PLBL1_BOVIN
ID PLBL1_BOVIN Reviewed; 545 AA.
AC Q9GL30; A6QPQ7; F1MBV7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Hereford; TISSUE=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-545 (ISOFORM 1).
RC TISSUE=Kidney;
RA Heikinheimo P.;
RT "Purification and identification of an unknown protein from bovine
RT kidneys.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 36-205 AND 225-545, PARTIAL
RP PROTEIN SEQUENCE, FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, SIGNAL
RP SEQUENCE CLEAVAGE SITE, AND GLYCOSYLATION AT ASN-68; ASN-305; ASN-363;
RP ASN-408 AND ASN-523.
RC TISSUE=Kidney;
RX PubMed=23934913; DOI=10.1002/prot.24388;
RA Repo H., Kuokkanen E., Oksanen E., Goldman A., Heikinheimo P.;
RT "Is the bovine lysosomal phospholipase B-like protein an amidase?";
RL Proteins 82:300-311(2014).
CC -!- FUNCTION: Exhibits a weak phospholipase activity, acting on various
CC phospholipids, including phosphatidylcholine, phosphatidylinositol,
CC phosphatidylethanolamine and lysophospholipids (By similarity).
CC However, in view of the small size of the putative binding pocket, it
CC has been proposed that it may act rather as an amidase or a peptidase
CC (PubMed:23934913). {ECO:0000250, ECO:0000269|PubMed:23934913}.
CC -!- SUBUNIT: May form a homodimer, each monomer is composed of a chain A
CC and a chain B.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:23934913}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GL30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GL30-2; Sequence=VSP_053706;
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.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR EMBL; DAAA02014236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02014237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02014238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02014239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02014240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC149435; AAI49436.1; -; mRNA.
DR EMBL; AJ299408; CAC13971.1; -; mRNA.
DR RefSeq; NP_001094514.2; NM_001101044.2. [Q9GL30-2]
DR RefSeq; NP_001159770.1; NM_001166298.1. [Q9GL30-1]
DR PDB; 4BWC; X-ray; 1.89 A; A=36-205, B=225-545.
DR PDBsum; 4BWC; -.
DR AlphaFoldDB; Q9GL30; -.
DR SMR; Q9GL30; -.
DR STRING; 9913.ENSBTAP00000020677; -.
DR MEROPS; C95.002; -.
DR iPTMnet; Q9GL30; -.
DR PaxDb; Q9GL30; -.
DR Ensembl; ENSBTAT00000020677; ENSBTAP00000020677; ENSBTAG00000015562. [Q9GL30-1]
DR Ensembl; ENSBTAT00000056815; ENSBTAP00000050579; ENSBTAG00000015562. [Q9GL30-2]
DR GeneID; 317710; -.
DR KEGG; bta:317710; -.
DR CTD; 79887; -.
DR VEuPathDB; HostDB:ENSBTAG00000015562; -.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_027106_3_0_1; -.
DR InParanoid; Q9GL30; -.
DR OrthoDB; 724258at2759; -.
DR TreeFam; TF315042; -.
DR Proteomes; UP000009136; Chromosome 5.
DR ExpressionAtlas; Q9GL30; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:23934913"
FT CHAIN 36..545
FT /note="Phospholipase B-like 1"
FT /id="PRO_5000066752"
FT CHAIN 36..205
FT /note="Phospholipase B-like 1 chain A"
FT /id="PRO_0000425417"
FT CHAIN 90..205
FT /note="Phospholipase B-like 1 chain C"
FT /id="PRO_0000425418"
FT PROPEP 206..224
FT /note="Removed in mature form"
FT /id="PRO_0000425419"
FT CHAIN 225..545
FT /note="Phospholipase B-like 1 chain B"
FT /id="PRO_0000425420"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:23934913"
FT DISULFID 467..472
FT DISULFID 471..486
FT VAR_SEQ 280..393
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053706"
FT CONFLICT 173
FT /note="A -> E (in Ref. 2; AAI49436)"
FT /evidence="ECO:0000305"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 92..122
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 126..149
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 154..180
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 444..451
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:4BWC"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:4BWC"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:4BWC"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:4BWC"
SQ SEQUENCE 545 AA; 62556 MW; A7D0E984AB134956 CRC64;
MSRHSQDERL GLPQPPALLP LLLLLLAVAV PLSQAGVYYA TAYWMPTEKT IQVKNVLDRK
GDAYGFYNNS VKTTGWGILE IKAGYGSQSL SNEIIMFAAG FLEGYLTAPH MDDHFTNLYP
QLIKKRSMLN KVQDFLTKQD QWTRENIKYY KSDPFWRHAD YVMAQMDGLF AGATKRAVLE
GKKPMTLFQI QFLNAIGDLL DLIPSLSPTK NSSLKFFKRW DMGHCSALIK VLPGFENIFF
AHSSWYTYAA MLRIYKHWDF NIVDKDTSSS RLSFSSYPGF LESLDDFYLL SSGLVLLQTT
NSVYNKTLLQ HVVPQSLLAW QRVRVASMMA NNGKQWAEVF SKYNSGTYNN QYMVLDLKKV
NLNHSLDEGT LYIVEQIPTY VEYSEQTAVL RRGYWPSYNI PFHEKVYNWS GYPILVKKLG
LDYSYDLASR AKIFRRDQGK VTDMESMKYI MRYNNYKQDP YSKGDPCNTV CCREDLNSHS
PSPGGCYDTK VADIYLASKY KAYAISGPTV QGGLPVFHWS RFNKTLHEGM PEAYNFDFIT
MKPIL
