TM168_MOUSE
ID TM168_MOUSE Reviewed; 697 AA.
AC Q91VX9; Q3TDA5;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Transmembrane protein 168;
GN Name=Tmem168;
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].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Spinal ganglion;
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].
RC STRAIN=FVB/N; 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TMEM168 family. {ECO:0000305}.
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DR EMBL; AK051532; BAC34665.1; -; mRNA.
DR EMBL; AK054353; BAC35747.1; -; mRNA.
DR EMBL; AK170302; BAE41699.1; -; mRNA.
DR EMBL; BC007160; AAH07160.1; -; mRNA.
DR EMBL; BC024911; AAH24911.1; -; mRNA.
DR CCDS; CCDS19915.1; -.
DR RefSeq; NP_083266.1; NM_028990.5.
DR RefSeq; XP_006505015.1; XM_006504952.3.
DR RefSeq; XP_006505016.1; XM_006504953.3.
DR AlphaFoldDB; Q91VX9; -.
DR BioGRID; 221586; 1.
DR STRING; 10090.ENSMUSP00000031554; -.
DR GlyGen; Q91VX9; 4 sites.
DR iPTMnet; Q91VX9; -.
DR PhosphoSitePlus; Q91VX9; -.
DR SwissPalm; Q91VX9; -.
DR EPD; Q91VX9; -.
DR MaxQB; Q91VX9; -.
DR PaxDb; Q91VX9; -.
DR PeptideAtlas; Q91VX9; -.
DR PRIDE; Q91VX9; -.
DR ProteomicsDB; 260681; -.
DR Antibodypedia; 17378; 92 antibodies from 19 providers.
DR DNASU; 101118; -.
DR Ensembl; ENSMUST00000031554; ENSMUSP00000031554; ENSMUSG00000029569.
DR GeneID; 101118; -.
DR KEGG; mmu:101118; -.
DR UCSC; uc009ayn.1; mouse.
DR CTD; 64418; -.
DR MGI; MGI:1921794; Tmem168.
DR VEuPathDB; HostDB:ENSMUSG00000029569; -.
DR eggNOG; ENOG502QRB6; Eukaryota.
DR GeneTree; ENSGT00390000005941; -.
DR HOGENOM; CLU_032315_0_0_1; -.
DR InParanoid; Q91VX9; -.
DR OMA; HLANWFC; -.
DR OrthoDB; 619817at2759; -.
DR PhylomeDB; Q91VX9; -.
DR TreeFam; TF328518; -.
DR BioGRID-ORCS; 101118; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q91VX9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91VX9; protein.
DR Bgee; ENSMUSG00000029569; Expressed in gonadal ridge and 260 other tissues.
DR ExpressionAtlas; Q91VX9; baseline and differential.
DR Genevisible; Q91VX9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR InterPro; IPR029713; TMEM168.
DR PANTHER; PTHR14437; PTHR14437; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..697
FT /note="Transmembrane protein 168"
FT /id="PRO_0000284631"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 303
FT /note="F -> L (in Ref. 1; BAE41699)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="L -> P (in Ref. 1; BAE41699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 697 AA; 79674 MW; DBAC20BAF6440D44 CRC64;
MCRSLRYCVS HCLYLAMTRL EEVNREVNMH SSVRYLGYLA RINLLVAICL GLYVRWEKTA
NSLILVIFIL GLFVLGIASI LYYYFSMEAA SLSLSNLWFG FLLGLLCFLD NSSFKSDVKE
ETTKYLLLTS IVLRILCALV ERISGYVRHR PTLLTTVEFL ELVGFAIAST TMLVEKSLSV
ILLVMALAML IIDLRMKSFL AIPNLIIFSV LLFFSSLETP QNPIAFACFF ICLVTDPFLD
IYFSGLSVTE RWKPFLHRGR ICRRLSVLFT AMIELTFFIL SAFKLRDTHL WYFVIPGFSI
FGFFWMICHI IFLLTLWGFH TKLNDCHKVY INHRADNNSL DRIMASKGMR HFCLISEQLV
FFSLLATAIL GAVSWQPTNG IFLSMFLIVL PLESMAHGLF HELGNCLGGT SVGYAIVIPT
NFCSPDGQPT LLPPEHVQEL NLRSTGMLNA IQRFFAYHMI ETYGCDYSTS GLSFDTLHSK
LKAFLELRTV DGPRHDTYVL YYSGHTHGSG EWALAGGDIL RLDTLLEWWR EKNGSFCSRL
IIILDSENST PWVKEVRKIN DQYVAVQGAE LAKTVDIEEA DPPQLGDFTR DWVEYNCNST
NNICWTEKGR TVRAVYGVSK RWSDYTLHLP TGSDVAKHWM LHFPRVTYPL VHLANWLCGL
NLFWVCKACF RCLKRLKMSW FLPTVLDTGQ GFKLVKS
