IGSF2_MOUSE
ID IGSF2_MOUSE Reviewed; 1033 AA.
AC A8E0Y8; A8E0Y9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Immunoglobulin superfamily member 2;
DE Short=IgSF2;
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=Igsf2;
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 [MRNA].
RC STRAIN=NOD.B6, and NOD/MrkTac;
RX PubMed=12765969; DOI=10.2337/diabetes.52.6.1551;
RA Penha-Goncalves C., Moule C., Smink L.J., Howson J., Gregory S., Rogers J.,
RA Lyons P.A., Suttie J.J., Lord C.J., Peterson L.B., Todd J.A., Wicker L.S.;
RT "Identification of a structurally distinct CD101 molecule encoded in the
RT 950-kb Idd10 region of NOD mice.";
RL Diabetes 52:1551-1556(2003).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AM849328; CAO94506.1; -; mRNA.
DR EMBL; AM849329; CAO94507.1; -; mRNA.
DR CCDS; CCDS51020.1; -.
DR RefSeq; NP_001161378.1; NM_001167906.1.
DR AlphaFoldDB; A8E0Y8; -.
DR STRING; 10090.ENSMUSP00000116643; -.
DR GlyGen; A8E0Y8; 2 sites.
DR iPTMnet; A8E0Y8; -.
DR PhosphoSitePlus; A8E0Y8; -.
DR MaxQB; A8E0Y8; -.
DR PaxDb; A8E0Y8; -.
DR PRIDE; A8E0Y8; -.
DR ProteomicsDB; 267302; -.
DR Antibodypedia; 20186; 372 antibodies from 33 providers.
DR Ensembl; ENSMUST00000147399; ENSMUSP00000116643; ENSMUSG00000086564.
DR GeneID; 630146; -.
DR KEGG; mmu:630146; -.
DR UCSC; uc012cuu.1; mouse.
DR CTD; 9398; -.
DR MGI; MGI:2685862; Cd101.
DR VEuPathDB; HostDB:ENSMUSG00000086564; -.
DR eggNOG; ENOG502QRRB; Eukaryota.
DR GeneTree; ENSGT00940000161722; -.
DR HOGENOM; CLU_005187_0_0_1; -.
DR InParanoid; A8E0Y8; -.
DR OMA; SKWVNQA; -.
DR OrthoDB; 180654at2759; -.
DR PhylomeDB; A8E0Y8; -.
DR TreeFam; TF332702; -.
DR Reactome; R-MMU-202433; Generation of second messenger molecules.
DR BioGRID-ORCS; 630146; 1 hit in 74 CRISPR screens.
DR PRO; PR:A8E0Y8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A8E0Y8; protein.
DR Bgee; ENSMUSG00000086564; Expressed in granulocyte and 16 other tissues.
DR ExpressionAtlas; A8E0Y8; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0002763; P:positive regulation of myeloid leukocyte differentiation; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00406; IGv; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 7.
PE 2: Evidence at transcript 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..1033
FT /note="Immunoglobulin superfamily member 2"
FT /id="PRO_0000363951"
FT TOPO_DOM 21..970
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 992..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..141
FT /note="Ig-like C2-type 1"
FT DOMAIN 144..266
FT /note="Ig-like C2-type 2"
FT DOMAIN 279..388
FT /note="Ig-like C2-type 3"
FT DOMAIN 408..529
FT /note="Ig-like C2-type 4"
FT DOMAIN 539..657
FT /note="Ig-like C2-type 5"
FT DOMAIN 670..797
FT /note="Ig-like C2-type 6"
FT DOMAIN 806..941
FT /note="Ig-like C2-type 7"
FT MOTIF 253..255
FT /note="EWI motif"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
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 432..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 560..638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 695..776
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 832..925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 175
FT /note="V -> A (in strain: NOD/MrkTac)"
FT VARIANT 296
FT /note="E -> K (in strain: NOD/MrkTac)"
FT VARIANT 318
FT /note="V -> A (in strain: NOD/MrkTac)"
FT VARIANT 392
FT /note="V -> I (in strain: NOD/MrkTac)"
FT VARIANT 451
FT /note="D -> N (in strain: NOD/MrkTac)"
FT VARIANT 557
FT /note="H -> D (in strain: NOD/MrkTac)"
FT VARIANT 565
FT /note="N -> D (in strain: NOD/MrkTac)"
FT VARIANT 620
FT /note="R -> H (in strain: NOD/MrkTac)"
FT VARIANT 648
FT /note="I -> M (in strain: NOD/MrkTac)"
FT VARIANT 860
FT /note="A -> T (in strain: NOD/MrkTac)"
SQ SEQUENCE 1033 AA; 114205 MW; E0A0DD07DE0927C0 CRC64;
MACILCVASL FLSLTKFSIG QREVKIQEGP LYRAEGYPVS IRCTVSGHQG PSTQDFRWSI
YLPSAPTKEV QIISTKDAGF SYAVYAQRVQ SKEIYIERLQ GDSVLLHISK LQMKDAGEYE
CHTPNTDGKY FGSYSAKTNL TVVPDTLSAT MPSQTLSKKE GEPLELTCET TKATVQHTHL
SLTWYLMQEG GGSQATEIVS LSKDFVLTPG SSYADRFVAG DVRLDKLGAT SFRLSVGKLQ
PSDQGQVFCE ATEWIQDPDE TWTLITRKQT DQTALRIQPA ARDFTVSITA SSSPDEGKPL
ELVCLAVGRD GNPQLQGVWF LNGKEIAQTD AGGVLDLKRD YRDRASQGQL QVSKLSAQTF
SLKIFSVGPE DVGTYSCEVA EVARTQMGSW QVLQRKQSPG YRVQLREPAA RSVTVSAEQR
TVWEGETLTL LCKAAGDVSA LSVSWWLTPQ DQSTPVFVAG MGQDGTVQLG VSSPGPAHRG
NRRLEKVDWA TFRLEIASAM VTDSGTYECR VSERLQNQAK GLQSTQKISV TVKSLKSSLR
VNLMSRQPQV MLAHTFHLSC VVRANYSDLK LPFSVTWQFQ PAGSGAFHRL IRIAHNGTVE
WGDVLSQIHR KTKVSQSFFR SQLQIYDAAM EETGVYRCTV EVYDRDSICT SGPARVSATS
NLLMITVTFP ESKLSVNSSS QVQELSISSS TQIECAILSR SAGNLPLSII WYFSSVSANA
SYLKILEMDQ SSVVKYGDEF QTPRSKQKFY SEKVSQDLFL LNILSVEDSD QGHYHCAVEE
WLLSTNDTWQ KLERKTSGLT ELKLRPTGSQ VHVSKVNWTG NATEYGEAGF SCSLDGSGST
ASLYSVTWYR GRGTATATAA AVANATATIT APAGSQMLVH LQYDGLLQYG REGSRRLQHC
YRSSPTDFVL KLHRVEMEDA GIYWCRVTEW QQHGHPGKWI NQASGESQRM VLRVLRSEPT
VSSLICSSGP LLHFLIVCPF VMLLLLATSF LCLYRKARKL SQLSLSAKKE KALWVGMRKT
SLQKEAGEES GHY
