ID A0A2U3VY04_ODORO Unreviewed; 864 AA.
AC A0A2U3VY04;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=PLA2G4E {ECO:0000313|RefSeq:XP_004400454.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004400454.1};
RN [1] {ECO:0000313|RefSeq:XP_004400454.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004400454.1; XM_004400397.1.
DR AlphaFoldDB; A0A2U3VY04; -.
DR STRING; 9708.A0A2U3VY04; -.
DR GeneID; 101386671; -.
DR KEGG; oro:101386671; -.
DR CTD; 123745; -.
DR InParanoid; A0A2U3VY04; -.
DR OrthoDB; 4250045at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005829; C:cytosol; 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; cd07201; cPLA2_Grp-IVB-IVD-IVE-IVF; 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:SF24; CYTOSOLIC PHOSPHOLIPASE A2 EPSILON; 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:UP000245340}.
FT DOMAIN 49..170
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 320..864
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 98994 MW; C6B66805D410EC8E CRC64;
MTRQSSEGCP GLGTDVFIPQ SLQETEEDSS SERNVSEFEH PQDPETPNLP PLLPIALWGS
QGGLSPCHLL TVKVIRMKNV RQADRVSQTD CFVSLWLPTA SRERLKTRTI SNCPNPEWNE
TFNFQIQSQV KNVLELSVCD EDTLTPDDHL LTILYDLTKL CFRKKTHVKF PLNPEGMEEL
EVEFLLEESP SPREILITNG VLVSRQVSRL EVHAECQRRK KSRKMKDLLV TVKESFEHTQ
RVSCCREPCC TNPACFHYPE YFQPCLHVDV PKNQWSRGLC CCCAHRKTSP VHQPLDCLPD
GQMVTLPVGE NCELHMKSTP CPQMLDVRLG FSLCPAEQEF LQKRKVVVAK ALQQVLQLEE
DLSADEVPLI AIMATGGGTR SMTAMYGHLL GLQKLNILNC ASYITGLSGA TWTMATLYRD
PNWSSKNLEP AIFEARRHVV KDKMPALFPD QLSKFQEELR QRGQEGYKVT FTDFWGLLVQ
ACLGDERNES KLSDQRAALC EGQNPLPIYL TINVKDDVSN QDFREWCEFS PYEVGLQKYG
AFIPTELFGS EFFMGRLMKR IPESRMCYML GLWSSIFSLN LLDAWNLSQS SEEFFHRWTR
ERVHDIEDEP LLPEIPKCDA NVLDTAVVIP GSWLSNTFRS ILTHRSFVSQ FHNFLLGLQL
HTDYLQNSQF SRWRDTVLDG FPNQLTESVK HLCLLDTAFF VNSSYPPLLR PERKVDLIIH
LNYCAGSQTK PIKQTCEYCT VQNIPFPKYE LQEDEENLKE CYLLENSQEP DAPIILFFPL
INDTFQKYKA PGVERSPEEL EQGHVDIYGP QTPYATKELT YTEAAFDKLV KLSEYNILNN
KDKLLQALRL AMEKKKHLKS ECPS
//
