IGSF2_HUMAN
ID IGSF2_HUMAN Reviewed; 1021 AA.
AC Q93033; Q15856;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Immunoglobulin superfamily member 2;
DE Short=IgSF2;
DE AltName: Full=Cell surface glycoprotein V7;
DE AltName: Full=Glu-Trp-Ile EWI motif-containing protein 101;
DE Short=EWI-101;
DE AltName: CD_antigen=CD101;
DE Flags: Precursor;
GN Name=CD101; Synonyms=EWI101, IGSF2, V7;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-415.
RX PubMed=7722300;
RA Ruegg C.L., Rivas A., Madani N.D., Zeitung J., Laus R., Engleman E.G.;
RT "V7, a novel leukocyte surface protein that participates in T cell
RT activation. II. Molecular cloning and characterization of the V7 gene.";
RL J. Immunol. 154:4434-4443(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP FUNCTION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=7722299;
RA Rivas A., Ruegg C.L., Zeitung J., Laus R., Warnke R., Benike C.,
RA Engleman E.G.;
RT "V7, a novel leukocyte surface protein that participates in T cell
RT activation. I. Tissue distribution and functional studies.";
RL J. Immunol. 154:4423-4433(1995).
RN [4]
RP FUNCTION.
RX PubMed=9233604;
RA Soares L.R.B., Rivas A., Tsavaler L., Engleman E.G.;
RT "Ligation of the V7 molecule on T cells blocks anergy induction through a
RT CD28-independent mechanism.";
RL J. Immunol. 159:1115-1124(1997).
RN [5]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=9389317; DOI=10.1111/j.1399-0039.1997.tb02898.x;
RA Bagot M., Martinel I., Charue D., Weill F., Boulland M.-L., Wechsler J.,
RA Freeman G.J., Bensussan A., Boumsell L.;
RT "CD101 is expressed by skin dendritic cells. Role in T-lymphocyte
RT activation.";
RL Tissue Antigens 50:439-448(1997).
RN [6]
RP FUNCTION.
RX PubMed=9647226;
RA Soares L.R.B., Tsavaler L., Rivas A., Engleman E.G.;
RT "V7 (CD101) ligation inhibits TCR/CD3-induced IL-2 production by blocking
RT Ca2+ flux and nuclear factor of activated T cell nuclear translocation.";
RL J. Immunol. 161:209-217(1998).
RN [7]
RP FUNCTION.
RX PubMed=11093127;
RX DOI=10.1002/1521-4141(200011)30:11<3132::aid-immu3132>3.0.co;2-e;
RA Bouloc A., Bagot M., Delaire S., Bensussan A., Boumsell L.;
RT "Triggering CD101 molecule on human cutaneous dendritic cells inhibits T
RT cell proliferation via IL-10 production.";
RL Eur. J. Immunol. 30:3132-3139(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10692025; DOI=10.1046/j.1365-2559.2000.00827.x;
RA Bouloc A., Boulland M.-L., Geissmann F., Fraitag S., Andry P., Teillac D.,
RA Bensussan A., Revuz J., Boumsell L., Wechsler J., Bagot M.;
RT "CD101 expression by Langerhans cell histiocytosis cells.";
RL Histopathology 36:229-232(2000).
RN [9]
RP DOMAIN EWI MOTIF.
RX PubMed=11504738; DOI=10.1074/jbc.m107338200;
RA Stipp C.S., Kolesnikova T.V., Hemler M.E.;
RT "EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein
RT subfamily.";
RL J. Biol. Chem. 276:40545-40554(2001).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15737213; DOI=10.1111/j.0022-202x.2005.23617.x;
RA Meyer N., Petrella T., Poszepczynska-Guigne E., Boumsell L., Wechsler J.,
RA Bensussan A., Bagot M.;
RT "CD4+ CD56+ blastic tumor cells express CD101 molecules.";
RL J. Invest. Dermatol. 124:668-669(2005).
CC -!- FUNCTION: Plays a role as inhibitor of T-cells proliferation induced by
CC CD3. Inhibits expression of IL2RA on activated T-cells and secretion of
CC IL2. Inhibits tyrosine kinases that are required for IL2 production and
CC cellular proliferation. Inhibits phospholipase C-gamma-1/PLCG1
CC phosphorylation and subsequent CD3-induced changes in intracellular
CC free calcium. Prevents nuclear translocation of nuclear factor of
CC activated T-cell to the nucleus. Plays a role in the inhibition of T-
CC cell proliferation via IL10 secretion by cutaneous dendritic cells. May
CC be a marker of CD4(+) CD56(+) leukemic tumor cells.
CC {ECO:0000269|PubMed:11093127, ECO:0000269|PubMed:15737213,
CC ECO:0000269|PubMed:7722299, ECO:0000269|PubMed:9233604,
CC ECO:0000269|PubMed:9389317, ECO:0000269|PubMed:9647226}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, thymus and small intestine.
CC Detected in cutaneous dendritic cells, activated T-cells, monocytes and
CC granulocytes as well as with epithelial cells with dendritic
CC morphology. Expressed in some leukemic cells, the CD4(+) CD56(+)
CC blastic tumor cells, as well as in Langerhans cells from LCH
CC (Langerhans cell histiocytosis) patients. {ECO:0000269|PubMed:10692025,
CC ECO:0000269|PubMed:15737213, ECO:0000269|PubMed:7722299,
CC ECO:0000269|PubMed:7722300, ECO:0000269|PubMed:9389317}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7722299}.
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DR EMBL; Z33642; CAA83923.1; -; mRNA.
DR EMBL; AL445231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS891.1; -.
DR PIR; I39207; I39207.
DR RefSeq; NP_001243035.1; NM_001256106.2.
DR RefSeq; NP_001243038.1; NM_001256109.2.
DR RefSeq; NP_004249.2; NM_004258.5.
DR AlphaFoldDB; Q93033; -.
DR BioGRID; 114795; 6.
DR IntAct; Q93033; 4.
DR STRING; 9606.ENSP00000358482; -.
DR GlyGen; Q93033; 4 sites.
DR iPTMnet; Q93033; -.
DR PhosphoSitePlus; Q93033; -.
DR BioMuta; CD101; -.
DR DMDM; 223590070; -.
DR EPD; Q93033; -.
DR jPOST; Q93033; -.
DR MassIVE; Q93033; -.
DR PaxDb; Q93033; -.
DR PeptideAtlas; Q93033; -.
DR PRIDE; Q93033; -.
DR ProteomicsDB; 75672; -.
DR Antibodypedia; 20186; 372 antibodies from 33 providers.
DR DNASU; 9398; -.
DR Ensembl; ENST00000256652.8; ENSP00000256652.4; ENSG00000134256.13.
DR Ensembl; ENST00000369470.1; ENSP00000358482.1; ENSG00000134256.13.
DR Ensembl; ENST00000682167.1; ENSP00000508039.1; ENSG00000134256.13.
DR GeneID; 9398; -.
DR KEGG; hsa:9398; -.
DR MANE-Select; ENST00000682167.1; ENSP00000508039.1; NM_001256106.3; NP_001243035.1.
DR UCSC; uc010oxc.3; human.
DR CTD; 9398; -.
DR DisGeNET; 9398; -.
DR GeneCards; CD101; -.
DR HGNC; HGNC:5949; CD101.
DR HPA; ENSG00000134256; Tissue enhanced (bone marrow, intestine, lung).
DR MIM; 604516; gene.
DR neXtProt; NX_Q93033; -.
DR OpenTargets; ENSG00000134256; -.
DR PharmGKB; PA29762; -.
DR VEuPathDB; HostDB:ENSG00000134256; -.
DR eggNOG; ENOG502QRRB; Eukaryota.
DR GeneTree; ENSGT00940000161722; -.
DR HOGENOM; CLU_005187_0_0_1; -.
DR InParanoid; Q93033; -.
DR OMA; SKWVNQA; -.
DR OrthoDB; 180654at2759; -.
DR PhylomeDB; Q93033; -.
DR TreeFam; TF332702; -.
DR PathwayCommons; Q93033; -.
DR Reactome; R-HSA-202433; Generation of second messenger molecules.
DR SignaLink; Q93033; -.
DR BioGRID-ORCS; 9398; 19 hits in 1067 CRISPR screens.
DR ChiTaRS; CD101; human.
DR GeneWiki; IGSF2; -.
DR GenomeRNAi; 9398; -.
DR Pharos; Q93033; Tbio.
DR PRO; PR:Q93033; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q93033; protein.
DR Bgee; ENSG00000134256; Expressed in monocyte and 94 other tissues.
DR Genevisible; Q93033; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0002763; P:positive regulation of myeloid leukocyte differentiation; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 3.
DR SMART; SM00409; IG; 7.
DR SMART; SM00406; IGv; 4.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 7.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1021
FT /note="Immunoglobulin superfamily member 2"
FT /id="PRO_0000253539"
FT TOPO_DOM 21..954
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..1021
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..139
FT /note="Ig-like C2-type 1"
FT DOMAIN 144..265
FT /note="Ig-like C2-type 2"
FT DOMAIN 279..389
FT /note="Ig-like C2-type 3"
FT DOMAIN 408..525
FT /note="Ig-like C2-type 4"
FT DOMAIN 541..651
FT /note="Ig-like C2-type 5"
FT DOMAIN 656..794
FT /note="Ig-like C2-type 6"
FT DOMAIN 808..925
FT /note="Ig-like C2-type 7"
FT MOTIF 253..255
FT /note="EWI motif"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 168..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 304..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 434..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 562..640
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 697..778
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 834..909
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 157
FT /note="G -> S (in dbSNP:rs34999087)"
FT /id="VAR_054434"
FT VARIANT 225
FT /note="N -> S (in dbSNP:rs3754112)"
FT /id="VAR_028371"
FT VARIANT 415
FT /note="M -> V (in dbSNP:rs2249265)"
FT /evidence="ECO:0000269|PubMed:7722300"
FT /id="VAR_028372"
FT VARIANT 518
FT /note="R -> Q (in dbSNP:rs17235766)"
FT /id="VAR_028373"
FT VARIANT 525
FT /note="S -> R (in dbSNP:rs17235773)"
FT /id="VAR_028374"
FT VARIANT 631
FT /note="T -> S (in dbSNP:rs34510762)"
FT /id="VAR_054435"
FT VARIANT 933
FT /note="R -> Q (in dbSNP:rs12093834)"
FT /id="VAR_054436"
FT VARIANT 955
FT /note="L -> F (in dbSNP:rs34223095)"
FT /id="VAR_054437"
FT VARIANT 965
FT /note="V -> I (in dbSNP:rs12097758)"
FT /id="VAR_028375"
FT VARIANT 988
FT /note="R -> C (in dbSNP:rs12067543)"
FT /id="VAR_028376"
FT VARIANT 992
FT /note="R -> W (in dbSNP:rs34248572)"
FT /id="VAR_054438"
FT CONFLICT 91
FT /note="S -> G (in Ref. 1; CAA83923)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="K -> N (in Ref. 1; CAA83923)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> R (in Ref. 1; CAA83923)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="V -> L (in Ref. 1; CAA83923)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="V -> G (in Ref. 1; CAA83923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1021 AA; 115109 MW; 12A07C648D21EB91 CRC64;
MAGISYVASF FLLLTKLSIG QREVTVQKGP LFRAEGYPVS IGCNVTGHQG PSEQHFQWSV
YLPTNPTQEV QIISTKDAAF SYAVYTQRVR SGDVYVERVQ GNSVLLHISK LQMKDAGEYE
CHTPNTDEKY YGSYSAKTNL IVIPDTLSAT MSSQTLGKEE GEPLALTCEA SKATAQHTHL
SVTWYLTQDG GGSQATEIIS LSKDFILVPG PLYTERFAAS DVQLNKLGPT TFRLSIERLQ
SSDQGQLFCE ATEWIQDPDE TWMFITKKQT DQTTLRIQPA VKDFQVNITA DSLFAEGKPL
ELVCLVVSSG RDPQLQGIWF FNGTEIAHID AGGVLGLKND YKERASQGEL QVSKLGPKAF
SLKIFSLGPE DEGAYRCVVA EVMKTRTGSW QVLQRKQSPD SHVHLRKPAA RSVVMSTKNK
QQVVWEGETL AFLCKAGGAE SPLSVSWWHI PRDQTQPEFV AGMGQDGIVQ LGASYGVPSY
HGNTRLEKMD WATFQLEITF TAITDSGTYE CRVSEKSRNQ ARDLSWTQKI SVTVKSLESS
LQVSLMSRQP QVMLTNTFDL SCVVRAGYSD LKVPLTVTWQ FQPASSHIFH QLIRITHNGT
IEWGNFLSRF QKKTKVSQSL FRSQLLVHDA TEEETGVYQC EVEVYDRNSL YNNRPPRASA
ISHPLRIAVT LPESKLKVNS RSQVQELSIN SNTDIECSIL SRSNGNLQLA IIWYFSPVST
NASWLKILEM DQTNVIKTGD EFHTPQRKQK FHTEKVSQDL FQLHILNVED SDRGKYHCAV
EEWLLSTNGT WHKLGEKKSG LTELKLKPTG SKVRVSKVYW TENVTEHREV AIRCSLESVG
SSATLYSVMW YWNRENSGSK LLVHLQHDGL LEYGEEGLRR HLHCYRSSST DFVLKLHQVE
MEDAGMYWCR VAEWQLHGHP SKWINQASDE SQRMVLTVLP SEPTLPSRIC SSAPLLYFLF
ICPFVLLLLL LISLLCLYWK ARKLSTLRSN TRKEKALWVD LKEAGGVTTN RREDEEEDEG
N
