PLBL1_HUMAN
ID PLBL1_HUMAN Reviewed; 553 AA.
AC Q6P4A8; A8K4E9; Q9BVV3; Q9H625;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 128.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-265.
RC TISSUE=Neutrophil, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-265 AND ALA-534.
RC TISSUE=Placenta;
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 [4]
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, PROTEOLYTIC PROCESSING, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Granulocyte;
RX PubMed=19019078; DOI=10.1111/j.1742-4658.2008.06771.x;
RA Xu S., Zhao L., Larsson A., Venge P.;
RT "The identification of a phospholipase B precursor in human neutrophils.";
RL FEBS J. 276:175-186(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: In view of the small size of the putative binding pocket, it
CC has been proposed that it may act as an amidase or a peptidase (By
CC similarity). Exhibits a weak phospholipase activity, acting on various
CC phospholipids, including phosphatidylcholine, phosphatidylinositol,
CC phosphatidylethanolamine and lysophospholipids. {ECO:0000250,
CC ECO:0000269|PubMed:19019078}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:19019078};
CC -!- SUBUNIT: May form a homodimer, each monomer is composed of a chain A
CC and a chain B. {ECO:0000269|PubMed:19019078}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils and monocytes.
CC {ECO:0000269|PubMed:19019078}.
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. {ECO:0000269|PubMed:19019078}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00909.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK026315; BAB15442.1; ALT_INIT; mRNA.
DR EMBL; AK290914; BAF83603.1; -; mRNA.
DR EMBL; AC008114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000909; AAH00909.2; ALT_INIT; mRNA.
DR EMBL; BC063561; AAH63561.1; -; mRNA.
DR CCDS; CCDS31751.1; -.
DR RefSeq; NP_079105.4; NM_024829.5.
DR AlphaFoldDB; Q6P4A8; -.
DR SMR; Q6P4A8; -.
DR BioGRID; 122972; 130.
DR IntAct; Q6P4A8; 15.
DR MINT; Q6P4A8; -.
DR STRING; 9606.ENSP00000240617; -.
DR GlyConnect; 1603; 12 N-Linked glycans (3 sites).
DR GlyGen; Q6P4A8; 6 sites, 11 N-linked glycans (3 sites).
DR iPTMnet; Q6P4A8; -.
DR PhosphoSitePlus; Q6P4A8; -.
DR BioMuta; PLBD1; -.
DR DMDM; 269849630; -.
DR EPD; Q6P4A8; -.
DR jPOST; Q6P4A8; -.
DR MassIVE; Q6P4A8; -.
DR MaxQB; Q6P4A8; -.
DR PaxDb; Q6P4A8; -.
DR PeptideAtlas; Q6P4A8; -.
DR PRIDE; Q6P4A8; -.
DR ProteomicsDB; 66958; -.
DR Antibodypedia; 23639; 63 antibodies from 13 providers.
DR DNASU; 79887; -.
DR Ensembl; ENST00000240617.10; ENSP00000240617.5; ENSG00000121316.11.
DR GeneID; 79887; -.
DR KEGG; hsa:79887; -.
DR MANE-Select; ENST00000240617.10; ENSP00000240617.5; NM_024829.6; NP_079105.4.
DR UCSC; uc001rcc.2; human.
DR CTD; 79887; -.
DR DisGeNET; 79887; -.
DR GeneCards; PLBD1; -.
DR HGNC; HGNC:26215; PLBD1.
DR HPA; ENSG00000121316; Tissue enhanced (bone).
DR MIM; 618486; gene.
DR neXtProt; NX_Q6P4A8; -.
DR OpenTargets; ENSG00000121316; -.
DR PharmGKB; PA164724597; -.
DR VEuPathDB; HostDB:ENSG00000121316; -.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_027106_3_0_1; -.
DR InParanoid; Q6P4A8; -.
DR OMA; MYDHFTN; -.
DR OrthoDB; 724258at2759; -.
DR PhylomeDB; Q6P4A8; -.
DR TreeFam; TF315042; -.
DR BRENDA; 3.1.1.5; 2681.
DR PathwayCommons; Q6P4A8; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR SignaLink; Q6P4A8; -.
DR BioGRID-ORCS; 79887; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; PLBD1; human.
DR GenomeRNAi; 79887; -.
DR Pharos; Q6P4A8; Tdark.
DR PRO; PR:Q6P4A8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6P4A8; protein.
DR Bgee; ENSG00000121316; Expressed in monocyte and 176 other tissues.
DR ExpressionAtlas; Q6P4A8; baseline and differential.
DR Genevisible; Q6P4A8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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..38
FT /evidence="ECO:0000255"
FT CHAIN 39..553
FT /note="Phospholipase B-like 1"
FT /id="PRO_0000286106"
FT CHAIN 39..208
FT /note="Phospholipase B-like 1 chain A"
FT /id="PRO_0000425421"
FT CHAIN 93..208
FT /note="Phospholipase B-like 1 chain C"
FT /id="PRO_0000425422"
FT PROPEP 209..227
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000425423"
FT CHAIN 228..553
FT /note="Phospholipase B-like 1 chain B"
FT /id="PRO_0000425424"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 470..475
FT /evidence="ECO:0000250"
FT DISULFID 474..489
FT /evidence="ECO:0000250"
FT VARIANT 265
FT /note="V -> I (in dbSNP:rs7957558)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032072"
FT VARIANT 377
FT /note="V -> A (in dbSNP:rs2287541)"
FT /id="VAR_032073"
FT VARIANT 534
FT /note="P -> A (in dbSNP:rs1600)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032074"
FT CONFLICT 18
FT /note="Missing (in Ref. 1; BAF83603 and 3; AAH63561)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="I -> V (in Ref. 3; BAB15442)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> A (in Ref. 1; BAF83603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 63255 MW; B4258DD2E1A16FE0 CRC64;
MTRGGPGGRP GLPQPPPLLL LLLLLPLLLV TAEPPKPAGV YYATAYWMPA EKTVQVKNVM
DKNGDAYGFY NNSVKTTGWG ILEIRAGYGS QTLSNEIIMF VAGFLEGYLT APHMNDHYTN
LYPQLITKPS IMDKVQDFME KQDKWTRKNI KEYKTDSFWR HTGYVMAQID GLYVGAKKRA
ILEGTKPMTL FQIQFLNSVG DLLDLIPSLS PTKNGSLKVF KRWDMGHCSA LIKVLPGFEN
ILFAHSSWYT YAAMLRIYKH WDFNVIDKDT SSSRLSFSSY PGFLESLDDF YILSSGLILL
QTTNSVFNKT LLKQVIPETL LSWQRVRVAN MMADSGKRWA DIFSKYNSGT YNNQYMVLDL
KKVKLNHSLD KGTLYIVEQI PTYVEYSEQT DVLRKGYWPS YNVPFHEKIY NWSGYPLLVQ
KLGLDYSYDL APRAKIFRRD QGKVTDTASM KYIMRYNNYK KDPYSRGDPC NTICCREDLN
SPNPSPGGCY DTKVADIYLA SQYTSYAISG PTVQGGLPVF RWDRFNKTLH QGMPEVYNFD
FITMKPILKL DIK
