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Dendritic cell-specific transmembrane protein (DC-STAMP) (hDC-STAMP) (Dendrocyte-expressed seven transmembrane protein) (IL-four-induced protein) (FIND) (Transmembrane 7 superfamily member 4)

 DCSTP_HUMAN             Reviewed;         470 AA.
Q9H295; B7ZVW2; E7ESG0; Q2M2D5;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 123.
RecName: Full=Dendritic cell-specific transmembrane protein;
Short=DC-STAMP;
Short=hDC-STAMP;
AltName: Full=Dendrocyte-expressed seven transmembrane protein;
AltName: Full=IL-four-induced protein;
Short=FIND;
AltName: Full=Transmembrane 7 superfamily member 4;
Name=DCSTAMP; Synonyms=TM7SF4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG39167.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
TOPOLOGY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Dendritic cell {ECO:0000312|EMBL:AAG39167.1};
PubMed=11169400;
DOI=10.1002/1521-4141(200012)30:12<3585::AID-IMMU3585>3.0.CO;2-Y;
Hartgers F.C., Vissers J.L.M., Looman M.W.G., van Zoelen C.,
Huffin C., Figdor C.G., Adema G.J.;
"DC-STAMP, a novel multimembrane-spanning molecule preferentially
expressed by dendritic cells.";
Eur. J. Immunol. 30:3585-3590(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAL02152.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Macrophage {ECO:0000269|PubMed:11345586}, and Monocyte;
PubMed=11345586; DOI=10.1007/s002510100306;
Staege H., Brauchlin A., Schoedon G., Schaffner A.;
"Two novel genes FIND and LIND differentially expressed in deactivated
and Listeria-infected human macrophages.";
Immunogenetics 53:105-113(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4] {ECO:0000312|EMBL:AAH69349.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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.
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]
INTERACTION WITH CREB3.
PubMed=20546900; DOI=10.1016/j.molimm.2010.04.019;
Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W.,
Hendriks I.A., Jansen B.J., Adema G.J.;
"DC-STAMP interacts with ER-resident transcription factor LUMAN which
becomes activated during DC maturation.";
Mol. Immunol. 47:1963-1973(2010).
-!- 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.
-!- SUBUNIT: 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) (By similarity). Interacts with CREB3.
{ECO:0000250, ECO:0000269|PubMed:20546900}.
-!- INTERACTION:
O43889-2:CREB3; NbExp=6; IntAct=EBI-6095316, EBI-625022;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endoplasmic reticulum membrane;
Multi-pass membrane protein. Endoplasmic reticulum-Golgi
intermediate compartment membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Endosome {ECO:0000250}.
Note=Localizes 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 (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H295-1; Sequence=Displayed;
Name=2;
IsoId=Q9H295-2; Sequence=VSP_044787, VSP_044788;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Preferentially expressed by dendritic cells
(DCs). Detected in both immature and mature DCs. Highly expressed
in lymph nodes, lung, kidney and liver. Expressed at lower levels
in pancreas, bone marrow, spleen, leukocytes, in freshly isolated
peripheral blood mononuclear cells (PBMC) and B-cells. Not
expressed in freshly isolated monocytes.
{ECO:0000269|PubMed:11169400, ECO:0000269|PubMed:11345586}.
-!- DEVELOPMENTAL STAGE: Constitutively expressed in dendritic cells
from day 3-8 in culture. {ECO:0000269|PubMed:11169400}.
-!- INDUCTION: Expression is down-regulated by dexamethasone and up-
regulated by IL4/interleukin-4 in macrophages. Down-regulated in
CD40L-activated dendritic cells. {ECO:0000269|PubMed:11169400,
ECO:0000269|PubMed:11345586}.
-!- 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 (By
similarity). {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF305068; AAG39167.1; -; mRNA.
EMBL; AF277290; AAL02152.1; -; mRNA.
EMBL; AP003471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069349; AAH69349.1; -; mRNA.
EMBL; BC112018; AAI12019.1; -; mRNA.
EMBL; BC112020; AAI12021.1; -; mRNA.
EMBL; BC171732; AAI71732.1; -; mRNA.
CCDS; CCDS59111.1; -. [Q9H295-2]
CCDS; CCDS6301.1; -. [Q9H295-1]
RefSeq; NP_001244246.1; NM_001257317.1. [Q9H295-2]
RefSeq; NP_110415.1; NM_030788.3. [Q9H295-1]
RefSeq; XP_011515623.1; XM_011517321.1. [Q9H295-1]
RefSeq; XP_011515626.1; XM_011517324.1. [Q9H295-2]
RefSeq; XP_016869367.1; XM_017013878.1.
RefSeq; XP_016869369.1; XM_017013880.1.
UniGene; Hs.652230; -.
UniGene; Hs.741954; -.
ProteinModelPortal; Q9H295; -.
SMR; Q9H295; -.
BioGrid; 123504; 1.
IntAct; Q9H295; 1.
STRING; 9606.ENSP00000297581; -.
TCDB; 1.N.1.1.1; the osteoclast fusion complex (ofc) family.
iPTMnet; Q9H295; -.
PhosphoSitePlus; Q9H295; -.
BioMuta; DCSTAMP; -.
DMDM; 71153342; -.
EPD; Q9H295; -.
PaxDb; Q9H295; -.
PRIDE; Q9H295; -.
ProteomicsDB; 80513; -.
Ensembl; ENST00000297581; ENSP00000297581; ENSG00000164935. [Q9H295-1]
Ensembl; ENST00000517991; ENSP00000428869; ENSG00000164935. [Q9H295-2]
Ensembl; ENST00000622554; ENSP00000480546; ENSG00000164935. [Q9H295-2]
GeneID; 81501; -.
KEGG; hsa:81501; -.
UCSC; uc003ylx.3; human. [Q9H295-1]
CTD; 81501; -.
DisGeNET; 81501; -.
EuPathDB; HostDB:ENSG00000164935.6; -.
GeneCards; DCSTAMP; -.
HGNC; HGNC:18549; DCSTAMP.
MIM; 605933; gene.
neXtProt; NX_Q9H295; -.
OpenTargets; ENSG00000164935; -.
PharmGKB; PA134938623; -.
eggNOG; ENOG410IUUT; Eukaryota.
eggNOG; ENOG4111T6M; LUCA.
GeneTree; ENSGT00730000111246; -.
HOGENOM; HOG000060200; -.
HOVERGEN; HBG085084; -.
InParanoid; Q9H295; -.
OMA; PRSPGWM; -.
OrthoDB; EOG091G0GX3; -.
PhylomeDB; Q9H295; -.
TreeFam; TF318254; -.
Reactome; R-HSA-8874211; CREB3 factors activate genes.
GenomeRNAi; 81501; -.
PRO; PR:Q9H295; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000164935; Expressed in 75 organ(s), highest expression level in amygdala.
CleanEx; HS_TM7SF4; -.
Genevisible; Q9H295; HS.
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; ISS:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA: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; IDA:UniProtKB.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:0072675; P:osteoclast fusion; ISS:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
GO; GO:0034241; P:positive regulation of macrophage fusion; ISS:UniProtKB.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS: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;
Polymorphism; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 470 Dendritic cell-specific transmembrane
protein.
/FTId=PRO_0000072584.
TOPO_DOM 1 34 Cytoplasmic. {ECO:0000255}.
TRANSMEM 35 55 Helical. {ECO:0000255}.
TOPO_DOM 56 57 Extracellular. {ECO:0000255}.
TRANSMEM 58 78 Helical. {ECO:0000255}.
TOPO_DOM 79 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:0000269|PubMed:11169400}.
COMPBIAS 60 63 Poly-Ala. {ECO:0000255}.
VAR_SEQ 277 283 YVIIPTF -> FISGFQS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044787.
VAR_SEQ 284 470 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044788.
VARIANT 349 349 D -> G (in dbSNP:rs3802204).
/FTId=VAR_051438.
CONFLICT 200 200 M -> R (in Ref. 4; AAI71732).
{ECO:0000305}.
SEQUENCE 470 AA; 53393 MW; EA2B858FD2C7560C CRC64;
MGIWTSGTDI FLSLWEIYVS PRSPGWMDFI QHLGVCCLVA LISVGLLSVA ACWFLPSIIA
AAASWIITCV LLCCSKHARC FILLVFLSCG LREGRNALIA AGTGIVILGH VENIFHNFKG
LLDGMTCNLR AKSFSIHFPL LKKYIEAIQW IYGLATPLSV FDDLVSWNQT LAVSLFSPSH
VLEAQLNDSK GEVLSVLYQM ATTTEVLSSL GQKLLAFAGL SLVLLGTGLF MKRFLGPCGW
KYENIYITRQ FVQFDERERH QQRPCVLPLN KEERRKYVII PTFWPTPKER KNLGLFFLPI
LIHLCIWVLF AAVDYLLYRL IFSVSKQFQS LPGFEVHLKL HGEKQGTQDI IHDSSFNISV
FEPNCIPKPK FLLSETWVPL SVILLILVML GLLSSILMQL KILVSASFYP SVERKRIQYL
HAKLLKKRSK QPLGEVKRRL SLYLTKIHFW LPVLKMIRKK QMDMASADKS


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