T161A_HUMAN
ID T161A_HUMAN Reviewed; 479 AA.
AC Q9NX61; B3KUE0; G5E9M6; Q7L2Y1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Transmembrane protein 161A;
DE AltName: Full=Adaptive response to oxidative stress protein 29;
DE Short=AROS-29;
DE Flags: Precursor;
GN Name=TMEM161A; ORFNames=UNQ582/PRO1152;
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).
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Signet-ring cell carcinoma, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-85.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=16551573; DOI=10.1080/10715760600570547;
RA Montesano Gesualdi N., Chirico G., Catanese M.T., Pirozzi G., Esposito F.;
RT "AROS-29 is involved in adaptive response to oxidative stress.";
RL Free Radic. Res. 40:467-476(2006).
CC -!- FUNCTION: May play a role in protection against oxidative stress.
CC Overexpression leads to reduced levels of oxidant-induced DNA damage
CC and apoptosis. {ECO:0000269|PubMed:16551573}.
CC -!- INTERACTION:
CC Q9NX61; O15354: GPR37; NbExp=2; IntAct=EBI-6138599, EBI-15639515;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NX61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NX61-2; Sequence=VSP_046042;
CC -!- INDUCTION: Up-regulated in cells which display transient adaptation to
CC mild oxidative stress by treatment with diethylmaleate, a glutathione-
CC depleting agent. Also induced by retinoic acid.
CC {ECO:0000269|PubMed:16551573}.
CC -!- SIMILARITY: Belongs to the TMEM161 family. {ECO:0000305}.
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DR EMBL; AY358088; AAQ88455.1; -; mRNA.
DR EMBL; AK000429; BAA91159.1; -; mRNA.
DR EMBL; AK096964; BAG53402.1; -; mRNA.
DR EMBL; AC002126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84787.1; -; Genomic_DNA.
DR EMBL; BC005210; AAH05210.1; -; mRNA.
DR EMBL; BC016478; AAH16478.2; -; mRNA.
DR CCDS; CCDS12393.1; -. [Q9NX61-1]
DR CCDS; CCDS58656.1; -. [Q9NX61-2]
DR RefSeq; NP_001243695.1; NM_001256766.1. [Q9NX61-2]
DR RefSeq; NP_060284.1; NM_017814.2. [Q9NX61-1]
DR AlphaFoldDB; Q9NX61; -.
DR BioGRID; 120269; 99.
DR IntAct; Q9NX61; 38.
DR MINT; Q9NX61; -.
DR STRING; 9606.ENSP00000162044; -.
DR GlyGen; Q9NX61; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX61; -.
DR PhosphoSitePlus; Q9NX61; -.
DR SwissPalm; Q9NX61; -.
DR BioMuta; TMEM161A; -.
DR DMDM; 74734686; -.
DR EPD; Q9NX61; -.
DR jPOST; Q9NX61; -.
DR MassIVE; Q9NX61; -.
DR MaxQB; Q9NX61; -.
DR PaxDb; Q9NX61; -.
DR PeptideAtlas; Q9NX61; -.
DR PRIDE; Q9NX61; -.
DR ProteomicsDB; 33985; -.
DR ProteomicsDB; 83046; -. [Q9NX61-1]
DR Antibodypedia; 43982; 155 antibodies from 22 providers.
DR DNASU; 54929; -.
DR Ensembl; ENST00000162044.14; ENSP00000162044.7; ENSG00000064545.15. [Q9NX61-1]
DR Ensembl; ENST00000450333.6; ENSP00000404208.2; ENSG00000064545.15. [Q9NX61-2]
DR GeneID; 54929; -.
DR KEGG; hsa:54929; -.
DR MANE-Select; ENST00000162044.14; ENSP00000162044.7; NM_017814.3; NP_060284.1.
DR UCSC; uc002nlg.5; human. [Q9NX61-1]
DR CTD; 54929; -.
DR DisGeNET; 54929; -.
DR GeneCards; TMEM161A; -.
DR HGNC; HGNC:26020; TMEM161A.
DR HPA; ENSG00000064545; Low tissue specificity.
DR MIM; 618966; gene.
DR neXtProt; NX_Q9NX61; -.
DR OpenTargets; ENSG00000064545; -.
DR PharmGKB; PA145147959; -.
DR VEuPathDB; HostDB:ENSG00000064545; -.
DR eggNOG; KOG3978; Eukaryota.
DR GeneTree; ENSGT00390000000672; -.
DR HOGENOM; CLU_027277_0_0_1; -.
DR InParanoid; Q9NX61; -.
DR OMA; VCAYIGS; -.
DR OrthoDB; 734854at2759; -.
DR PhylomeDB; Q9NX61; -.
DR TreeFam; TF314570; -.
DR PathwayCommons; Q9NX61; -.
DR SignaLink; Q9NX61; -.
DR BioGRID-ORCS; 54929; 20 hits in 1087 CRISPR screens.
DR ChiTaRS; TMEM161A; human.
DR GenomeRNAi; 54929; -.
DR Pharos; Q9NX61; Tdark.
DR PRO; PR:Q9NX61; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NX61; protein.
DR Bgee; ENSG00000064545; Expressed in pancreatic ductal cell and 190 other tissues.
DR ExpressionAtlas; Q9NX61; baseline and differential.
DR Genevisible; Q9NX61; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:BHF-UCL.
DR GO; GO:0034644; P:cellular response to UV; IDA:BHF-UCL.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR InterPro; IPR019395; Transmembrane_161A/B.
DR PANTHER; PTHR13624; PTHR13624; 1.
DR Pfam; PF10268; Tmemb_161AB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..479
FT /note="Transmembrane protein 161A"
FT /id="PRO_0000288084"
FT TOPO_DOM 29..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..479
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 96..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046042"
FT VARIANT 85
FT /note="E -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036537"
FT CONFLICT 455
FT /note="I -> V (in Ref. 2; BAG53402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 53602 MW; 4DEA8A1C04CCA33D CRC64;
MAVLGVQLVV TLLTATLMHR LAPHCSFARW LLCNGSLFRY KHPSEEELRA LAGKPRPRGR
KERWANGLSE EKPLSVPRDA PFQLETCPLT TVDALVLRFF LEYQWFVDFA VYSGGVYLFT
EAYYYMLGPA KETNIAVFWC LLTVTFSIKM FLTVTRLYFS AEEGGERSVC LTFAFLFLLL
AMLVQVVREE TLELGLEPGL ASMTQNLEPL LKKQGWDWAL PVAKLAIRVG LAVVGSVLGA
FLTFPGLRLA QTHRDALTMS EDRPMLQFLL HTSFLSPLFI LWLWTKPIAR DFLHQPPFGE
TRFSLLSDSA FDSGRLWLLV VLCLLRLAVT RPHLQAYLCL AKARVEQLRR EAGRIEAREI
QQRVVRVYCY VTVVSLQYLT PLILTLNCTL LLKTLGGYSW GLGPAPLLSP DPSSASAAPI
GSGEDEVQQT AARIAGALGG LLTPLFLRGV LAYLIWWTAA CQLLASLFGL YFHQHLAGS
