OSTM1_MOUSE
ID OSTM1_MOUSE Reviewed; 338 AA.
AC Q8BGT0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Osteopetrosis-associated transmembrane protein 1;
DE AltName: Full=Chloride channel 7 beta subunit;
DE AltName: Full=Grey-lethal protein;
DE Flags: Precursor;
GN Name=Ostm1; Synonyms=Gl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISEASE.
RC STRAIN=C57BL/6J;
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].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 FUNCTION, GLYCOSYLATION, PROTEOLYTIC CLEAVAGE, SUBUNIT, INTERACTION WITH
RP CLCN7, AND SUBCELLULAR LOCATION.
RX PubMed=16525474; DOI=10.1038/nature04535;
RA Lange P.F., Wartosch L., Jentsch T.J., Fuhrmann J.C.;
RT "ClC-7 requires Ostm1 as a beta-subunit to support bone resorption and
RT lysosomal function.";
RL Nature 440:220-223(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND SER-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for osteoclast and melanocyte maturation and
CC function. {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16525474}.
CC -!- SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta
CC (OSTM1) subunits. {ECO:0000269|PubMed:16525474}.
CC -!- INTERACTION:
CC Q8BGT0; O70496: Clcn7; NbExp=7; IntAct=EBI-987431, EBI-987482;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:12627228,
CC ECO:0000269|PubMed:16525474}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12627228, ECO:0000269|PubMed:16525474}.
CC Note=Requires CLCN7 to travel to lysosomes.
CC -!- TISSUE SPECIFICITY: Expressed primarily in osteoclasts and melanocytes
CC as well as brain, kidney and spleen. Found at lower levels in the
CC thymus, testis, heart and liver. {ECO:0000269|PubMed:12627228}.
CC -!- DEVELOPMENTAL STAGE: Expression was detected in fetal liver neuronal
CC and bone tissues (12.5 dpc and 15.5 dpc). High expression was detected
CC in thymus and gut at 18.5 dpc and continued postnatally. Expression in
CC bone (mandible and vertebrae) and brain tissues (cerebellum,
CC hippocampus and cortex) remained high after birth. In addition high
CC expression was detected in kidney, spleen and skin at P5 and P10.
CC {ECO:0000269|PubMed:12627228}.
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:0000269|PubMed:16525474}.
CC -!- PTM: Highly N-glycosylated. {ECO:0000269|PubMed:16525474}.
CC -!- DISEASE: Note=Defects in Ostm1 are the cause of the spontaneous gray-
CC lethal (gl) mutant, which is responsible for a coat color defect and
CC for the development of the most severe autosomal recessive form of
CC osteopetrosis. Osteopetrosis is a rare genetic disease characterized by
CC abnormally dense bone, due to defective resorption of immature bone.
CC The disorder occurs in two forms: a severe autosomal recessive form
CC occurring in utero, infancy, or childhood, and a benign autosomal
CC dominant form occurring in adolescence or adulthood.
CC {ECO:0000269|PubMed:12627228}.
CC -!- SIMILARITY: Belongs to the OSTM1 family. {ECO:0000305}.
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DR EMBL; AF533890; AAO72748.1; -; mRNA.
DR EMBL; AK004546; BAC25087.1; -; mRNA.
DR EMBL; AK050513; BAC34300.1; -; mRNA.
DR EMBL; BC057635; AAH57635.1; -; mRNA.
DR CCDS; CCDS23814.1; -.
DR RefSeq; NP_766004.1; NM_172416.3.
DR AlphaFoldDB; Q8BGT0; -.
DR SMR; Q8BGT0; -.
DR BioGRID; 199939; 17.
DR IntAct; Q8BGT0; 4.
DR MINT; Q8BGT0; -.
DR STRING; 10090.ENSMUSP00000035516; -.
DR GlyConnect; 2571; 5 N-Linked glycans (4 sites).
DR GlyGen; Q8BGT0; 10 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q8BGT0; -.
DR PhosphoSitePlus; Q8BGT0; -.
DR EPD; Q8BGT0; -.
DR jPOST; Q8BGT0; -.
DR MaxQB; Q8BGT0; -.
DR PaxDb; Q8BGT0; -.
DR PeptideAtlas; Q8BGT0; -.
DR PRIDE; Q8BGT0; -.
DR ProteomicsDB; 294398; -.
DR Antibodypedia; 2255; 191 antibodies from 26 providers.
DR Ensembl; ENSMUST00000040718; ENSMUSP00000035516; ENSMUSG00000038280.
DR GeneID; 14628; -.
DR KEGG; mmu:14628; -.
DR UCSC; uc007eyu.2; mouse.
DR CTD; 28962; -.
DR MGI; MGI:2655574; Ostm1.
DR VEuPathDB; HostDB:ENSMUSG00000038280; -.
DR eggNOG; KOG4617; Eukaryota.
DR GeneTree; ENSGT00390000012341; -.
DR HOGENOM; CLU_070677_0_0_1; -.
DR InParanoid; Q8BGT0; -.
DR OMA; FQQVASK; -.
DR OrthoDB; 1105868at2759; -.
DR PhylomeDB; Q8BGT0; -.
DR TreeFam; TF323313; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 14628; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ostm1; mouse.
DR PRO; PR:Q8BGT0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BGT0; protein.
DR Bgee; ENSMUSG00000038280; Expressed in pigmented layer of retina and 221 other tissues.
DR ExpressionAtlas; Q8BGT0; baseline and differential.
DR Genevisible; Q8BGT0; MM.
DR GO; GO:0034707; C:chloride channel complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR GO; GO:0030321; P:transepithelial chloride transport; ISO:MGI.
DR InterPro; IPR019172; Osteopetrosis-assoc_TM_1.
DR PANTHER; PTHR15644; PTHR15644; 1.
DR Pfam; PF09777; OSTMP1; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..338
FT /note="Osteopetrosis-associated transmembrane protein 1"
FT /id="PRO_0000021964"
FT TOPO_DOM 35..288
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 38000 MW; 73EF8EE9ED760C08 CRC64;
MARDAELARS SGWPWRWLPA LLLLQLLRWR CALCALPFTS SRHPGFADLL SEQQLLEVQD
LTLSLLQGGG LGPLSLLPPD LPDLEPECRE LLMDFANSSA ELTACMVRSA RPVRLCQTCY
PLFQQVAIKM DNISRNIGNT SEGPRCGGSL LTADRMQIVL MVSEFFNSTW QEANCANCLT
NNGEDLSNNT EDFLSLFNKT LACFEHNLQG HTYSLLPPKN YSEVCRNCKE AYKNLSLLYS
QMQKLNGLEN KAEPETHLCI DVEDAMNITR KLWSRTFNCS VTCSDTVSVV AVSVFILFLP
VVFYLSSFLH SEQKKRKLIL PKRLKSSTSF ANIQENAT
