ID   TMIG1_BOVIN             Reviewed;         261 AA.
AC   Q3T113;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Transmembrane and immunoglobulin domain-containing protein 1 {ECO:0000250|UniProtKB:Q6UXZ0};
DE   Flags: Precursor;
GN   Name=TMIGD1 {ECO:0000250|UniProtKB:Q6UXZ0};
GN   Synonyms=TMIGD {ECO:0000250|UniProtKB:Q6UXZ0};
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May control cell-cell adhesion, cell migration and
CC       proliferation, cell morphology, and protects renal epithelial cells
CC       from oxidative cell injury to promote cell survival.
CC       {ECO:0000250|UniProtKB:Q6UXZ0}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6UXZ0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6UXZ0};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6UXZ0}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q6UXZ0}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6UXZ0}.
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DR   EMBL; BC102165; AAI02166.1; -; mRNA.
DR   RefSeq; NP_001030208.1; NM_001035036.2.
DR   AlphaFoldDB; Q3T113; -.
DR   SMR; Q3T113; -.
DR   STRING; 9913.ENSBTAP00000003375; -.
DR   PaxDb; Q3T113; -.
DR   GeneID; 506345; -.
DR   KEGG; bta:506345; -.
DR   CTD; 388364; -.
DR   eggNOG; ENOG502RZZ3; Eukaryota.
DR   InParanoid; Q3T113; -.
DR   OrthoDB; 1099491at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0090559; P:regulation of membrane permeability; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
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; IPR003598; Ig_sub2.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..261
FT                   /note="Transmembrane and immunoglobulin domain-containing
FT                   protein 1"
FT                   /id="PRO_0000045789"
FT   TOPO_DOM        28..219
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..114
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          122..208
FT                   /note="Ig-like C2-type 2"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        143..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   261 AA;  29229 MW;  5ADB4E1D5CF9073F CRC64;
     MAQKTSGLIQ RCRFLLLMIL FLPHVMTSSV LSVNGKTENY ILDTEPGLQE SLKCAVQNHI
     RDEELLWYRE DGRVDLKSGN KINSSSVCVS GISEDDNGIT FTCKLQRNQS VSISVVLNVT
     FPPLLSGNDF QTAEEGSDVK LVCNVKSNPQ AQMMWYKNNG ILNLENHHQI QQTSEYFQLS
     ITKVKKSDNG TYSCIANSLI ETKTKDFHLI VKDKGSTVPI EPIIAACVVV FLTLVFGVIA
     RRKRIMKLCR KDQGPQCRTA L