ID GLMP_HUMAN Reviewed; 406 AA. AC Q8WWB7; A6NH16; B4DJN4; Q5SZX4; Q6UX96; Q8IV07; Q96F65; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 29-MAY-2024, entry version 153. DE RecName: Full=Glycosylated lysosomal membrane protein {ECO:0000312|HGNC:HGNC:29436}; DE AltName: Full=Lysosomal protein NCU-G1 {ECO:0000305}; DE Flags: Precursor; GN Name=GLMP {ECO:0000312|HGNC:HGNC:29436}; GN Synonyms=C1orf85 {ECO:0000312|HGNC:HGNC:29436}; GN ORFNames=PSEC0030, UNQ2553/PRO6182; 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] (ISOFORM 1), AND VARIANT ILE-94. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thalamus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-203 RP AND VAL-223. RC TISSUE=Colon, Skin, and Spleen; 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 [6] RP PUTATIVE FUNCTION. RX PubMed=18021396; DOI=10.1186/1471-2199-8-106; RA Steffensen K.R., Bouzga M., Skjeldal F., Kasi C., Karahasan A., Matre V., RA Bakke O., Guerin S., Eskild W.; RT "Human NCU-G1 can function as a transcription factor and as a nuclear RT receptor co-activator."; RL BMC Mol. Biol. 8:106-106(2007). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Placenta; RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x; RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., RA Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [8] RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=19556463; DOI=10.1126/science.1174447; RA Sardiello M., Palmieri M., di Ronza A., Medina D.L., Valenza M., RA Gennarino V.A., Di Malta C., Donaudy F., Embrione V., Polishchuk R.S., RA Banfi S., Parenti G., Cattaneo E., Ballabio A.; RT "A gene network regulating lysosomal biogenesis and function."; RL Science 325:473-477(2009). RN [9] 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: Required to protect lysosomal transporter MFSD1 from CC lysosomal proteolysis and for MFSD1 lysosomal localization. CC {ECO:0000250|UniProtKB:Q9JHJ3}. CC -!- SUBUNIT: Interacts (via lumenal domain) with lysosomal protein MFSD1; CC the interaction starts while both proteins are still in the endoplasmic CC reticulum and is required for stability and lysosomal localization of CC MFSD1. {ECO:0000250|UniProtKB:Q9JHJ3}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319, CC ECO:0000269|PubMed:19556463}; Single-pass type I membrane protein CC {ECO:0000255}; Lumenal side {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WWB7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WWB7-2; Sequence=VSP_037842; CC -!- INDUCTION: Transcription is activated by TFEB. CC {ECO:0000269|PubMed:19556463}. CC -!- PTM: Highly N-glycosylated. N-glycosylation is essential for GLMP CC stability and for MFSD1 lysosomal localization. CC {ECO:0000250|UniProtKB:Q9JHJ3}. CC -!- SIMILARITY: Belongs to the GLMP family. {ECO:0000305}. CC -!- CAUTION: According to PubMed:18021396, it binds DNA and acts as a CC transcription factor. However, the localization in lysosomes which was CC confirmed by different groups and the presence of transmembrane region CC strongly suggests that it does not have coactivator activity. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH11575.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY358450; AAQ88815.1; -; mRNA. DR EMBL; AK075349; BAC11561.1; -; mRNA. DR EMBL; AK296157; BAG58896.1; -; mRNA. DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC018757; AAH18757.1; -; mRNA. DR EMBL; BC011575; AAH11575.1; ALT_INIT; mRNA. DR EMBL; BC036340; AAH36340.1; -; mRNA. DR CCDS; CCDS1139.1; -. [Q8WWB7-1] DR CCDS; CCDS72947.1; -. [Q8WWB7-2] DR RefSeq; NP_001243538.1; NM_001256609.1. [Q8WWB7-2] DR RefSeq; NP_653181.1; NM_144580.2. [Q8WWB7-1] DR AlphaFoldDB; Q8WWB7; -. DR SMR; Q8WWB7; -. DR BioGRID; 125204; 155. DR IntAct; Q8WWB7; 67. DR STRING; 9606.ENSP00000354553; -. DR TCDB; 2.A.1.53.3; the major facilitator superfamily (mfs). DR GlyConnect; 794; 3 N-Linked glycans (2 sites). DR GlyCosmos; Q8WWB7; 5 sites, 4 glycans. DR GlyGen; Q8WWB7; 6 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q8WWB7; -. DR PhosphoSitePlus; Q8WWB7; -. DR BioMuta; GLMP; -. DR DMDM; 74760578; -. DR EPD; Q8WWB7; -. DR jPOST; Q8WWB7; -. DR MassIVE; Q8WWB7; -. DR MaxQB; Q8WWB7; -. DR PaxDb; 9606-ENSP00000354553; -. DR PeptideAtlas; Q8WWB7; -. DR ProteomicsDB; 74874; -. [Q8WWB7-1] DR ProteomicsDB; 74875; -. [Q8WWB7-2] DR Pumba; Q8WWB7; -. DR Antibodypedia; 34210; 45 antibodies from 12 providers. DR DNASU; 112770; -. DR Ensembl; ENST00000362007.6; ENSP00000354553.1; ENSG00000198715.13. [Q8WWB7-1] DR Ensembl; ENST00000614643.4; ENSP00000480936.1; ENSG00000198715.13. [Q8WWB7-2] DR Ensembl; ENST00000647767.1; ENSP00000497576.1; ENSG00000198715.13. [Q8WWB7-1] DR GeneID; 112770; -. DR KEGG; hsa:112770; -. DR MANE-Select; ENST00000362007.6; ENSP00000354553.1; NM_144580.3; NP_653181.1. DR UCSC; uc001foh.5; human. [Q8WWB7-1] DR AGR; HGNC:29436; -. DR CTD; 112770; -. DR DisGeNET; 112770; -. DR GeneCards; GLMP; -. DR HGNC; HGNC:29436; GLMP. DR HPA; ENSG00000198715; Low tissue specificity. DR MIM; 619958; gene. DR neXtProt; NX_Q8WWB7; -. DR OpenTargets; ENSG00000198715; -. DR PharmGKB; PA142672533; -. DR VEuPathDB; HostDB:ENSG00000198715; -. DR eggNOG; ENOG502QSBM; Eukaryota. DR GeneTree; ENSGT00390000005131; -. DR HOGENOM; CLU_040225_0_0_1; -. DR InParanoid; Q8WWB7; -. DR OMA; TLHYLWD; -. DR OrthoDB; 5353396at2759; -. DR PhylomeDB; Q8WWB7; -. DR TreeFam; TF324431; -. DR PathwayCommons; Q8WWB7; -. DR SignaLink; Q8WWB7; -. DR BioGRID-ORCS; 112770; 28 hits in 1162 CRISPR screens. DR ChiTaRS; GLMP; human. DR GenomeRNAi; 112770; -. DR Pharos; Q8WWB7; Tdark. DR PRO; PR:Q8WWB7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8WWB7; Protein. DR Bgee; ENSG00000198715; Expressed in right adrenal gland cortex and 170 other cell types or tissues. DR ExpressionAtlas; Q8WWB7; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR InterPro; IPR029382; NCU-G1. DR PANTHER; PTHR31981; GLYCOSYLATED LYSOSOMAL MEMBRANE PROTEIN; 1. DR PANTHER; PTHR31981:SF1; GLYCOSYLATED LYSOSOMAL MEMBRANE PROTEIN; 1. DR Pfam; PF15065; NCU-G1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Glycoprotein; Lysosome; Membrane; Reference proteome; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..35 FT /evidence="ECO:0000255" FT CHAIN 36..406 FT /note="Glycosylated lysosomal membrane protein" FT /evidence="ECO:0000305" FT /id="PRO_0000284484" FT TOPO_DOM 36..372 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 373..393 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 394..406 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOTIF 402..406 FT /note="Lysosomal targeting motif" FT /evidence="ECO:0000250|UniProtKB:Q9JHJ3" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 134 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 187 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 230 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..81 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037842" FT VARIANT 94 FT /note="V -> I (in dbSNP:rs1570805)" FT /evidence="ECO:0000269|PubMed:12975309" FT /id="VAR_031742" FT VARIANT 203 FT /note="P -> S (in dbSNP:rs10908496)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031743" FT VARIANT 223 FT /note="I -> V (in dbSNP:rs10908495)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031744" SQ SEQUENCE 406 AA; 43864 MW; 9FB23252A6FE9163 CRC64; MRGSVECTWG WGHCAPSPLL LWTLLLFAAP FGLLGEKTRQ VSLEVIPNWL GPLQNLLHIR AVGTNSTLHY VWSSLGPLAV VMVATNTPHS TLSVNWSLLL SPEPDGGLMV LPKDSIQFSS ALVFTRLLEF DSTNVSDTAA KPLGRPYPPY SLADFSWNNI TDSLDPATLS ATFQGHPMND PTRTFANGSL AFRVQAFSRS SRPAQPPRLL HTADTCQLEV ALIGASPRGN RSLFGLEVAT LGQGPDCPSM QEQHSIDDEY APAVFQLDQL LWGSLPSGFA QWRPVAYSQK PGGRESALPC QASPLHPALA YSLPQSPIVR AFFGSQNNFC AFNLTFGAST GPGYWDQHYL SWSMLLGVGF PPVDGLSPLV LGIMAVALGA PGLMLLGGGL VLLLHHKKYS EYQSIN //