ID I3LCG5_PIG Unreviewed; 544 AA.
AC I3LCG5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN Name=PLBD1 {ECO:0000313|Ensembl:ENSSSCP00000021740.2};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000021740.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000021740.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000021740.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDC62265.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000021740.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR EMBL; DQIR01306787; HDC62265.1; -; Transcribed_RNA.
DR RefSeq; NP_001231558.1; NM_001244629.1.
DR PaxDb; 9823-ENSSSCP00000021740; -.
DR Ensembl; ENSSSCT00000032057.4; ENSSSCP00000021740.2; ENSSSCG00000057970.1.
DR GeneID; 100155493; -.
DR KEGG; ssc:100155493; -.
DR CTD; 79887; -.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_1003043_0_0_1; -.
DR OrthoDB; 180150at2759; -.
DR ChiTaRS; PLBD1; pig.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000026724; Expressed in ovary and 41 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.60.20; -; 1.
DR Gene3D; 2.10.70.60; Phospholipase B-like, domain 1; 1.
DR Gene3D; 1.10.439.20; Phospholipase B-like, domain 2; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR InterPro; IPR043040; PLipase_B-like_dom1.
DR InterPro; IPR043041; PLipase_B-like_dom2.
DR InterPro; IPR043042; PLipase_B-like_dom3.
DR PANTHER; PTHR12370:SF1; PHOSPHOLIPASE B-LIKE 1; 1.
DR PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:I3LCG5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364138}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT CHAIN 35..544
FT /note="Phospholipase B-like"
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT /id="PRO_5041479870"
SQ SEQUENCE 544 AA; 62308 MW; 7C6C374213BC5E6F CRC64;
MSRRSRDGRL GLPAPPAPLL LLLLLAAAVP PSLAGVYYAT AYWMPTEKRM LVKNVLDRNG
DAYGFYNDSM KTTGWGILEI RAGYGSQSLS NNIIMFAAGY LEGYLTAPHI YDHFTNLYPQ
LIKKSSVLDK VQDFLRKQDQ WTRDNIKNYK NDPFWRHTGY VMAQMDGLYV GAMKRAVSEG
RKPITLFQIQ FLNAVGDLLD LIPSLSPINY SDLKVFKRWD MGHCSALIKV LPGFENIFFA
HSSWYTYAAM LRIYKHWDFN IIDKDTSSSR LSFSSYPGFL ESLDDFYLLG SGLVLLQTTN
SVYNKTLMKQ VVPQSLLAWQ RVRVANMMAS GGKQWAEVFS KYNSGTYNNQ YMVLDLKKVN
LNYGLGKGTL YIVEQIPTYV EYSEQTDVLK RGYWPSYNIP FHEKIYNWSG YPMLVKKLGL
DFSYALASRA KIFRRDQGKV TDMESMKYIM RYNNYKKEPY SKGDPCNTIC CREDLNELNP
SPGGCYDTKV ADIHLASTYT AYAISGPTVQ DGLPVFHWNH FNKTLHEGMP EAYNFDFITM
KPTL
//