PLBL2_HUMAN
ID PLBL2_HUMAN Reviewed; 589 AA.
AC Q8NHP8; F5H5E2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative phospholipase B-like 2;
DE EC=3.1.1.-;
DE AltName: Full=76 kDa protein;
DE Short=p76;
DE AltName: Full=LAMA-like protein 2;
DE AltName: Full=Lamina ancestor homolog 2;
DE AltName: Full=Phospholipase B domain-containing protein 2;
DE Contains:
DE RecName: Full=Putative phospholipase B-like 2 32 kDa form;
DE Contains:
DE RecName: Full=Putative phospholipase B-like 2 45 kDa form;
DE Flags: Precursor;
GN Name=PLBD2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 42-49 AND 244-250, GLYCOSYLATION AT ASN-88; ASN-110;
RP ASN-231; ASN-436; ASN-465 AND ASN-515, INTERACTION WITH IGF2R, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17105447; DOI=10.1042/bj20061205;
RA Jensen A.G., Chemali M., Chapel A., Kieffer-Jaquinod S., Jadot M.,
RA Garin J., Journet A.;
RT "Biochemical characterization and lysosomal localization of the mannose-6-
RT phosphate protein p76 (hypothetical protein LOC196463).";
RL Biochem. J. 402:449-458(2007).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-465.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Putative phospholipase. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IGF2R. {ECO:0000269|PubMed:17105447}.
CC -!- INTERACTION:
CC Q8NHP8; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-10968883, EBI-17247926;
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:17105447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NHP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NHP8-2; Sequence=VSP_055623;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC heart, brain and liver. {ECO:0000269|PubMed:17105447}.
CC -!- PTM: The p76 protein is synthesized as a 80 kDa precursor which is then
CC processed into a N-terminal 32 kDa form and a C-terminal 45 kDa form.
CC -!- PTM: Glycosylated; contains mannose 6-phosphate sugars.
CC {ECO:0000269|PubMed:17105447, ECO:0000269|PubMed:19159218}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
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DR EMBL; AC010178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030618; AAH30618.1; -; mRNA.
DR EMBL; BC071832; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS53834.1; -. [Q8NHP8-2]
DR CCDS; CCDS9168.1; -. [Q8NHP8-1]
DR RefSeq; NP_001153199.1; NM_001159727.1. [Q8NHP8-2]
DR RefSeq; NP_775813.2; NM_173542.3. [Q8NHP8-1]
DR AlphaFoldDB; Q8NHP8; -.
DR SMR; Q8NHP8; -.
DR BioGRID; 128208; 32.
DR IntAct; Q8NHP8; 13.
DR STRING; 9606.ENSP00000280800; -.
DR MEROPS; C95.001; -.
DR GlyConnect; 1700; 6 N-Linked glycans (3 sites).
DR GlyGen; Q8NHP8; 9 sites, 7 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q8NHP8; -.
DR MetOSite; Q8NHP8; -.
DR PhosphoSitePlus; Q8NHP8; -.
DR BioMuta; PLBD2; -.
DR DMDM; 224471847; -.
DR EPD; Q8NHP8; -.
DR jPOST; Q8NHP8; -.
DR MassIVE; Q8NHP8; -.
DR MaxQB; Q8NHP8; -.
DR PaxDb; Q8NHP8; -.
DR PeptideAtlas; Q8NHP8; -.
DR PRIDE; Q8NHP8; -.
DR ProteomicsDB; 26851; -.
DR ProteomicsDB; 73733; -. [Q8NHP8-1]
DR Antibodypedia; 2539; 100 antibodies from 19 providers.
DR DNASU; 196463; -.
DR Ensembl; ENST00000280800.5; ENSP00000280800.3; ENSG00000151176.8. [Q8NHP8-1]
DR Ensembl; ENST00000545182.6; ENSP00000443463.2; ENSG00000151176.8. [Q8NHP8-2]
DR GeneID; 196463; -.
DR KEGG; hsa:196463; -.
DR MANE-Select; ENST00000280800.5; ENSP00000280800.3; NM_173542.4; NP_775813.2.
DR UCSC; uc001tve.3; human. [Q8NHP8-1]
DR CTD; 196463; -.
DR DisGeNET; 196463; -.
DR GeneCards; PLBD2; -.
DR HGNC; HGNC:27283; PLBD2.
DR HPA; ENSG00000151176; Tissue enhanced (adrenal).
DR neXtProt; NX_Q8NHP8; -.
DR OpenTargets; ENSG00000151176; -.
DR PharmGKB; PA164724624; -.
DR VEuPathDB; HostDB:ENSG00000151176; -.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_027106_4_0_1; -.
DR InParanoid; Q8NHP8; -.
DR OMA; FQWSKSP; -.
DR OrthoDB; 724258at2759; -.
DR PhylomeDB; Q8NHP8; -.
DR TreeFam; TF315042; -.
DR PathwayCommons; Q8NHP8; -.
DR SignaLink; Q8NHP8; -.
DR BioGRID-ORCS; 196463; 18 hits in 1091 CRISPR screens.
DR ChiTaRS; PLBD2; human.
DR GenomeRNAi; 196463; -.
DR Pharos; Q8NHP8; Tbio.
DR PRO; PR:Q8NHP8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NHP8; protein.
DR Bgee; ENSG00000151176; Expressed in right adrenal gland cortex and 175 other tissues.
DR ExpressionAtlas; Q8NHP8; baseline and differential.
DR Genevisible; Q8NHP8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; 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 Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000269|PubMed:17105447"
FT CHAIN 42..589
FT /note="Putative phospholipase B-like 2"
FT /id="PRO_0000286110"
FT CHAIN 42..243
FT /note="Putative phospholipase B-like 2 32 kDa form"
FT /id="PRO_0000314074"
FT CHAIN 244..589
FT /note="Putative phospholipase B-like 2 45 kDa form"
FT /id="PRO_0000314075"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17105447"
FT DISULFID 142..152
FT /evidence="ECO:0000250"
FT DISULFID 492..495
FT /evidence="ECO:0000250"
FT VAR_SEQ 374..405
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055623"
FT VARIANT 54
FT /note="Q -> P (in dbSNP:rs7965471)"
FT /id="VAR_062187"
FT VARIANT 524
FT /note="R -> C (in dbSNP:rs12425042)"
FT /id="VAR_032075"
FT CONFLICT 521
FT /note="Q -> K (in Ref. 2; AAH30618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65472 MW; D0D1BACCFBF756BB CRC64;
MVGQMYCYPG SHLARALTRA LALALVLALL VGPFLSGLAG AIPAPGGRWA RDGQVPPASR
SRSVLLDVSA GQLLMVDGRH PDAVAWANLT NAIRETGWAF LELGTSGQYN DSLQAYAAGV
VEAAVSEELI YMHWMNTVVN YCGPFEYEVG YCERLKSFLE ANLEWMQEEM ESNPDSPYWH
QVRLTLLQLK GLEDSYEGRV SFPAGKFTIK PLGFLLLQLS GDLEDLELAL NKTKIKPSLG
SGSCSALIKL LPGQSDLLVA HNTWNNYQHM LRVIKKYWLQ FREGPWGDYP LVPGNKLVFS
SYPGTIFSCD DFYILGSGLV TLETTIGNKN PALWKYVRPR GCVLEWVRNI VANRLASDGA
TWADIFKRFN SGTYNNQWMI VDYKAFIPGG PSPGSRVLTI LEQIPGMVVV ADKTSELYQK
TYWASYNIPS FETVFNASGL QALVAQYGDW FSYDGSPRAQ IFRRNQSLVQ DMDSMVRLMR
YNDFLHDPLS LCKACNPQPN GENAISARSD LNPANGSYPF QALRQRSHGG IDVKVTSMSL
ARILSLLAAS GPTWDQVPPF QWSTSPFSGL LHMGQPDLWK FAPVKVSWD
