IGS11_MOUSE
ID IGS11_MOUSE Reviewed; 428 AA.
AC P0C673;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Immunoglobulin superfamily member 11;
DE Short=IgSF11;
DE AltName: Full=Brain and testis-specific immunoglobulin superfamily protein;
DE Short=Bt-IGSF;
DE Flags: Precursor;
GN Name=Igsf11;
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], GLYCOSYLATION, TOPOLOGY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=12207903; DOI=10.1016/s0006-291x(02)02025-9;
RA Suzu S., Hayashi Y., Harumi T., Nomaguchi K., Yamada M., Hayasawa H.,
RA Motoyoshi K.;
RT "Molecular cloning of a novel immunoglobulin superfamily gene
RT preferentially expressed by brain and testis.";
RL Biochem. Biophys. Res. Commun. 296:1215-1221(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-375, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Functions as a cell adhesion molecule through homophilic
CC interaction. Stimulates cell growth (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and detected in kidney
CC and adrenal gland. In brain, expressed in commissure fibers of the
CC corpus callosum and pyramidal cell layers of the dentate gyrus and
CC hippocampus where it is probably expressed by both neurons and glial
CC cells. {ECO:0000269|PubMed:12207903}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12207903}.
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DR EMBL; AB079880; BAC07547.1; -; mRNA.
DR EMBL; BC057555; AAH57555.1; -; mRNA.
DR CCDS; CCDS28175.1; -.
DR RefSeq; NP_733548.2; NM_170599.2.
DR AlphaFoldDB; P0C673; -.
DR SMR; P0C673; -.
DR STRING; 10090.ENSMUSP00000023478; -.
DR GlyGen; P0C673; 1 site.
DR iPTMnet; P0C673; -.
DR PhosphoSitePlus; P0C673; -.
DR MaxQB; P0C673; -.
DR PaxDb; P0C673; -.
DR PeptideAtlas; P0C673; -.
DR PRIDE; P0C673; -.
DR ProteomicsDB; 269467; -.
DR Antibodypedia; 46572; 220 antibodies from 26 providers.
DR Ensembl; ENSMUST00000023478; ENSMUSP00000023478; ENSMUSG00000022790.
DR GeneID; 207683; -.
DR KEGG; mmu:207683; -.
DR UCSC; uc007zfp.1; mouse.
DR CTD; 152404; -.
DR MGI; MGI:2388477; Igsf11.
DR VEuPathDB; HostDB:ENSMUSG00000022790; -.
DR eggNOG; ENOG502QV48; Eukaryota.
DR GeneTree; ENSGT00940000156392; -.
DR InParanoid; P0C673; -.
DR OMA; WHNPKPS; -.
DR OrthoDB; 841952at2759; -.
DR PhylomeDB; P0C673; -.
DR TreeFam; TF330875; -.
DR BioGRID-ORCS; 207683; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Igsf11; mouse.
DR PRO; PR:P0C673; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P0C673; protein.
DR Bgee; ENSMUSG00000022790; Expressed in gastrula and 112 other tissues.
DR ExpressionAtlas; P0C673; baseline and differential.
DR Genevisible; P0C673; MM.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0045185; P:maintenance of protein location; ISO:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR042758; IGSF11.
DR PANTHER; PTHR44699; PTHR44699; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Growth regulation; Immunoglobulin domain; Membrane; Methylation; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..428
FT /note="Immunoglobulin superfamily member 11"
FT /id="PRO_0000317371"
FT TOPO_DOM 23..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..136
FT /note="Ig-like V-type"
FT DOMAIN 144..234
FT /note="Ig-like C2-type"
FT REGION 376..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 375
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 349
FT /note="A -> P (in Ref. 1; BAC07547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 46067 MW; 64A45D8C6A0258CE CRC64;
MTRRRSAPAS WLLVSLLGVA TSLEVSESPG SVQVARGQTA VLPCAFSTSA ALLNLNVIWM
VIPLSNANQP EQVILYQGGQ MFDGALRFHG RVGFTGTMPA TNVSIFINNT QLSDTGTYQC
LVNNLPDRGG RNIGVTGLTV LVPPSAPQCQ IQGSQDLGSD VILLCSSEEG IPRPTYLWEK
LDNTLKLPPT ATQDQVQGTV TIRNISALSS GLYQCVASNA IGTSTCLLDL QVISPQPRSV
GVIAGAVGTG AVLIVICLAL ISGAFFYWRS KNKEEEEEEI PNEIREDDLP PKCSSAKAFH
TEISSSENNT LTSSNTYNSR YWNNNPKPHR NTESFNHFSD LRQSFSGNAV IPSIYANGNH
LVLGPHKTLV VTANRGSSPQ VLPRNNGSVS RKPWPQHTHS YTVSQMTLER IGAVPVMVPA
QSRAGSLV
