ID S4R5E3_PETMA Unreviewed; 141 AA.
AC S4R5E3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Phospholipase A1 member A {ECO:0000256|ARBA:ARBA00040696};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000000423.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000000423.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC ChEBI:CHEBI:77342; Evidence={ECO:0000256|ARBA:ARBA00036960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC Evidence={ECO:0000256|ARBA:ARBA00036960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000256|ARBA:ARBA00000834};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000256|ARBA:ARBA00000834};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC Evidence={ECO:0000256|ARBA:ARBA00036542};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC Evidence={ECO:0000256|ARBA:ARBA00036542};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701, ECO:0000256|RuleBase:RU004262}.
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DR AlphaFoldDB; S4R5E3; -.
DR STRING; 7757.ENSPMAP00000000423; -.
DR Ensembl; ENSPMAT00000000424.1; ENSPMAP00000000423.1; ENSPMAG00000000381.1.
DR GeneTree; ENSGT00940000159279; -.
DR HOGENOM; CLU_027171_8_2_1; -.
DR OMA; TICKXSS; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; LIPASE; 1.
DR PANTHER; PTHR11610:SF111; PHOSPHOLIPASE A1 MEMBER A; 1.
DR Pfam; PF00151; Lipase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245300};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 15..140
FT /note="Lipase"
FT /evidence="ECO:0000259|Pfam:PF00151"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 141 AA; 15125 MW; 45C385878A602011 CRC64;
MVGRLCGGQQ RPVQHNVTSL DPASPGFSQV GPAERLDPSD AAFVDAIHTD GDNFGLRQPV
GHVDFYVNGG DDQPGCGGFD HHAGYQSMIC DHMRAVRLWL SSLRSPCELR AFPCDSVAAL
AAGRCLECRT ERTASCPRLG L
//
