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Dendritic cell-specific transmembrane protein (DC-STAMP) (mDC-STAMP) (Dendrocyte-expressed seven transmembrane protein) (Transmembrane 7 superfamily member 4)

 DCSTP_MOUSE             Reviewed;         470 AA.
Q7TNJ0; B2RT61; Q6R315; Q7TNI9; Q9D619;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
10-MAY-2017, entry version 97.
RecName: Full=Dendritic cell-specific transmembrane protein;
Short=DC-STAMP;
Short=mDC-STAMP;
AltName: Full=Dendrocyte-expressed seven transmembrane protein;
AltName: Full=Transmembrane 7 superfamily member 4;
Name=Dcstamp; Synonyms=Tm7sf4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC81438.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
LOCATION, AND INDUCTION.
TISSUE=Macrophage {ECO:0000269|PubMed:15452179};
PubMed=15452179; DOI=10.1084/jem.20040518;
Kukita T., Wada N., Kukita A., Kakimoto T., Sandra F., Toh K.,
Nagata K., Iijima T., Horiuchi M., Matsusaki H., Hieshima K.,
Yoshie O., Nomiyama H.;
"RANKL-induced DC-STAMP is essential for osteoclastogenesis.";
J. Exp. Med. 200:941-946(2004).
[2] {ECO:0000305, ECO:0000312|EMBL:AAR99406.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4).
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAR99406.1};
TISSUE=Osteoclast {ECO:0000312|EMBL:AAR99406.1};
Miyamoto T., Sawatani Y., Suda T.;
"Identification and characterization of osteoclast specific
molecules.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, GLYCOSYLATION, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=15601667; DOI=10.1189/jlb.0804441;
Eleveld-Trancikova D., Triantis V., Moulin V., Looman M.W., Wijers M.,
Fransen J.A., Lemckert A.A., Havenga M.J., Figdor C.G., Janssen R.A.,
Adema G.J.;
"The dendritic cell-derived protein DC-STAMP is highly conserved and
localizes to the endoplasmic reticulum.";
J. Leukoc. Biol. 77:337-343(2005).
[6]
FUNCTION IN CELL FUSION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
DISRUPTION PHENOTYPE, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=16061724; DOI=10.1084/jem.20050645;
Yagi M., Miyamoto T., Sawatani Y., Iwamoto K., Hosogane N., Fujita N.,
Morita K., Ninomiya K., Suzuki T., Miyamoto K., Oike Y., Takeya M.,
Toyama Y., Suda T.;
"DC-STAMP is essential for cell-cell fusion in osteoclasts and foreign
body giant cells.";
J. Exp. Med. 202:345-351(2005).
[7]
FUNCTION IN CELL FUSION, AND DISRUPTION PHENOTYPE.
PubMed=16937266; DOI=10.1007/s00774-006-0697-9;
Yagi M., Miyamoto T., Toyama Y., Suda T.;
"Role of DC-STAMP in cellular fusion of osteoclasts and macrophage
giant cells.";
J. Bone Miner. Metab. 24:355-358(2006).
[8]
FUNCTION IN CELL FUSION, AND DISRUPTION PHENOTYPE.
PubMed=17164993; DOI=10.3109/s10165-006-0524-0;
Miyamoto T.;
"The dendritic cell-specific transmembrane protein DC-STAMP is
essential for osteoclast fusion and osteoclast bone-resorbing
activity.";
Mod. Rheumatol. 16:341-342(2006).
[9]
FUNCTION IN IMMUNE TOLERANCE, SUBCELLULAR LOCATION, AND DISRUPTION
PHENOTYPE.
PubMed=18653699; DOI=10.1093/intimm/dxn082;
Sawatani Y., Miyamoto T., Nagai S., Maruya M., Imai J., Miyamoto K.,
Fujita N., Ninomiya K., Suzuki T., Iwasaki R., Toyama Y.,
Shinohara M., Koyasu S., Suda T.;
"The role of DC-STAMP in maintenance of immune tolerance through
regulation of dendritic cell function.";
Int. Immunol. 20:1259-1268(2008).
[10]
FUNCTION IN MYELOID DIFFERENTIATION.
PubMed=17713547; DOI=10.1038/sj.leu.2404910;
Eleveld-Trancikova D., Janssen R.A., Hendriks I.A., Looman M.W.,
Moulin V., Jansen B.J., Jansen J.H., Figdor C.G., Adema G.J.;
"The DC-derived protein DC-STAMP influences differentiation of myeloid
cells.";
Leukemia 22:455-459(2008).
[11]
FUNCTION, INTERACTION WITH OS9, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=18952287; DOI=10.1016/j.molimm.2008.06.032;
Jansen B.J., Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.,
Hendriks I.A., Looman M.G., Leusen J.H., Adema G.J.;
"OS9 interacts with DC-STAMP and modulates its intracellular
localization in response to TLR ligation.";
Mol. Immunol. 46:505-515(2009).
[12]
FUNCTION IN MYELOID DIFFERENTIATION, HOMODIMERIZATION, AND SUBCELLULAR
LOCATION.
PubMed=20039274; DOI=10.1002/jcp.22012;
Mensah K.A., Ritchlin C.T., Schwarz E.M.;
"RANKL induces heterogeneous DC-STAMP(lo) and DC-STAMP(hi) osteoclast
precursors of which the DC-STAMP(lo) precursors are the master
fusogens.";
J. Cell. Physiol. 223:76-83(2010).
[13]
FUNCTION IN CELL FUSION, DISRUPTION PHENOTYPE, INDUCTION, AND TISSUE
SPECIFICITY.
PubMed=22337159; DOI=10.1002/jbmr.1575;
Miyamoto H., Suzuki T., Miyauchi Y., Iwasaki R., Kobayashi T.,
Sato Y., Miyamoto K., Hoshi H., Hashimoto K., Yoshida S., Hao W.,
Mori T., Kanagawa H., Katsuyama E., Fujie A., Morioka H.,
Matsumoto M., Chiba K., Takeya M., Toyama Y., Miyamoto T.;
"Osteoclast stimulatory transmembrane protein and dendritic cell-
specific transmembrane protein cooperatively modulate cell-cell fusion
to form osteoclasts and foreign body giant cells.";
J. Bone Miner. Res. 27:1289-1297(2012).
-!- FUNCTION: Probable cell surface receptor that plays several roles
in cellular fusion, cell differentiation, bone and immune
homeostasis. Plays a role in TNFSF11-mediated osteoclastogenesis.
Cooperates with OCSTAMP in modulating cell-cell fusion in both
osteoclasts and foreign body giant cells (FBGCs). Participates in
osteoclast bone resorption. Involved in inducing the expression of
tartrate-resistant acid phosphatase in osteoclast precursors.
Plays a role in haematopoietic stem cell differentiation of bone
marrow cells toward the myeloid lineage. Inhibits the development
of neutrophilic granulocytes. Plays also a role in the regulation
of dendritic cell (DC) antigen presentation activity by
controlling phagocytic activity. Involved in the maintenance of
immune self-tolerance and avoidance of autoimmune reactions.
{ECO:0000269|PubMed:15452179, ECO:0000269|PubMed:16061724,
ECO:0000269|PubMed:16937266, ECO:0000269|PubMed:17164993,
ECO:0000269|PubMed:17713547, ECO:0000269|PubMed:18653699,
ECO:0000269|PubMed:18952287, ECO:0000269|PubMed:20039274,
ECO:0000269|PubMed:22337159}.
-!- SUBUNIT: Interacts with CREB3 (By similarity). Monomer. Homodimer.
Isoform 1 interacts (via the C-terminus cytoplasmic tail) with OS9
isoform 1 (via the C-terminus tail); the interaction induces
DCSTAMP redistribution to the endoplasmic reticulum-Golgi
intermediate compartment. Isoform 1 interacts (via the C-terminus
cytoplasmic tail) with OS9 isoform 2 (via the C-terminus tail).
{ECO:0000250, ECO:0000269|PubMed:18952287}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
membrane protein {ECO:0000305}. Endoplasmic reticulum membrane;
Multi-pass membrane protein. Endoplasmic reticulum-Golgi
intermediate compartment membrane; Multi-pass membrane protein.
Endosome. Note=Localized to the cell surface in osteoclasts and
undifferentiated monocytes. Intracellular internalized DCSTAMP is
detected in a fraction of RANKL-induced osteoclast precursor.
Colocalizes with OS9 in the endoplasmic reticulum (ER) of immature
dendritic cell (DC). Translocates from the endoplasmic reticulum
to the intermediate/Golgi compartment upon maturation of DC in a
OS9-dependent manner. Colocalizes with LAMP1 in endosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1 {ECO:0000269|PubMed:15452179};
IsoId=Q7TNJ0-1; Sequence=Displayed;
Name=2 {ECO:0000269|Ref.2};
IsoId=Q7TNJ0-2; Sequence=VSP_051763;
Name=3 {ECO:0000269|PubMed:15452179};
IsoId=Q7TNJ0-3; Sequence=VSP_051765;
Name=4 {ECO:0000269|Ref.2};
IsoId=Q7TNJ0-4; Sequence=VSP_051764;
-!- TISSUE SPECIFICITY: Expressed in macrophages and bone marrow
dendritic cells (BM-DC). Weakly expressed in the spleen and lymph
node. Highly expressed in multi-nuclear osteoclasts compared to
mono-nuclear macrophages. Expressed in foreign body giant cells
(FBGCs). Isoform 1 and isoform 2 are expressed in osteoclasts.
{ECO:0000269|PubMed:15601667, ECO:0000269|PubMed:16061724,
ECO:0000269|PubMed:22337159}.
-!- INDUCTION: Up-regulated by IL4/interleukin-4, macrophage colony-
stimulating factor (M-CSF), receptor activator of NF-KB ligand
(RANKL), lipopolysaccharide (LPS) and toll-like receptor (TLR).
Up-regulated by TNFSF11-induced osteoclast differentiation in
combination with TNF-alpha. Down-regulated upon dendritic cell
(DC) maturation. {ECO:0000269|PubMed:15452179,
ECO:0000269|PubMed:15601667, ECO:0000269|PubMed:16061724,
ECO:0000269|PubMed:18952287, ECO:0000269|PubMed:22337159}.
-!- DOMAIN: Several domains are necessary for interacting with OS9.
The region in the cytoplasmic tail that is necessary for
interaction with OS9, is also required for its transport.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:15601667}.
-!- DISRUPTION PHENOTYPE: Mice show a lack of osteoclast and foreign
body giant cells multi-nuclear formation and a bone-resorbing
efficiency reduction. Mice show increased bone mass. Older (>12
months) mice suffered from multisystemic inflammations in the
kidney, lung and salivary gland. Mice show autoimmune symptoms,
like dendritic cells (DC) with increased phagocytotic activity and
antigen presentation. {ECO:0000269|PubMed:16061724,
ECO:0000269|PubMed:16937266, ECO:0000269|PubMed:17164993,
ECO:0000269|PubMed:18653699, ECO:0000269|PubMed:22337159}.
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EMBL; AB109560; BAC81438.1; -; mRNA.
EMBL; AB109561; BAC81439.1; -; mRNA.
EMBL; AY517483; AAR99406.1; -; mRNA.
EMBL; AY517484; AAR99407.1; -; mRNA.
EMBL; AY517485; AAR99408.1; -; mRNA.
EMBL; AK014697; BAB29508.1; -; mRNA.
EMBL; BC139146; AAI39147.1; -; mRNA.
CCDS; CCDS27444.1; -. [Q7TNJ0-1]
RefSeq; NP_001276437.1; NM_001289508.1. [Q7TNJ0-3]
RefSeq; NP_001276441.1; NM_001289512.1. [Q7TNJ0-4]
RefSeq; NP_083698.1; NM_029422.4. [Q7TNJ0-1]
UniGene; Mm.159563; -.
STRING; 10090.ENSMUSP00000022913; -.
PhosphoSitePlus; Q7TNJ0; -.
PaxDb; Q7TNJ0; -.
PRIDE; Q7TNJ0; -.
Ensembl; ENSMUST00000022913; ENSMUSP00000022913; ENSMUSG00000022303. [Q7TNJ0-1]
GeneID; 75766; -.
KEGG; mmu:75766; -.
UCSC; uc007voi.2; mouse. [Q7TNJ0-1]
UCSC; uc007voj.2; mouse. [Q7TNJ0-4]
UCSC; uc011zsn.2; mouse. [Q7TNJ0-3]
CTD; 81501; -.
MGI; MGI:1923016; Dcstamp.
eggNOG; ENOG410IUUT; Eukaryota.
eggNOG; ENOG4111T6M; LUCA.
GeneTree; ENSGT00730000111246; -.
HOGENOM; HOG000060200; -.
HOVERGEN; HBG085084; -.
InParanoid; Q7TNJ0; -.
OMA; PVLKMIR; -.
OrthoDB; EOG091G0GX3; -.
PhylomeDB; Q7TNJ0; -.
TreeFam; TF318254; -.
PRO; PR:Q7TNJ0; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022303; -.
CleanEx; MM_TM7SF4; -.
Genevisible; Q7TNJ0; MM.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0071353; P:cellular response to interleukin-4; ISS:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IDA:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
GO; GO:0072675; P:osteoclast fusion; IDA:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; IMP:UniProtKB.
GO; GO:0034241; P:positive regulation of macrophage fusion; IDA:UniProtKB.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:UniProtKB.
InterPro; IPR012858; DC_STAMP-like.
Pfam; PF07782; DC_STAMP; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Differentiation; Endoplasmic reticulum; Endosome; Immunity; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 470 Dendritic cell-specific transmembrane
protein.
/FTId=PRO_0000072585.
TOPO_DOM 1 33 Cytoplasmic. {ECO:0000255}.
TRANSMEM 34 54 Helical. {ECO:0000255}.
TOPO_DOM 55 55 Extracellular. {ECO:0000255}.
TRANSMEM 56 76 Helical. {ECO:0000255}.
TOPO_DOM 77 97 Cytoplasmic. {ECO:0000255}.
TRANSMEM 98 118 Helical. {ECO:0000255}.
TOPO_DOM 119 209 Extracellular. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 292 Cytoplasmic. {ECO:0000255}.
TRANSMEM 293 313 Helical. {ECO:0000255}.
TOPO_DOM 314 376 Extracellular. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 470 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 95 177 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_051763.
VAR_SEQ 344 446 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.2}.
/FTId=VSP_051764.
VAR_SEQ 344 399 Missing (in isoform 3).
{ECO:0000303|PubMed:15452179}.
/FTId=VSP_051765.
CONFLICT 449 449 F -> L (in Ref. 2; AAR99408 and 3).
{ECO:0000305}.
SEQUENCE 470 AA; 53876 MW; 9CCFBB82DFC2BE6E CRC64;
MRLWTLGTSI FLRLWGTYVF PRSPSWLDFI QHLGVCCFVA FLSVSLFSAA FYWILPPVAL
LSSVWMITCV FLCCSKRARC FILLAVLSCG LREGRNALIA AGTGVVIFGH VENIFYNFRG
LLDSMTCNLR AKSFSVHFPL LKRYTEAIQW IYGLATPLNL FDDLVSWNQT LVVSLFSPSH
ALEAHMNDTR GEVLGVLHHM VVTTELLTSV GQKLLALAGL LLILVSTGLF LKRFLGPCGW
KYENVYITKQ FVRFDEKERH QQRPCVLPLN KKERKKYVIV PSLQLTPKEK KTLGLFFLPV
LTYLYMWVLF AAVDYLLYRL ISSMNKQFQS LPGLEVHLKL RGEKQGTQGV VHDSAFNISM
FEPSCIPKPR LSVSETWVPL SIILLTLIIL GLLSSMLMQL KILVSVSFYP KVERERIEYL
HAKLLEKRSK QPLREADGKP SLYFKKIHFW FPVLKMIRKK QTIPANEDDL


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