TMIG1_MOUSE
ID TMIG1_MOUSE Reviewed; 261 AA.
AC Q9D7L8; Q8R202;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transmembrane and immunoglobulin domain-containing protein 1;
DE Flags: Precursor;
GN Name=Tmigd1 {ECO:0000312|MGI:MGI:1913851};
GN Synonyms=Tmigd {ECO:0000250|UniProtKB:Q6UXZ0};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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: 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; AK009118; BAB26083.1; -; mRNA.
DR EMBL; AL603842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022683; AAH22683.1; -; mRNA.
DR EMBL; BC061082; AAH61082.1; -; mRNA.
DR CCDS; CCDS25072.1; -.
DR RefSeq; NP_079931.1; NM_025655.2.
DR RefSeq; XP_006534010.2; XM_006533947.3.
DR RefSeq; XP_006534013.1; XM_006533950.2.
DR AlphaFoldDB; Q9D7L8; -.
DR SMR; Q9D7L8; -.
DR IntAct; Q9D7L8; 1.
DR MINT; Q9D7L8; -.
DR STRING; 10090.ENSMUSP00000099553; -.
DR GlyGen; Q9D7L8; 6 sites.
DR PhosphoSitePlus; Q9D7L8; -.
DR jPOST; Q9D7L8; -.
DR MaxQB; Q9D7L8; -.
DR PaxDb; Q9D7L8; -.
DR PRIDE; Q9D7L8; -.
DR ProteomicsDB; 259578; -.
DR Antibodypedia; 15126; 60 antibodies from 22 providers.
DR DNASU; 66601; -.
DR Ensembl; ENSMUST00000072633; ENSMUSP00000072427; ENSMUSG00000020839.
DR Ensembl; ENSMUST00000102495; ENSMUSP00000099553; ENSMUSG00000020839.
DR GeneID; 66601; -.
DR KEGG; mmu:66601; -.
DR UCSC; uc007kgc.1; mouse.
DR CTD; 388364; -.
DR MGI; MGI:1913851; Tmigd1.
DR VEuPathDB; HostDB:ENSMUSG00000020839; -.
DR eggNOG; ENOG502RZR9; Eukaryota.
DR GeneTree; ENSGT00510000048311; -.
DR HOGENOM; CLU_082747_0_0_1; -.
DR InParanoid; Q9D7L8; -.
DR OMA; VQNHTRD; -.
DR OrthoDB; 1099491at2759; -.
DR PhylomeDB; Q9D7L8; -.
DR TreeFam; TF336634; -.
DR BioGRID-ORCS; 66601; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9D7L8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D7L8; protein.
DR Bgee; ENSMUSG00000020839; Expressed in right colon and 99 other tissues.
DR ExpressionAtlas; Q9D7L8; baseline and differential.
DR Genevisible; Q9D7L8; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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; -; 2.
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; 2.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..261
FT /note="Transmembrane and immunoglobulin domain-containing
FT protein 1"
FT /id="PRO_0000045791"
FT TOPO_DOM 27..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..206
FT /note="Ig-like C2-type 2"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
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 53..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 142..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 261 AA; 29051 MW; 1FE1FC02D27E83CD CRC64;
MVWKITGPLQ ACQLLLVVLS LPQGRTSSVL TVNGRTENYI LDTQHGVQAS LECAVQNHTE
DEELLWYRED GIVDLKNGNK INISSVCVSP INESDNGVRF TCKLQRDQTV SVTVVLNVTF
PPLLSGNGFQ TVEENSDVSL VCNVKSNPQA QMMWYKNNSA LVLEKGRHQI HQTRESFQLS
ITKVKKSDNG TYSCIASSSL KMETMDFHLL VKDKVFVMPA EPIIAACVVV VLTMAFALFS
RRKRIMKLCG KKNDPNSETA L
