TM181_HUMAN
ID TM181_HUMAN Reviewed; 612 AA.
AC Q9P2C4; Q5VTU1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transmembrane protein 181;
GN Name=TMEM181; Synonyms=GPR178, KIAA1423;
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].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP FUNCTION, AND INTERACTION WITH CYTOLETHAL DISTENDING TOXIN.
RX PubMed=19965467; DOI=10.1126/science.1178955;
RA Carette J.E., Guimaraes C.P., Varadarajan M., Park A.S., Wuethrich I.,
RA Godarova A., Kotecki M., Cochran B.H., Spooner E., Ploegh H.L.,
RA Brummelkamp T.R.;
RT "Haploid genetic screens in human cells identify host factors used by
RT pathogens.";
RL Science 326:1231-1235(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Mediates action of cytolethal distending toxins (CDT), which
CC are secreted by many pathogenic bacteria. Expression level of TMEM181
CC is rate-limiting for intoxication. {ECO:0000269|PubMed:19965467}.
CC -!- SUBUNIT: Interacts with cytolethal distending toxin.
CC {ECO:0000269|PubMed:19965467}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92661.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037844; BAA92661.1; ALT_INIT; mRNA.
DR EMBL; AL591025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_065874.1; NM_020823.1.
DR AlphaFoldDB; Q9P2C4; -.
DR SMR; Q9P2C4; -.
DR BioGRID; 121635; 30.
DR IntAct; Q9P2C4; 4.
DR MINT; Q9P2C4; -.
DR STRING; 9606.ENSP00000356057; -.
DR GlyGen; Q9P2C4; 1 site.
DR iPTMnet; Q9P2C4; -.
DR PhosphoSitePlus; Q9P2C4; -.
DR SwissPalm; Q9P2C4; -.
DR BioMuta; TMEM181; -.
DR DMDM; 108935999; -.
DR EPD; Q9P2C4; -.
DR jPOST; Q9P2C4; -.
DR MassIVE; Q9P2C4; -.
DR MaxQB; Q9P2C4; -.
DR PaxDb; Q9P2C4; -.
DR PeptideAtlas; Q9P2C4; -.
DR PRIDE; Q9P2C4; -.
DR ProteomicsDB; 83769; -.
DR Antibodypedia; 50333; 58 antibodies from 17 providers.
DR DNASU; 57583; -.
DR Ensembl; ENST00000367090.4; ENSP00000356057.4; ENSG00000146433.10.
DR GeneID; 57583; -.
DR KEGG; hsa:57583; -.
DR UCSC; uc003qrm.5; human.
DR CTD; 57583; -.
DR DisGeNET; 57583; -.
DR GeneCards; TMEM181; -.
DR HGNC; HGNC:20958; TMEM181.
DR HPA; ENSG00000146433; Low tissue specificity.
DR MIM; 613209; gene.
DR neXtProt; NX_Q9P2C4; -.
DR PharmGKB; PA162406036; -.
DR VEuPathDB; HostDB:ENSG00000146433; -.
DR eggNOG; ENOG502QPXU; Eukaryota.
DR HOGENOM; CLU_040299_0_0_1; -.
DR InParanoid; Q9P2C4; -.
DR OrthoDB; 673869at2759; -.
DR PhylomeDB; Q9P2C4; -.
DR TreeFam; TF324083; -.
DR PathwayCommons; Q9P2C4; -.
DR SignaLink; Q9P2C4; -.
DR BioGRID-ORCS; 57583; 10 hits in 1084 CRISPR screens.
DR ChiTaRS; TMEM181; human.
DR GenomeRNAi; 57583; -.
DR Pharos; Q9P2C4; Tbio.
DR PRO; PR:Q9P2C4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P2C4; protein.
DR Bgee; ENSG00000146433; Expressed in pylorus and 192 other tissues.
DR Genevisible; Q9P2C4; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
DR InterPro; IPR040416; TMEM181.
DR PANTHER; PTHR31918; PTHR31918; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..612
FT /note="Transmembrane protein 181"
FT /id="PRO_0000239661"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
SQ SEQUENCE 612 AA; 69325 MW; 2104278D3F64F1CF CRC64;
MGAAPSPTQA SSRGGGPGPP APTRAVSSSS RARGGALSAL GPSPARPLTT SPAPAPPPRS
RPARQQPDPQ CWEKRGGAGG DTKGGAAGPG PGRLRGMDAE YPAFEPPLCS ELKHLCRRLR
EAYRELKEDL TPFKDDRYYR LAPMRLYTLS KRHFVLVFVV FFICFGLTIF VGIRGPKVIQ
TSAANFSLNN SKKLKPIQIL SNPLSTYNQQ LWLTCVVELD QSKETSIKTS FPMTVKVDGV
AQDGTTMYIH NKVHNRTRTL TCAGKCAEII VAHLGYLNYT QYTVIVGFEH LKLPIKGMNF
TWKTYNPAFS RLEIWFRFFF VVLTFIVTCL FAHSLRKFSM RDWGIEQKWM SVLLPLLLLY
NDPFFPLSFL VNSWLPGMLD DLFQSMFLCA LLLFWLCVYH GIRVQGERKC LTFYLPKFFI
VGLLWLASVT LGIWQTVNEL HDPMYQYRVD TGNFQGMKVF FMVVAAVYIL YLLFLIVRAC
SELRHMPYVD LRLKFLTALT FVVLVISIAI LYLRFGAQVL QDNFVAELST HYQNSAEFLS
FYGLLNFYLY TLAFVYSPSK NALYESQLKD NPAFSMLNDS DDDVIYGSDY EEMPLQNGQA
IRAKYKEESD SD
