ID A0A455BTV1_PHYMC Unreviewed; 1082 AA.
AC A0A455BTV1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC102990390 {ECO:0000313|RefSeq:XP_028351243.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028351243.1};
RN [1] {ECO:0000313|RefSeq:XP_028351243.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028351243.1};
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_028351243.1; XM_028495442.2.
DR AlphaFoldDB; A0A455BTV1; -.
DR InParanoid; A0A455BTV1; -.
DR OrthoDB; 4250045at2759; -.
DR Proteomes; UP000248484; Chromosome 11.
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 Gene3D; 2.60.120.10; Jelly Rolls; 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; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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; PF13621; Cupin_8; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51184; JMJC; 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:UP000248484}.
FT DOMAIN 128..334
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 292..413
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 548..1082
FT /note="PLA2c"
FT /evidence="ECO:0000259|PROSITE:PS51210"
SQ SEQUENCE 1082 AA; 121699 MW; ECC9093D2BE8A667 CRC64;
MADAALDAVR RELREFPAAA RELSVPLAVP YLDKPPGPLH FYRDWVCPNR PCIIRNALQH
WPALQKWSLP YLRATAGSAE VSVAVTPDGY ADAVRGDRFV MPAERRLPLS CVLDVLEGRA
QHPGVLYVQK QCSNLLTELP QLLPDLEPHV PWASEALGKM PDAVNFWLGE AAAVTSLHKD
HYENLYCVVS GEKHFLLHPP SDRPFIPYEL YTPASYQLSE EGSFKMVDEE TMEKVPWIPL
DPLAPDLAQY PSYSQAQALH CTVQTGEMLY LPALWFHHVQ QSHGCMAGAA RHSFLLRILC
LMALAKVPGT CLLTIHVLQA HGLPSKDLVT ASDCYVTLWL PSASSHQVQT RVVKNSRNPI
WNQSFHFRIH SQLKNIVQLQ VFDQDLLTQD DPLLSVLFDV GTLQAGESRR ESFSLNPQGK
EQLEVEFRLQ NLTGCAERLV SNGILVAREL SCLHVRLEKA GDQQGLEGGV QLVVPGSCEG
PQEASVGAGS FRFHWPACWE QELSIHLQDA PQEQLKVPLR ALPSDQVVRL VFPTSQDPLM
KVELKKEEGP RELAVRLDCG PCAEERAFLS RRKQVVAKAL KQALQLDGDL QEDEIPVVAV
MATGGGIRAM TSLYGQLAGL KELGLLDCIS CITGASGSTW ALANLYEDPE WSQKDLAGPI
ESLKMQVTKS KLGVLAPSQL WRYRQELAER ACLGHPTCFT TLWALINEAL LHDEPHNHKL
SDQREALSRG QNPLPIYCAL NTKERNLTTF EFGEWCEFSP YEVGFPKYGA FIPSELFGSE
FFMGRLTKRL PESRICFLEG IWSNLYAASL QDSLYWASEP SQFWDRWAQA QASLDKEQVP
LLNIEEPPTV ASRIAEFFTD LLTWRPLAQA THNFLRGLSF HKDYFQHPHF SAWKATKLDG
LPNQLTPAEP FLCLLDVGYL VNTSCPPLLR PTRDVDLILS LDYNLDGAFQ QLQLLDRFCQ
EQGIPFPSIS PSPEEQRQPR ECHLFSDPAR PDAPAVLHFP LVNASFREHS APGVRRTAEA
QEAGEVNLSS SDSPYHYLKV TYSREDMDKL LRLTHYNICN NQEQLLEALR EAVRRRKQRR
AE
//
