T161A_MOUSE
ID T161A_MOUSE Reviewed; 480 AA.
AC Q8VCA6; Q8BNL7; Q8BSL1; Q8C2I8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transmembrane protein 161A;
DE Flags: Precursor;
GN Name=Tmem161a;
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Hippocampus, and Thymus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 play a role in protection against oxidative stress.
CC Overexpression leads to reduced levels of oxidant-induced DNA damage
CC and apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VCA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCA6-2; Sequence=VSP_025644;
CC Name=3;
CC IsoId=Q8VCA6-3; Sequence=VSP_025643, VSP_025645;
CC -!- SIMILARITY: Belongs to the TMEM161 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK032711; BAC27995.1; -; mRNA.
DR EMBL; AK049979; BAC34016.1; -; mRNA.
DR EMBL; AK082916; BAC38686.1; -; mRNA.
DR EMBL; AK088569; BAC40428.1; ALT_INIT; mRNA.
DR EMBL; AK147962; BAE28253.1; -; mRNA.
DR EMBL; BC021367; AAH21367.1; -; mRNA.
DR CCDS; CCDS40369.1; -. [Q8VCA6-1]
DR CCDS; CCDS80890.1; -. [Q8VCA6-2]
DR RefSeq; NP_001280726.1; NM_001293797.1. [Q8VCA6-2]
DR RefSeq; NP_663572.1; NM_145597.4. [Q8VCA6-1]
DR AlphaFoldDB; Q8VCA6; -.
DR STRING; 10090.ENSMUSP00000002413; -.
DR GlyGen; Q8VCA6; 1 site.
DR PhosphoSitePlus; Q8VCA6; -.
DR EPD; Q8VCA6; -.
DR MaxQB; Q8VCA6; -.
DR PaxDb; Q8VCA6; -.
DR PRIDE; Q8VCA6; -.
DR ProteomicsDB; 263217; -. [Q8VCA6-1]
DR ProteomicsDB; 263218; -. [Q8VCA6-2]
DR ProteomicsDB; 263219; -. [Q8VCA6-3]
DR Antibodypedia; 43982; 155 antibodies from 22 providers.
DR Ensembl; ENSMUST00000002413; ENSMUSP00000002413; ENSMUSG00000002342. [Q8VCA6-1]
DR Ensembl; ENSMUST00000182980; ENSMUSP00000138499; ENSMUSG00000002342. [Q8VCA6-2]
DR GeneID; 234371; -.
DR KEGG; mmu:234371; -.
DR UCSC; uc009lzc.2; mouse. [Q8VCA6-1]
DR UCSC; uc012geu.2; mouse. [Q8VCA6-3]
DR CTD; 54929; -.
DR MGI; MGI:2384577; Tmem161a.
DR VEuPathDB; HostDB:ENSMUSG00000002342; -.
DR eggNOG; KOG3978; Eukaryota.
DR GeneTree; ENSGT00390000000672; -.
DR HOGENOM; CLU_027277_0_0_1; -.
DR InParanoid; Q8VCA6; -.
DR OMA; VCAYIGS; -.
DR OrthoDB; 734854at2759; -.
DR PhylomeDB; Q8VCA6; -.
DR TreeFam; TF314570; -.
DR BioGRID-ORCS; 234371; 5 hits in 109 CRISPR screens.
DR PRO; PR:Q8VCA6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VCA6; protein.
DR Bgee; ENSMUSG00000002342; Expressed in interventricular septum and 245 other tissues.
DR ExpressionAtlas; Q8VCA6; baseline and differential.
DR Genevisible; Q8VCA6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR InterPro; IPR019395; Transmembrane_161A/B.
DR PANTHER; PTHR13624; PTHR13624; 1.
DR Pfam; PF10268; Tmemb_161AB; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..480
FT /note="Transmembrane protein 161A"
FT /id="PRO_0000288085"
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..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..196
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025643"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025644"
FT VAR_SEQ 197..198
FT /note="EP -> MA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025645"
FT CONFLICT 342
FT /note="K -> E (in Ref. 1; BAC27995)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="P -> L (in Ref. 1; BAC40428)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> V (in Ref. 1; BAC40428)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="L -> M (in Ref. 1; BAC40428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 54015 MW; 511D268E06DA2EE8 CRC64;
MAVLGVQLVV TLFTATLMHR LAPHCSFARW LLCNGSLFRY IHPSEEELRA LSGKLRPRVR
KERWANGLHD EKPLSVPRDA HFQLQTCPLT AVDALVLRFF LEYQWFVDFA VYSVGVYLFT
EAYYFVLGPV QETNIAVFWC LLTLAFSLKV FLMVTRLYFS TKEGGERSVC LSFAFLFLLL
AMLVQVVREE TLELGLEPGL ASMTQHLEPI LKKQDWDWTL PVIKLAIRLG LAVLGSLLGA
FLIFPGLRLA QTHQDALTLS ADRPLLQLLL HTSFLSPLCT LWLWTKPVAR DFLYQAPTRN
MTFSVPSEGA FDSLRLWVLV ALCLLRLAVT RPHLQAYLCL AKARVEQLRK EAGRIEAREI
QQRVVRVYCY VTVVSLQYLT PLILTLHCTL LLKTLGGYSW ALSSTPPPLA PSQPSEALIP
VDPAGDEAQQ TAAQVAGILG GLLTPLFLRG MLAYIIWWTA ACQLLSSLFG LYFHQHLAAS
