GLMP_HUMAN
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 03-AUG-2022, entry version 144.
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};
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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 GlyGen; Q8WWB7; 5 sites, 4 N-linked glycans (2 sites).
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; Q8WWB7; -.
DR PeptideAtlas; Q8WWB7; -.
DR PRIDE; Q8WWB7; -.
DR ProteomicsDB; 74874; -. [Q8WWB7-1]
DR ProteomicsDB; 74875; -. [Q8WWB7-2]
DR Antibodypedia; 34210; 43 antibodies from 11 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 CTD; 112770; -.
DR GeneCards; GLMP; -.
DR HGNC; HGNC:29436; GLMP.
DR HPA; ENSG00000198715; Low tissue specificity.
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; 562253at2759; -.
DR PhylomeDB; Q8WWB7; -.
DR TreeFam; TF324431; -.
DR PathwayCommons; Q8WWB7; -.
DR SignaLink; Q8WWB7; -.
DR BioGRID-ORCS; 112770; 26 hits in 1082 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 168 other tissues.
DR ExpressionAtlas; Q8WWB7; baseline and differential.
DR Genevisible; Q8WWB7; HS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA: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; PTHR31981; 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
