PLBL1_RAT
ID PLBL1_RAT Reviewed; 550 AA.
AC Q5U2V4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Phospholipase B-like 1;
DE EC=3.1.1.-;
DE AltName: Full=LAMA-like protein 1;
DE AltName: Full=Lamina ancestor homolog 1;
DE AltName: Full=Phospholipase B domain-containing protein 1;
DE Contains:
DE RecName: Full=Phospholipase B-like 1 chain A;
DE Contains:
DE RecName: Full=Phospholipase B-like 1 chain B;
DE Contains:
DE RecName: Full=Phospholipase B-like 1 chain C;
DE Flags: Precursor;
GN Name=Plbd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Exhibits weak phospholipase activity, acting on various
CC phospholipids, including phosphatidylcholine, phosphatidylinositol,
CC phosphatidylethanolamine and lysophospholipids. However, in view of the
CC small size of the putative binding pocket, it has been proposed that it
CC may act rather as an amidase or a peptidase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: May form a homodimer, each monomer is composed of a chain A
CC and a chain B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- PTM: The maturation cleavages that produces chains A and B are required
CC to open the putative substrate binding pocket. Both chains A and B
CC remain associated in the mature protein (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR EMBL; BC085851; AAH85851.1; -; mRNA.
DR RefSeq; NP_001013949.1; NM_001013927.1.
DR AlphaFoldDB; Q5U2V4; -.
DR SMR; Q5U2V4; -.
DR BioGRID; 255637; 2.
DR IntAct; Q5U2V4; 1.
DR STRING; 10116.ENSRNOP00000011930; -.
DR GlyGen; Q5U2V4; 4 sites.
DR PhosphoSitePlus; Q5U2V4; -.
DR PaxDb; Q5U2V4; -.
DR PRIDE; Q5U2V4; -.
DR Ensembl; ENSRNOT00000011930; ENSRNOP00000011930; ENSRNOG00000008933.
DR GeneID; 297694; -.
DR KEGG; rno:297694; -.
DR UCSC; RGD:1308734; rat.
DR CTD; 79887; -.
DR RGD; 1308734; Plbd1.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_027106_3_0_1; -.
DR InParanoid; Q5U2V4; -.
DR OMA; MYDHFTN; -.
DR OrthoDB; 724258at2759; -.
DR PhylomeDB; Q5U2V4; -.
DR TreeFam; TF315042; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR Reactome; R-RNO-1483115; Hydrolysis of LPC.
DR PRO; PR:Q5U2V4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008933; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5U2V4; RN.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.439.20; -; 1.
DR Gene3D; 2.10.70.60; -; 1.
DR Gene3D; 3.60.60.20; -; 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; PTHR12370; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000250"
FT CHAIN 40..550
FT /note="Phospholipase B-like 1"
FT /id="PRO_0000286108"
FT CHAIN 40..209
FT /note="Phospholipase B-like 1 chain A"
FT /id="PRO_0000425429"
FT CHAIN 94..209
FT /note="Phospholipase B-like 1 chain C"
FT /id="PRO_0000425430"
FT PROPEP 210..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425431"
FT CHAIN 229..550
FT /note="Phospholipase B-like 1 chain B"
FT /id="PRO_0000425432"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 471..476
FT /evidence="ECO:0000250"
FT DISULFID 475..490
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 63027 MW; 09F979E6AA382AC3 CRC64;
MCHRSHGRSL RPPSPLLLLL PLLLQSPWAA GAAEKHNSAG VHYATAYWLP DTKAVEIKMV
LDKKGDAYGF YNDSIQTTGW GVLEIKAGYG SQILSNEIIM FLAGYLEGYL TALHMYDHFT
NLYPQLIKNP SIVKKVQDFM EKQELWTRKN IKDQKDDPFW RHTGYVVSQL DGMYLGAQKR
ASEEEMKPMT MFQIQFLNAV GDLLDLIPSL SPTKSSSLKK FKIWEMGHCS ALIKVLPGFE
NIYFAHSSWY TYAAMLRIYK HWDFNIKDKY TASNRLSFSS YPGFLESLDD FYILSSGLIL
LQTTNSVYNK TLLKLVVPES LLAWQRVRVA NMMAQGGKEW SQLFSMYNSG TYNNQYMVLD
LKKVTLKKSI DRGALYVVEQ IPTYVEYSDQ TNILRKGYWA SYNIPFHKTV YNWSGYPLLV
HKLGLDYSYD LAPRAKIFRR DQGTVTDMAS MKHIMRYNNY KVDPYSKGDP CSTICCREDL
NEASPSPGGC YDTKVADIFL ASQYKAYAIS GPTVQNGLPP FNWNRFNDTL HQGMPDVFDF
DFVTMKPILT
