ID   IGS11_RAT               Reviewed;         428 AA.
AC   Q5U2P2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Immunoglobulin superfamily member 11;
DE            Short=IgSF11;
DE   Flags: Precursor;
GN   Name=Igsf11;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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).
CC   -!- FUNCTION: Functions as a cell adhesion molecule through homophilic
CC       interaction. Stimulates cell growth (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
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DR   EMBL; BC085929; AAH85929.1; -; mRNA.
DR   RefSeq; NP_001013138.1; NM_001013120.1.
DR   AlphaFoldDB; Q5U2P2; -.
DR   SMR; Q5U2P2; -.
DR   STRING; 10116.ENSRNOP00000059779; -.
DR   GlyGen; Q5U2P2; 1 site.
DR   iPTMnet; Q5U2P2; -.
DR   PhosphoSitePlus; Q5U2P2; -.
DR   PaxDb; Q5U2P2; -.
DR   Ensembl; ENSRNOT00000066997; ENSRNOP00000059779; ENSRNOG00000001525.
DR   GeneID; 303926; -.
DR   KEGG; rno:303926; -.
DR   UCSC; RGD:1308758; rat.
DR   CTD; 152404; -.
DR   RGD; 1308758; Igsf11.
DR   eggNOG; ENOG502QV48; Eukaryota.
DR   GeneTree; ENSGT00940000156392; -.
DR   HOGENOM; CLU_040549_3_0_1; -.
DR   InParanoid; Q5U2P2; -.
DR   OMA; WHNPKPS; -.
DR   OrthoDB; 841952at2759; -.
DR   PhylomeDB; Q5U2P2; -.
DR   TreeFam; TF330875; -.
DR   PRO; PR:Q5U2P2; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001525; Expressed in ovary and 16 other tissues.
DR   Genevisible; Q5U2P2; RN.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0060076; C:excitatory synapse; IMP:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:UniProtKB.
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; IMP:UniProtKB.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; IMP:UniProtKB.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
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   2: Evidence at transcript 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_0000317372"
FT   TOPO_DOM        23..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..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   MOD_RES         375
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C673"
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"
SQ   SEQUENCE   428 AA;  46021 MW;  C628CEE36D03A1F2 CRC64;
     MTRRRSALAS WLLLSLLGVA ASLEVSESPG SVQVARGQTA VLPCAFSTSA ALLNLNVIWM
     VIPLSNANQP EQVILYQGGQ MFDGALRFHG RVGFTGTMPA TNVSIFINNT QLSDTGTYQC
     LVNNLPDRGG RNIGVTGLTV LVPPSAPNCQ IQGSQDIGSD VILLCSSEEG IPRPTYLWEK
     LDNTLKLPPT ATQDQVQGTV TIRNISALSS GLYQCVASNA IGTSTCLLDL QVISPQPRSV
     GVIAGAVGTG AVLIVICLAL TSGAFFYWRS KNKEEEEEEI PNEIREDDLP PKCSSAKAFH
     TEISSSENNT LTSSNTYNSR YWNNNPKPHK NTESFNHFSD LRQSFSGNAV IPSIYANGNH
     LVLGPHKTLV VTANRGSSPQ VMPRNNGSVS RKPWSQHTHS YTVSQMTLER IGAVPVMVPA
     QSRAGSLV