TMM18_HUMAN
ID TMM18_HUMAN Reviewed; 140 AA.
AC Q96B42; D6W4X9; Q8N5H2; Q9NTH3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane protein 18;
GN Name=TMEM18;
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 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, and Lung;
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, AND SUBCELLULAR LOCATION.
RX PubMed=18559506; DOI=10.1158/0008-5472.can-07-5291;
RA Jurvansuu J., Zhao Y., Leung D.S., Boulaire J., Yu Y.H., Ahmed S., Wang S.;
RT "Transmembrane protein 18 enhances the tropism of neural stem cells for
RT glioma cells.";
RL Cancer Res. 68:4614-4622(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND DNA-BINDING.
RX PubMed=21980424; DOI=10.1371/journal.pone.0025317;
RA Jurvansuu J.M., Goldman A.;
RT "Obesity risk gene TMEM18 encodes a sequence-specific DNA-binding
RT protein.";
RL PLoS ONE 6:E25317-E25317(2011).
CC -!- FUNCTION: Transcription repressor. Sequence-specific ssDNA and dsDNA
CC binding protein, with preference for GCT end CTG repeats. Cell
CC migration modulator which enhances the glioma-specific migration
CC ability of neural stem cells (NSC) and neural precursor cells (NPC).
CC {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}.
CC -!- SUBUNIT: Forms homooligomers, independently of the DNA-binding domain.
CC {ECO:0000269|PubMed:21980424}.
CC -!- INTERACTION:
CC Q96B42-2; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-17196383, EBI-7545592;
CC Q96B42-2; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-17196383, EBI-10192441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18559506,
CC ECO:0000269|PubMed:21980424}. Nucleus membrane
CC {ECO:0000269|PubMed:18559506, ECO:0000269|PubMed:21980424}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96B42-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96B42-2; Sequence=VSP_024469;
CC -!- SIMILARITY: Belongs to the TMEM18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB70668.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL137269; CAB70668.1; ALT_INIT; mRNA.
DR EMBL; AC092159; AAY14770.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01100.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01101.1; -; Genomic_DNA.
DR EMBL; BC016010; AAH16010.2; -; mRNA.
DR EMBL; BC032379; AAH32379.1; -; mRNA.
DR CCDS; CCDS33141.1; -. [Q96B42-1]
DR CCDS; CCDS86815.1; -. [Q96B42-2]
DR PIR; T46342; T46342.
DR RefSeq; NP_690047.2; NM_152834.2. [Q96B42-1]
DR AlphaFoldDB; Q96B42; -.
DR BioGRID; 126206; 13.
DR IntAct; Q96B42; 2.
DR STRING; 9606.ENSP00000281017; -.
DR TCDB; 9.B.228.1.1; the tmem18 (tmem18) family.
DR iPTMnet; Q96B42; -.
DR PhosphoSitePlus; Q96B42; -.
DR SwissPalm; Q96B42; -.
DR BioMuta; TMEM18; -.
DR DMDM; 121944491; -.
DR MassIVE; Q96B42; -.
DR PaxDb; Q96B42; -.
DR PeptideAtlas; Q96B42; -.
DR PRIDE; Q96B42; -.
DR ProteomicsDB; 76042; -. [Q96B42-1]
DR ProteomicsDB; 76043; -. [Q96B42-2]
DR Antibodypedia; 26187; 88 antibodies from 23 providers.
DR DNASU; 129787; -.
DR Ensembl; ENST00000281017.8; ENSP00000281017.3; ENSG00000151353.15. [Q96B42-1]
DR Ensembl; ENST00000355654.6; ENSP00000347874.2; ENSG00000151353.15. [Q96B42-2]
DR GeneID; 129787; -.
DR KEGG; hsa:129787; -.
DR MANE-Select; ENST00000281017.8; ENSP00000281017.3; NM_152834.4; NP_690047.2.
DR UCSC; uc002qwl.4; human. [Q96B42-1]
DR CTD; 129787; -.
DR DisGeNET; 129787; -.
DR GeneCards; TMEM18; -.
DR HGNC; HGNC:25257; TMEM18.
DR HPA; ENSG00000151353; Low tissue specificity.
DR MIM; 613220; gene.
DR neXtProt; NX_Q96B42; -.
DR OpenTargets; ENSG00000151353; -.
DR PharmGKB; PA134873089; -.
DR VEuPathDB; HostDB:ENSG00000151353; -.
DR eggNOG; ENOG502S2NZ; Eukaryota.
DR GeneTree; ENSGT00390000015191; -.
DR HOGENOM; CLU_101161_1_1_1; -.
DR InParanoid; Q96B42; -.
DR OMA; IVVMWVR; -.
DR OrthoDB; 1575793at2759; -.
DR PhylomeDB; Q96B42; -.
DR TreeFam; TF324883; -.
DR PathwayCommons; Q96B42; -.
DR SignaLink; Q96B42; -.
DR BioGRID-ORCS; 129787; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; TMEM18; human.
DR GeneWiki; TMEM18; -.
DR GenomeRNAi; 129787; -.
DR Pharos; Q96B42; Tbio.
DR PRO; PR:Q96B42; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96B42; protein.
DR Bgee; ENSG00000151353; Expressed in calcaneal tendon and 186 other tissues.
DR ExpressionAtlas; Q96B42; baseline and differential.
DR Genevisible; Q96B42; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR InterPro; IPR026721; TMEM18.
DR Pfam; PF14770; TMEM18; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; DNA-binding; Membrane;
KW Nucleus; Reference proteome; Transcription; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..140
FT /note="Transmembrane protein 18"
FT /id="PRO_0000284369"
FT TOPO_DOM 1..25
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..52
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..91
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..140
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT REGION 113..140
FT /note="DNA-binding"
FT COILED 116..140
FT /evidence="ECO:0000255"
FT MOTIF 130..138
FT /note="Nuclear localization signal"
FT VAR_SEQ 2..19
FT /note="PSAFSVSSFPVSIPAVLT -> LSGYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024469"
SQ SEQUENCE 140 AA; 16265 MW; FDE25DA6B7CCC2BC CRC64;
MPSAFSVSSF PVSIPAVLTQ TDWTEPWLMG LATFHALCVL LTCLSSRSYR LQIGHFLCLV
ILVYCAEYIN EAAAMNWRLF SKYQYFDSRG MFISIVFSAP LLVNAMIIVV MWVWKTLNVM
TDLKNAQERR KEKKRRRKED
