DCSTP_HUMAN
ID DCSTP_HUMAN Reviewed; 470 AA.
AC Q9H295; B7ZVW2; E7ESG0; Q2M2D5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Dendritic cell-specific transmembrane protein;
DE Short=DC-STAMP;
DE Short=hDC-STAMP;
DE AltName: Full=Dendrocyte-expressed seven transmembrane protein;
DE AltName: Full=IL-four-induced protein;
DE Short=FIND;
DE AltName: Full=Transmembrane 7 superfamily member 4;
GN Name=DCSTAMP; Synonyms=TM7SF4;
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] {ECO:0000305, ECO:0000312|EMBL:AAG39167.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TOPOLOGY,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:AAG39167.1};
RX PubMed=11169400;
RX DOI=10.1002/1521-4141(200012)30:12<3585::aid-immu3585>3.0.co;2-y;
RA Hartgers F.C., Vissers J.L.M., Looman M.W.G., van Zoelen C., Huffin C.,
RA Figdor C.G., Adema G.J.;
RT "DC-STAMP, a novel multimembrane-spanning molecule preferentially expressed
RT by dendritic cells.";
RL Eur. J. Immunol. 30:3585-3590(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAL02152.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Macrophage {ECO:0000269|PubMed:11345586}, and Monocyte;
RX PubMed=11345586; DOI=10.1007/s002510100306;
RA Staege H., Brauchlin A., Schoedon G., Schaffner A.;
RT "Two novel genes FIND and LIND differentially expressed in deactivated and
RT Listeria-infected human macrophages.";
RL Immunogenetics 53:105-113(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4] {ECO:0000312|EMBL:AAH69349.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=15601667; DOI=10.1189/jlb.0804441;
RA Eleveld-Trancikova D., Triantis V., Moulin V., Looman M.W., Wijers M.,
RA Fransen J.A., Lemckert A.A., Havenga M.J., Figdor C.G., Janssen R.A.,
RA Adema G.J.;
RT "The dendritic cell-derived protein DC-STAMP is highly conserved and
RT localizes to the endoplasmic reticulum.";
RL J. Leukoc. Biol. 77:337-343(2005).
RN [6]
RP INTERACTION WITH CREB3.
RX PubMed=20546900; DOI=10.1016/j.molimm.2010.04.019;
RA Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W.,
RA Hendriks I.A., Jansen B.J., Adema G.J.;
RT "DC-STAMP interacts with ER-resident transcription factor LUMAN which
RT becomes activated during DC maturation.";
RL Mol. Immunol. 47:1963-1973(2010).
CC -!- FUNCTION: Probable cell surface receptor that plays several roles in
CC cellular fusion, cell differentiation, bone and immune homeostasis.
CC Plays a role in TNFSF11-mediated osteoclastogenesis. Cooperates with
CC OCSTAMP in modulating cell-cell fusion in both osteoclasts and foreign
CC body giant cells (FBGCs). Participates in osteoclast bone resorption.
CC Involved in inducing the expression of tartrate-resistant acid
CC phosphatase in osteoclast precursors. Plays a role in haematopoietic
CC stem cell differentiation of bone marrow cells toward the myeloid
CC lineage. Inhibits the development of neutrophilic granulocytes. Plays
CC also a role in the regulation of dendritic cell (DC) antigen
CC presentation activity by controlling phagocytic activity. Involved in
CC the maintenance of immune self-tolerance and avoidance of autoimmune
CC reactions.
CC -!- SUBUNIT: Monomer. Homodimer. Isoform 1 interacts (via the C-terminus
CC cytoplasmic tail) with OS9 isoform 1 (via the C-terminus tail); the
CC interaction induces DCSTAMP redistribution to the endoplasmic
CC reticulum-Golgi intermediate compartment. Isoform 1 interacts (via the
CC C-terminus cytoplasmic tail) with OS9 isoform 2 (via the C-terminus
CC tail) (By similarity). Interacts with CREB3. {ECO:0000250,
CC ECO:0000269|PubMed:20546900}.
CC -!- INTERACTION:
CC Q9H295; O43889-2: CREB3; NbExp=6; IntAct=EBI-6095316, EBI-625022;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Endosome {ECO:0000250}. Note=Localizes to the cell surface in
CC osteoclasts and undifferentiated monocytes. Intracellular internalized
CC DCSTAMP is detected in a fraction of RANKL-induced osteoclast
CC precursor. Colocalizes with OS9 in the endoplasmic reticulum (ER) of
CC immature dendritic cell (DC). Translocates from the endoplasmic
CC reticulum to the intermediate/Golgi compartment upon maturation of DC
CC in a OS9-dependent manner. Colocalizes with LAMP1 in endosomes (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H295-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H295-2; Sequence=VSP_044787, VSP_044788;
CC -!- TISSUE SPECIFICITY: Preferentially expressed by dendritic cells (DCs).
CC Detected in both immature and mature DCs. Highly expressed in lymph
CC nodes, lung, kidney and liver. Expressed at lower levels in pancreas,
CC bone marrow, spleen, leukocytes, in freshly isolated peripheral blood
CC mononuclear cells (PBMC) and B-cells. Not expressed in freshly isolated
CC monocytes. {ECO:0000269|PubMed:11169400, ECO:0000269|PubMed:11345586}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed in dendritic cells from
CC day 3-8 in culture. {ECO:0000269|PubMed:11169400}.
CC -!- INDUCTION: Expression is down-regulated by dexamethasone and up-
CC regulated by IL4/interleukin-4 in macrophages. Down-regulated in CD40L-
CC activated dendritic cells. {ECO:0000269|PubMed:11169400,
CC ECO:0000269|PubMed:11345586}.
CC -!- DOMAIN: Several domains are necessary for interacting with OS9. The
CC region in the cytoplasmic tail that is necessary for interaction with
CC OS9, is also required for its transport (By similarity). {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
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DR EMBL; AF305068; AAG39167.1; -; mRNA.
DR EMBL; AF277290; AAL02152.1; -; mRNA.
DR EMBL; AP003471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069349; AAH69349.1; -; mRNA.
DR EMBL; BC112018; AAI12019.1; -; mRNA.
DR EMBL; BC112020; AAI12021.1; -; mRNA.
DR EMBL; BC171732; AAI71732.1; -; mRNA.
DR CCDS; CCDS59111.1; -. [Q9H295-2]
DR CCDS; CCDS6301.1; -. [Q9H295-1]
DR RefSeq; NP_001244246.1; NM_001257317.1. [Q9H295-2]
DR RefSeq; NP_110415.1; NM_030788.3. [Q9H295-1]
DR RefSeq; XP_011515623.1; XM_011517321.1. [Q9H295-1]
DR RefSeq; XP_011515626.1; XM_011517324.1. [Q9H295-2]
DR RefSeq; XP_016869367.1; XM_017013878.1.
DR RefSeq; XP_016869369.1; XM_017013880.1.
DR AlphaFoldDB; Q9H295; -.
DR BioGRID; 123504; 1.
DR IntAct; Q9H295; 1.
DR STRING; 9606.ENSP00000297581; -.
DR TCDB; 1.N.1.1.1; the osteoclast fusion complex (ofc) family.
DR iPTMnet; Q9H295; -.
DR PhosphoSitePlus; Q9H295; -.
DR BioMuta; DCSTAMP; -.
DR DMDM; 71153342; -.
DR PaxDb; Q9H295; -.
DR PeptideAtlas; Q9H295; -.
DR PRIDE; Q9H295; -.
DR ProteomicsDB; 80513; -. [Q9H295-1]
DR Antibodypedia; 42882; 80 antibodies from 17 providers.
DR DNASU; 81501; -.
DR Ensembl; ENST00000297581.2; ENSP00000297581.2; ENSG00000164935.6. [Q9H295-1]
DR Ensembl; ENST00000517991.5; ENSP00000428869.1; ENSG00000164935.6. [Q9H295-2]
DR Ensembl; ENST00000622554.1; ENSP00000480546.1; ENSG00000164935.6. [Q9H295-2]
DR GeneID; 81501; -.
DR KEGG; hsa:81501; -.
DR MANE-Select; ENST00000297581.2; ENSP00000297581.2; NM_030788.4; NP_110415.1.
DR UCSC; uc003ylx.3; human. [Q9H295-1]
DR CTD; 81501; -.
DR DisGeNET; 81501; -.
DR GeneCards; DCSTAMP; -.
DR HGNC; HGNC:18549; DCSTAMP.
DR HPA; ENSG00000164935; Group enriched (brain, epididymis, lung).
DR MIM; 605933; gene.
DR neXtProt; NX_Q9H295; -.
DR OpenTargets; ENSG00000164935; -.
DR PharmGKB; PA134938623; -.
DR VEuPathDB; HostDB:ENSG00000164935; -.
DR eggNOG; ENOG502QWDQ; Eukaryota.
DR GeneTree; ENSGT00940000153269; -.
DR HOGENOM; CLU_046145_0_0_1; -.
DR InParanoid; Q9H295; -.
DR OMA; CFKHLRC; -.
DR OrthoDB; 821078at2759; -.
DR PhylomeDB; Q9H295; -.
DR TreeFam; TF318254; -.
DR PathwayCommons; Q9H295; -.
DR Reactome; R-HSA-8874211; CREB3 factors activate genes.
DR SignaLink; Q9H295; -.
DR BioGRID-ORCS; 81501; 6 hits in 1063 CRISPR screens.
DR GenomeRNAi; 81501; -.
DR Pharos; Q9H295; Tbio.
DR PRO; PR:Q9H295; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H295; protein.
DR Bgee; ENSG00000164935; Expressed in stromal cell of endometrium and 103 other tissues.
DR Genevisible; Q9H295; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:UniProtKB.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISS:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0072675; P:osteoclast fusion; ISS:UniProtKB.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
DR GO; GO:0034241; P:positive regulation of macrophage fusion; ISS:UniProtKB.
DR GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:UniProtKB.
DR InterPro; IPR012858; DC_STAMP-like.
DR Pfam; PF07782; DC_STAMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Differentiation;
KW Endoplasmic reticulum; Endosome; Immunity; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Dendritic cell-specific transmembrane protein"
FT /id="PRO_0000072584"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11169400"
FT VAR_SEQ 277..283
FT /note="YVIIPTF -> FISGFQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044787"
FT VAR_SEQ 284..470
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044788"
FT VARIANT 349
FT /note="D -> G (in dbSNP:rs3802204)"
FT /id="VAR_051438"
FT CONFLICT 200
FT /note="M -> R (in Ref. 4; AAI71732)"
FT /evidence="ECO:0000305"
SQ 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
