PLBL1_MOUSE
ID PLBL1_MOUSE Reviewed; 550 AA.
AC Q8VCI0; Q3TA89; Q9D1S0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 119.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-72.
RC TISSUE=Epidermis;
RX PubMed=16170054; DOI=10.1074/mcp.m500203-mcp200;
RA Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K.,
RA Nishimura S.;
RT "High throughput quantitative glycomics and glycoform-focused proteomics of
RT murine dermis and epidermis.";
RL Mol. Cell. Proteomics 4:1977-1989(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE42780.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003169; BAB22618.1; -; mRNA.
DR EMBL; AK172021; BAE42780.1; ALT_FRAME; mRNA.
DR EMBL; BC019793; AAH19793.1; -; mRNA.
DR CCDS; CCDS20652.1; -.
DR RefSeq; NP_080082.1; NM_025806.2.
DR AlphaFoldDB; Q8VCI0; -.
DR SMR; Q8VCI0; -.
DR BioGRID; 211766; 2.
DR STRING; 10090.ENSMUSP00000032336; -.
DR GlyGen; Q8VCI0; 5 sites.
DR iPTMnet; Q8VCI0; -.
DR PhosphoSitePlus; Q8VCI0; -.
DR jPOST; Q8VCI0; -.
DR MaxQB; Q8VCI0; -.
DR PaxDb; Q8VCI0; -.
DR PeptideAtlas; Q8VCI0; -.
DR PRIDE; Q8VCI0; -.
DR ProteomicsDB; 289613; -.
DR GeneID; 66857; -.
DR KEGG; mmu:66857; -.
DR UCSC; uc009elz.2; mouse.
DR CTD; 79887; -.
DR MGI; MGI:1914107; Plbd1.
DR eggNOG; KOG3774; Eukaryota.
DR InParanoid; Q8VCI0; -.
DR OrthoDB; 724258at2759; -.
DR PhylomeDB; Q8VCI0; -.
DR TreeFam; TF315042; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR BioGRID-ORCS; 66857; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Plbd1; mouse.
DR PRO; PR:Q8VCI0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VCI0; protein.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
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 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_0000286107"
FT CHAIN 40..209
FT /note="Phospholipase B-like 1 chain A"
FT /id="PRO_0000425425"
FT CHAIN 94..209
FT /note="Phospholipase B-like 1 chain C"
FT /id="PRO_0000425426"
FT PROPEP 210..228
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425427"
FT CHAIN 229..550
FT /note="Phospholipase B-like 1 chain B"
FT /id="PRO_0000425428"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:16170054"
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 367
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 367
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"
FT CONFLICT 127
FT /note="I -> F (in Ref. 1; BAB22618)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="E -> D (in Ref. 1; BAB22618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 62998 MW; C89FC31C0D14B5F6 CRC64;
MCHRSPGRSL RPPSPLLLLL PLLLQPPWAA GAASQSDPTG VHCATAYWSP ESKKVEIKTV
LDKNGDAYGY YNDSIKTTGW GILEIRAGYG SQVLSNEIIM FLAGYLEGYL TALHMYDHFT
NLYPQLIKNP SIVKKVQDFM EKQEMWTRQN IKAQKDDPFW RHTGYVVTQL DGLYLGAQKR
ASEEKIKPMT MFQIQFLNAV GDLLDLIPSL SPTKSSSMMK FKIWEMGHCS ALIKVLPGFE
NIYFAHSSWY TYAAMLRIYK HWDFNIKDKY TLSKRLSFSS YPGFLESLDD FYILSSGLIL
LQTTNSVYNK TLLKQVVPKT LLAWQRVRVA NMMAEGGKEW AQIFSKHNSG TYNNQYMVLD
LKKVTINRSL DKGTLYIVEQ IPTYVEYSDQ TNVLRKGYWA SYNIPFHKTI YNWSGYPLLV
HKLGLDYSYD LAPRAKIFRR DQGNVTDMAS MKYIMRYNNY KEDPYSKGDP CSTICCREDL
NGASPSPGGC YDTKVADIFL ASQYKAYAIS GPTVQDGLPP FNWNRFNETL HRGMPEVFDF
NFVTMKPILS
