEVEFRLQS LADRGEWLVS NGVLVAWELS CLHVQLEETG DQKSSERRVQ LVVPGSCEGP
QEASVGTGTF HFHCPACWEQ ELSIHLQDAP EEQLKVPLSA LPSGQVVRLV FPTSQEPLMR
VELNKEAGLR ELAVRLGFGP CAEEQAFLSR RKQVVAAALR QALQLDGDLQ EDEIPVVAIM
ATGGGIRAMT SLYGQLAGLK ELGLLDCLSY ITGASGSTWA LANLYEDPEW SQKDLAGPTE
LLKTQVTKNK LGVLAPSQLQ RYRQELAERA RLGYPSCFTN LWALISEALL HDEPHDHKLS
DQREALSHGQ NPLPIYCALN TKGQSLTTFE FGEWCEFSPY EVGFPKYGAF IPSELFGSEF
FMGQLMKRLP ESRICFLEGI WSNLYAANLQ DSLYWASEPS QFWDRWVRNQ ANLDKEQVPL
LKIEEPPSTA GRIAEFFTDL LTWRPLAQAT HNFLRGLHFH KDYFQHPHFS TWKATTLDGL
PNQLTPSEPH LCLLDVGYLI NTSCLPLLQP TRDVDLILSL DYNLHGAFQQ LQLLGRFCQE
QGIPFPPISP SPEEQLQPRE CHTFSDPTCP VAPAVLHFPL VSDSFREYSA PGVRRTPEEA
AAGEVNLSSS DSPYHYTKVT YSQEDVDKLL HLTHYNVCNN QEQLLEALRQ AVQRRRQRRP
H
//
