ID   IGS11_BOVIN             Reviewed;         437 AA.
AC   Q08DK1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Immunoglobulin superfamily member 11;
DE            Short=IgSF11;
DE   Flags: Precursor;
GN   Name=IGSF11;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC123707; AAI23708.1; -; mRNA.
DR   RefSeq; NP_001070389.1; NM_001076921.1.
DR   AlphaFoldDB; Q08DK1; -.
DR   SMR; Q08DK1; -.
DR   STRING; 9913.ENSBTAP00000056206; -.
DR   PaxDb; Q08DK1; -.
DR   GeneID; 540003; -.
DR   KEGG; bta:540003; -.
DR   CTD; 152404; -.
DR   eggNOG; ENOG502QV48; Eukaryota.
DR   InParanoid; Q08DK1; -.
DR   OrthoDB; 841952at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
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: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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; 2.
DR   SMART; SM00406; IGv; 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..437
FT                   /note="Immunoglobulin superfamily member 11"
FT                   /id="PRO_0000317369"
FT   TOPO_DOM        23..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..437
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          382..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         379
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   437 AA;  46530 MW;  FEF1C19A44F32123 CRC64;
     MTCRGSPLAP LLLFSLHGVA ASLEVSESPG SVQVARGQTA VLPCTFTTSA ALINLNVIWM
     VIPLSNANQP EQVILYQGGQ MFDGAPRFHG RVGFTGTMPA TNVSIFINNT QLSDTGTYQC
     LVNNLPDRGG RNIGVTGLTV LVPPSAPHCQ IQGSQDIGSD VILLCSSEEG IPRPTYLWEK
     LDNTLKLPPT ATQDQVQGTV TIRNISALSS GLYQCVASNA IGTSTCLLDL QVISPQPRSI
     GLIAGAIGTG AVIIIFCIAL ILGAFFYWRS KNKEEEEEEI PNEIREDDLP PKCSSSAKAF
     HMEISSSENN TLTSSNTYNS RYWSSNPKAH RNTESFGHFG DLRQSFSLHS GNASVPAIYA
     NGSHLAPAPH KTLVVTANRG SSLPAVSRSN GSVSRKARPP PVPSLHTHSY TVSQATLERI
     GAVPVMVPAQ SRAGSLV