TMIG3_HUMAN
ID TMIG3_HUMAN Reviewed; 266 AA.
AC P0DMS9; A2A3P4; P33765; Q5QNY7; Q6P2N6; Q6UWU0; Q9BYZ1;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Transmembrane domain-containing protein TMIGD3 {ECO:0000305};
GN Name=TMIGD3 {ECO:0000312|HGNC:HGNC:51375}; ORFNames=UNQ1931/PRO4406;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-266 (ISOFORM 1).
RC TISSUE=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 [5]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP ALTERNATIVE SPLICING.
RX PubMed=27886186; DOI=10.1038/ncomms13561;
RA Iyer S.V., Ranjan A., Elias H.K., Parrales A., Sasaki H., Roy B.C.,
RA Umar S., Tawfik O.W., Iwakuma T.;
RT "Genome-wide RNAi screening identifies TMIGD3 isoform1 as a suppressor of
RT NF-kappaB and osteosarcoma progression.";
RL Nat. Commun. 7:13561-13561(2016).
CC -!- FUNCTION: [Isoform 1]: Plays a suppressive role in osteosarcoma
CC malignancy by inhibiting NF-kappa-B activity (PubMed:27886186).
CC {ECO:0000269|PubMed:27886186}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:27886186}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3; Synonyms=TMIGD3 i3 {ECO:0000303|PubMed:27886186}, A3AR i3
CC {ECO:0000303|PubMed:27886186};
CC IsoId=P0DMS9-1; Sequence=Displayed;
CC Name=1; Synonyms=TMIGD3 i1 {ECO:0000303|PubMed:27886186}, A3AR i1
CC {ECO:0000303|PubMed:27886186};
CC IsoId=P0DMS9-2; Sequence=VSP_057521;
CC Name=2; Synonyms=A3AR i2 {ECO:0000303|PubMed:27886186}, A3AR
CC {ECO:0000303|PubMed:27886186};
CC IsoId=P0DMS8-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in the lung and bone. Expressed at lower
CC levels in osteosarcoma tissues (at protein level).
CC {ECO:0000269|PubMed:27886186}.
CC -!- MISCELLANEOUS: [Isoform 1]: The first exon of TMIGD3 isoform 1 (i1) is
CC shared with the first exon of ADORA3 isoform 2 (A3AR i2, commonly known
CC as A3AR), resulting in a fusion protein. {ECO:0000303|PubMed:27886186}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH41707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH64411.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW56500.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AY358644; AAQ89007.1; -; mRNA.
DR EMBL; AL390195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56500.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041707; AAH41707.1; ALT_INIT; mRNA.
DR EMBL; BC064411; AAH64411.1; ALT_INIT; mRNA.
DR CCDS; CCDS41369.1; -. [P0DMS9-1]
DR CCDS; CCDS838.1; -. [P0DMS9-2]
DR RefSeq; NP_001075445.1; NM_001081976.2. [P0DMS9-1]
DR RefSeq; NP_001289609.1; NM_001302680.1.
DR RefSeq; NP_065734.5; NM_020683.6. [P0DMS9-2]
DR AlphaFoldDB; P0DMS9; -.
DR SMR; P0DMS9; -.
DR STRING; 9606.ENSP00000358730; -.
DR BindingDB; P0DMS9; -.
DR ChEMBL; CHEMBL3712907; -.
DR GlyGen; P0DMS9; 1 site.
DR iPTMnet; P0DMS9; -.
DR PhosphoSitePlus; P0DMS9; -.
DR BioMuta; TMIGD3; -.
DR DMDM; 380876892; -.
DR MassIVE; P0DMS9; -.
DR PaxDb; P0DMS9; -.
DR PeptideAtlas; P0DMS9; -.
DR PRIDE; P0DMS9; -.
DR Antibodypedia; 20120; 88 antibodies from 19 providers.
DR DNASU; 140; -.
DR DNASU; 57413; -.
DR Ensembl; ENST00000369716.9; ENSP00000358730.4; ENSG00000121933.19. [P0DMS9-2]
DR Ensembl; ENST00000369717.8; ENSP00000358731.4; ENSG00000121933.19. [P0DMS9-1]
DR GeneID; 57413; -.
DR KEGG; hsa:57413; -.
DR MANE-Select; ENST00000369716.9; ENSP00000358730.4; NM_020683.7; NP_065734.5. [P0DMS9-2]
DR CTD; 57413; -.
DR DisGeNET; 57413; -.
DR GeneCards; TMIGD3; -.
DR HGNC; HGNC:51375; TMIGD3.
DR HPA; ENSG00000121933; Tissue enriched (testis).
DR neXtProt; NX_P0DMS9; -.
DR OpenTargets; ENSG00000121933; -.
DR PharmGKB; PA24589; -.
DR VEuPathDB; HostDB:ENSG00000121933; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00930000151073; -.
DR HOGENOM; CLU_091386_0_0_1; -.
DR OMA; VHFLPVM; -.
DR OrthoDB; 890536at2759; -.
DR PathwayCommons; P0DMS9; -.
DR BioGRID-ORCS; 57413; 5 hits in 93 CRISPR screens.
DR ChiTaRS; TMIGD3; human.
DR GenomeRNAi; 57413; -.
DR Pharos; P0DMS9; Tchem.
DR PRO; PR:P0DMS9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P0DMS9; protein.
DR Bgee; ENSG00000121933; Expressed in left testis and 114 other tissues.
DR ExpressionAtlas; P0DMS9; baseline and differential.
DR Genevisible; P0DMS9; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..266
FT /note="Transmembrane domain-containing protein TMIGD3"
FT /id="PRO_0000416044"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..36
FT /note="MEGSPAGPIEQKEARWESSWEEQPDWTLGCLSPESQ -> MPNNSTALSLAN
FT VTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIV
FT VSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVR (in isoform
FT 1)"
FT /id="VSP_057521"
SQ SEQUENCE 266 AA; 30327 MW; 8D6506430DD5C208 CRC64;
MEGSPAGPIE QKEARWESSW EEQPDWTLGC LSPESQFRIP GLPGCILSFQ LKVCFLPVMW
LFILLSLALI SDAMVMDEKV KRSFVLDTAS AICNYNAHYK NHPKYWCRGY FRDYCNIIAF
SPNSTNHVAL RDTGNQLIVT MSCLTKEDTG WYWCGIQRDF ARDDMDFTEL IVTDDKGTLA
NDFWSGKDLS GNKTRSCKAP KVVRKADRSR TSILIICILI TGLGIISVIS HLTKRRRSQR
NRRVGNTLKP FSRVLTPKEM APTEQM
