ID A0A6Q2XWU5_ESOLU Unreviewed; 533 AA.
AC A0A6Q2XWU5;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000057581.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000057581.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000057581.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Putative phospholipase. {ECO:0000256|RuleBase:RU364138}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family.
CC {ECO:0000256|ARBA:ARBA00007835, ECO:0000256|RuleBase:RU364138}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A6Q2XWU5; -.
DR Ensembl; ENSELUT00000078534.1; ENSELUP00000057581.1; ENSELUG00000012500.2.
DR GeneTree; ENSGT00530000063509; -.
DR Proteomes; UP000265140; LG13.
DR Bgee; ENSELUG00000012500; Expressed in spleen and 15 other cell types or tissues.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.60.30; -; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR PANTHER; PTHR12370:SF3; PHOSPHOLIPASE B-LIKE 2-RELATED; 1.
DR PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364138};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU364138};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU364138};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364138}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT CHAIN 31..533
FT /note="Phospholipase B-like"
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT /id="PRO_5028523832"
SQ SEQUENCE 533 AA; 60263 MW; F5DEED5E3E00C708 CRC64;
MTDRRSHQLT TAMMAVFLCL LYLTWTSVRA EINSAFLDKD TGQLSLQEGF RDDYVAWGNF
TDDIENSGWA YLEVTTSGRY NDSIQAYAAG AVEADLTSQL IYKHWMNTLM GYCGPLTFES
GFCQRLKDYI NTNLEWVSQQ IEDHPNCPYW HQVQLALLQL KGLEDGYNNQ LSFPTGPFTF
NPFGFLLFQM GGDVEDLEGA LNKSSRSRTL GSGSCSAFIK LLPGNKDLLV SHDTWSNYQS
MLRILKKYMF SYHLSPTDSD PIPGGTQAFS SYPGSIYSGD DFYILSSGLV TMETTIGNSN
PSLWKFVQPT GAVMEWLRNI VANRLAANGK EWAEIFSKHN SGTYNNQWMI VDYKHFTPGM
TETKEQLFTV LEQIPGLVVH TDKTQQLLQK SYWSSYNIPF YEEVFNASGY RELVEQFGPW
FSIDMNPRAQ IFKRNQSHVT DMDSMVRLMR FNNFKQDPLS RCEGCDPPGN GENTISARSD
LNPANGTYPF GALKQRSHGG IDMKVRLFGC CNLLVCVCVC VCVTKCPNEC SNI
//
