OCSTP_MOUSE
ID OCSTP_MOUSE Reviewed; 498 AA.
AC Q9D611; Q8C046;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Osteoclast stimulatory transmembrane protein;
DE Short=OC-STAMP;
GN Name=Ocstamp;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Olfactory bulb, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=18064667; DOI=10.1002/jcp.21331;
RA Yang M., Birnbaum M.J., MacKay C.A., Mason-Savas A., Thompson B.,
RA Odgren P.R.;
RT "Osteoclast stimulatory transmembrane protein (OC-STAMP), a novel protein
RT induced by RANKL that promotes osteoclast differentiation.";
RL J. Cell. Physiol. 215:497-505(2008).
RN [5]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=20882308; DOI=10.1007/s00726-010-0755-4;
RA Kim M.H., Park M., Baek S.H., Kim H.J., Kim S.H.;
RT "Molecules and signaling pathways involved in the expression of OC-STAMP
RT during osteoclastogenesis.";
RL Amino Acids 40:1447-1459(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=22337159; DOI=10.1002/jbmr.1575;
RA Miyamoto H., Suzuki T., Miyauchi Y., Iwasaki R., Kobayashi T., Sato Y.,
RA Miyamoto K., Hoshi H., Hashimoto K., Yoshida S., Hao W., Mori T.,
RA Kanagawa H., Katsuyama E., Fujie A., Morioka H., Matsumoto M., Chiba K.,
RA Takeya M., Toyama Y., Miyamoto T.;
RT "Osteoclast stimulatory transmembrane protein and dendritic cell-specific
RT transmembrane protein cooperatively modulate cell-cell fusion to form
RT osteoclasts and foreign body giant cells.";
RL J. Bone Miner. Res. 27:1289-1297(2012).
CC -!- FUNCTION: Probable cell surface receptor that plays a role in cellular
CC fusion and cell differentiation. Cooperates with DCSTAMP in modulating
CC cell-cell fusion in both osteoclasts and foreign body giant cells
CC (FBGCs). Involved in osteoclast bone resorption. Promotes osteoclast
CC differentiation and may play a role in the multinucleated osteoclast
CC maturation. {ECO:0000269|PubMed:18064667, ECO:0000269|PubMed:20882308,
CC ECO:0000269|PubMed:22337159}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in osteoclast (at protein level).
CC Ubiquitous. Highly expressed in multi-nuclear osteoclast cells compared
CC to mono-nuclear macrophages. Expressed in foreign body giant cells
CC (FBGCs). {ECO:0000269|PubMed:18064667, ECO:0000269|PubMed:20882308,
CC ECO:0000269|PubMed:22337159}.
CC -!- INDUCTION: Up-regulated during osteoclast and foreign body giant cells
CC (FBGCs) differentiation by TNFSF11 and cytokines. Down-regulated by
CC estrogen. {ECO:0000269|PubMed:18064667, ECO:0000269|PubMed:20882308,
CC ECO:0000269|PubMed:22337159}.
CC -!- DISRUPTION PHENOTYPE: Mice show a lack of multi-nuclear osteoclast and
CC foreign body giant cell formation and a bone-resorbing efficiency
CC reduction. {ECO:0000269|PubMed:22337159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27818.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK032330; BAC27818.1; ALT_FRAME; mRNA.
DR EMBL; BC020160; AAH20160.1; -; mRNA.
DR EMBL; AK014751; BAB29531.1; -; mRNA.
DR EMBL; AK042271; BAC31210.1; -; mRNA.
DR EMBL; AL591064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17080.1; -.
DR RefSeq; NP_083297.1; NM_029021.1.
DR AlphaFoldDB; Q9D611; -.
DR STRING; 10090.ENSMUSP00000029213; -.
DR iPTMnet; Q9D611; -.
DR PhosphoSitePlus; Q9D611; -.
DR PaxDb; Q9D611; -.
DR PRIDE; Q9D611; -.
DR Antibodypedia; 28113; 17 antibodies from 9 providers.
DR DNASU; 74614; -.
DR Ensembl; ENSMUST00000029213; ENSMUSP00000029213; ENSMUSG00000027670.
DR GeneID; 74614; -.
DR KEGG; mmu:74614; -.
DR UCSC; uc008nxr.1; mouse.
DR CTD; 128506; -.
DR MGI; MGI:1921864; Ocstamp.
DR VEuPathDB; HostDB:ENSMUSG00000027670; -.
DR eggNOG; ENOG502QWNK; Eukaryota.
DR GeneTree; ENSGT00940000153269; -.
DR HOGENOM; CLU_045128_0_0_1; -.
DR InParanoid; Q9D611; -.
DR OMA; WRSWHLG; -.
DR OrthoDB; 1224213at2759; -.
DR PhylomeDB; Q9D611; -.
DR TreeFam; TF332562; -.
DR BioGRID-ORCS; 74614; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9D611; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D611; protein.
DR Bgee; ENSMUSG00000027670; Expressed in intramembranous bone and 27 other tissues.
DR Genevisible; Q9D611; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0072674; P:multinuclear osteoclast differentiation; IMP:UniProtKB.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; IGI:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; IDA:UniProtKB.
DR InterPro; IPR012858; DC_STAMP-like.
DR Pfam; PF07782; DC_STAMP; 1.
PE 1: Evidence at protein level;
KW Differentiation; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..498
FT /note="Osteoclast stimulatory transmembrane protein"
FT /id="PRO_0000342122"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 449..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 54574 MW; FD27C03258923B55 CRC64;
MRTIRAATEH LFGLGWKFWR LGICKAVVPL QAAWKAFSQP VPASCNELLT QLLLCVSLAS
LIAGLAHHWL VSLQLYPLGP PALVTSLCGL FVFLSLGLVP PIRCLFVLSV PTLGSKQGRR
LLLSYSAANL AVAVVPNVLG NVRAAGQVLS CVTEGSLESL LNTTYQLRQA ARELGPASRA
GSRSLTFEVE GKGSAFRLHM HTITQEILED FSGLEFLARA ALGTQRVVTG LFLLGLLGES
AWYLHRYLTD LRFDNIYATR QLVRQLAQAG ATHLLTSPPP WLLQTAQPKL SREELLSCLL
RLGLLALLLV ATAVTVASDY GAFLLAQAAV AWAQKLPTVP ITLTVKYDAS YKVLDFILFV
LNQPPVESVF ASMQRSFQWE LRFTPHDCHL PQAQPPRVTA ALAAGALQLL AGATLVLQAY
AWRLRHTIAA SFFPDQEARR LSHLQARLQR RHNQSDHLNK QPGTMATRES RKPGQGTRTL
ESQGPQAHDS LGPPYDLE
