OSTM1_HUMAN
ID OSTM1_HUMAN Reviewed; 334 AA.
AC Q86WC4; E1P5E3; Q5R391; Q6PCA7; Q7RTW6; Q8NC29; Q8TC82; Q9Y2S9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Osteopetrosis-associated transmembrane protein 1;
DE AltName: Full=Chloride channel 7 beta subunit;
DE Flags: Precursor;
GN Name=OSTM1; Synonyms=GL; ORFNames=HSPC019, UNQ6098/PRO21201;
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 [MRNA], AND INVOLVEMENT IN OPTB5.
RX PubMed=12627228; DOI=10.1038/nm842;
RA Chalhoub N., Benachenhou N., Rajapurohitam V., Pata M., Ferron M.,
RA Frattini A., Villa A., Vacher J.;
RT "Grey-lethal mutation induces severe malignant autosomal recessive
RT osteopetrosis in mouse and human.";
RL Nat. Med. 9:399-406(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-334.
RX PubMed=12079282; DOI=10.1006/geno.2002.6795;
RA Abrahams B.S., Mak G.M., Berry M.L., Palmquist D.L., Saionz J.R., Tay A.,
RA Tan Y.H., Brenner S., Simpson E.M., Venkatesh B.;
RT "Novel vertebrate genes and putative regulatory elements identified at
RT kidney disease and NR2E1/fierce loci.";
RL Genomics 80:45-53(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-334.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INVOLVEMENT IN OPTB5.
RX PubMed=16813530; DOI=10.1359/jbmr.060403;
RA Pangrazio A., Poliani P.L., Megarbane A., Lefranc G., Lanino E.,
RA Di Rocco M., Rucci F., Lucchini F., Ravanini M., Facchetti F., Abinun M.,
RA Vezzoni P., Villa A., Frattini A.;
RT "Mutations in OSTM1 (grey lethal) define a particularly severe form of
RT autosomal recessive osteopetrosis with neural involvement.";
RL J. Bone Miner. Res. 21:1098-1105(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-325 AND SER-333, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH CLCN7, AND SUBCELLULAR LOCATION.
RX PubMed=21527911; DOI=10.1038/emboj.2011.137;
RA Leisle L., Ludwig C.F., Wagner F.A., Jentsch T.J., Stauber T.;
RT "ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1
RT for transport activity.";
RL EMBO J. 30:2140-2152(2011).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Required for osteoclast and melanocyte maturation and
CC function. {ECO:0000250, ECO:0000269|PubMed:21527911}.
CC -!- SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta
CC (OSTM1) subunits. {ECO:0000269|PubMed:21527911}.
CC -!- INTERACTION:
CC Q86WC4; P51798: CLCN7; NbExp=3; IntAct=EBI-11037160, EBI-4402346;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:21527911};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:21527911}.
CC Note=Requires CLCN7 to travel to lysosomes.
CC -!- PTM: Undergoes proteolytic cleavage in the luminal domain, the cleaved
CC fragments might be linked by disulfide bonds with the remnant of the
CC protein. {ECO:0000250}.
CC -!- PTM: Highly N-glycosylated.
CC -!- DISEASE: Osteopetrosis, autosomal recessive 5 (OPTB5) [MIM:259720]: A
CC rare genetic disease characterized by abnormally dense bone, due to
CC defective resorption of immature bone. Osteopetrosis occurs in two
CC forms: a severe autosomal recessive form occurring in utero, infancy,
CC or childhood, and a benign autosomal dominant form occurring in
CC adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC early infancy with macrocephaly, feeding difficulties, evolving
CC blindness and deafness, bone marrow failure, severe anemia, and
CC hepatosplenomegaly. Deafness and blindness are generally thought to
CC represent effects of pressure on nerves. OPTB5 patients manifest
CC primary central nervous system involvement in addition to the classical
CC stigmata of severe bone sclerosis, growth failure, anemia,
CC thrombocytopenia and visual impairment with optic atrophy.
CC {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16813530}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the OSTM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27000.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF533891; AAO72749.1; -; mRNA.
DR EMBL; AY358795; AAQ89155.1; -; mRNA.
DR EMBL; AK075012; BAC11351.1; -; mRNA.
DR EMBL; Z98200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48389.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48390.1; -; Genomic_DNA.
DR EMBL; BC068581; AAH68581.1; -; mRNA.
DR EMBL; BK000461; DAA00039.1; -; mRNA.
DR EMBL; AF077205; AAD27000.1; ALT_FRAME; mRNA.
DR CCDS; CCDS5062.1; -.
DR RefSeq; NP_054747.2; NM_014028.3.
DR PDB; 7BXU; EM; 3.70 A; C/D=1-334.
DR PDB; 7CQ5; EM; 2.60 A; A/B=1-334.
DR PDB; 7CQ6; EM; 3.00 A; A/B=1-334.
DR PDB; 7CQ7; EM; 3.55 A; A/B=1-334.
DR PDB; 7JM7; EM; 2.82 A; B/D=1-334.
DR PDBsum; 7BXU; -.
DR PDBsum; 7CQ5; -.
DR PDBsum; 7CQ6; -.
DR PDBsum; 7CQ7; -.
DR PDBsum; 7JM7; -.
DR AlphaFoldDB; Q86WC4; -.
DR SMR; Q86WC4; -.
DR BioGRID; 118788; 85.
DR ComplexPortal; CPX-6321; CLCN7-OSTM1 chloride channel complex.
DR IntAct; Q86WC4; 10.
DR MINT; Q86WC4; -.
DR STRING; 9606.ENSP00000193322; -.
DR TCDB; 2.A.49.3.3; the chloride carrier/channel (clc) family.
DR GlyConnect; 1589; 5 N-Linked glycans (4 sites).
DR GlyGen; Q86WC4; 10 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q86WC4; -.
DR PhosphoSitePlus; Q86WC4; -.
DR BioMuta; OSTM1; -.
DR DMDM; 51316434; -.
DR EPD; Q86WC4; -.
DR jPOST; Q86WC4; -.
DR MassIVE; Q86WC4; -.
DR MaxQB; Q86WC4; -.
DR PaxDb; Q86WC4; -.
DR PeptideAtlas; Q86WC4; -.
DR PRIDE; Q86WC4; -.
DR ProteomicsDB; 70145; -.
DR Antibodypedia; 2255; 191 antibodies from 26 providers.
DR DNASU; 28962; -.
DR Ensembl; ENST00000193322.8; ENSP00000193322.3; ENSG00000081087.15.
DR GeneID; 28962; -.
DR KEGG; hsa:28962; -.
DR MANE-Select; ENST00000193322.8; ENSP00000193322.3; NM_014028.4; NP_054747.2.
DR UCSC; uc003psd.3; human.
DR CTD; 28962; -.
DR DisGeNET; 28962; -.
DR GeneCards; OSTM1; -.
DR HGNC; HGNC:21652; OSTM1.
DR HPA; ENSG00000081087; Low tissue specificity.
DR MalaCards; OSTM1; -.
DR MIM; 259720; phenotype.
DR MIM; 607649; gene.
DR neXtProt; NX_Q86WC4; -.
DR OpenTargets; ENSG00000081087; -.
DR Orphanet; 85179; Infantile osteopetrosis with neuroaxonal dysplasia.
DR PharmGKB; PA134941162; -.
DR VEuPathDB; HostDB:ENSG00000081087; -.
DR eggNOG; KOG4617; Eukaryota.
DR GeneTree; ENSGT00390000012341; -.
DR HOGENOM; CLU_070677_0_0_1; -.
DR InParanoid; Q86WC4; -.
DR OMA; FQQVASK; -.
DR OrthoDB; 1105868at2759; -.
DR PhylomeDB; Q86WC4; -.
DR TreeFam; TF323313; -.
DR PathwayCommons; Q86WC4; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q86WC4; -.
DR BioGRID-ORCS; 28962; 8 hits in 1110 CRISPR screens.
DR ChiTaRS; OSTM1; human.
DR GeneWiki; OSTM1; -.
DR GenomeRNAi; 28962; -.
DR Pharos; Q86WC4; Tbio.
DR PRO; PR:Q86WC4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86WC4; protein.
DR Bgee; ENSG00000081087; Expressed in choroid plexus epithelium and 198 other tissues.
DR ExpressionAtlas; Q86WC4; baseline and differential.
DR Genevisible; Q86WC4; HS.
DR GO; GO:0034707; C:chloride channel complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ComplexPortal.
DR GO; GO:0030316; P:osteoclast differentiation; IBA:GO_Central.
DR GO; GO:0030321; P:transepithelial chloride transport; IDA:ComplexPortal.
DR InterPro; IPR019172; Osteopetrosis-assoc_TM_1.
DR PANTHER; PTHR15644; PTHR15644; 1.
DR Pfam; PF09777; OSTMP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Lysosome; Membrane; Osteopetrosis;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..334
FT /note="Osteopetrosis-associated transmembrane protein 1"
FT /id="PRO_0000021963"
FT TOPO_DOM 32..284
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 52
FT /note="L -> F (in dbSNP:rs9480830)"
FT /id="VAR_051257"
FT CONFLICT 87
FT /note="L -> P (in Ref. 3; BAC11351)"
FT /evidence="ECO:0000305"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 82..104
FT /evidence="ECO:0007829|PDB:7CQ5"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:7CQ5"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:7CQ5"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:7CQ5"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 184..202
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:7CQ5"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 225..244
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 256..270
FT /evidence="ECO:0007829|PDB:7CQ5"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:7CQ5"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:7CQ5"
SQ SEQUENCE 334 AA; 37257 MW; 108719C2FDC5853D CRC64;
MEPGPTAAQR RCSLPPWLPL GLLLWSGLAL GALPFGSSPH RVFHDLLSEQ QLLEVEDLSL
SLLQGGGLGP LSLPPDLPDL DPECRELLLD FANSSAELTG CLVRSARPVR LCQTCYPLFQ
QVVSKMDNIS RAAGNTSESQ SCARSLLMAD RMQIVVILSE FFNTTWQEAN CANCLTNNSE
ELSNSTVYFL NLFNHTLTCF EHNLQGNAHS LLQTKNYSEV CKNCREAYKT LSSLYSEMQK
MNELENKAEP GTHLCIDVED AMNITRKLWS RTFNCSVPCS DTVPVIAVSV FILFLPVVFY
LSSFLHSEQK KRKLILPKRL KSSTSFANIQ ENSN
