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DescriptionRecName: Full=Transmembrane protein 176A; AltName: Full=Gene signature 188; AltName: Full=Kidney-expressed gene 2 protein;
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MyHits synonymsT176A_MOUSE , Q9DCS1 , Q3UCE2 , Q8BV92 , Q8K4T0 , 515A3988A6243CCA
match map segment
ipfam:CD20  
Legends: 1, Phosphoserine. {ECO:0000244|PubMed:21183079}; 2, CONFLICT P -> H (in Ref. 2; BAC37625). {ECO:0000305}; 3, TRANSMEM Helical. {ECO:0000255}.
ID   T176A_MOUSE             Reviewed;         244 AA.
AC   Q9DCS1; Q3UCE2; Q8BV92; Q8K4T0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   10-MAY-2017, entry version 102.
DE   RecName: Full=Transmembrane protein 176A;
DE   AltName: Full=Gene signature 188;
DE   AltName: Full=Kidney-expressed gene 2 protein;
GN   Name=Tmem176a; Synonyms=Gs188, Keg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6N; TISSUE=Kidney;
RX   PubMed=11967007; DOI=10.1046/j.1523-1755.2002.00300.x;
RA   Nakajima H., Takenaka M., Kaimori J.-Y., Nagasawa Y., Kosugi A.,
RA   Kawamoto S., Imai E., Hori M., Okubo K.;
RT   "Gene expression profile of renal proximal tubules regulated by
RT   proteinuria.";
RL   Kidney Int. 61:1577-1587(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/HeJ, and C57BL/6J;
RC   TISSUE=Bone marrow, Brain, Cerebellum, and Kidney;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in lung, kidney and
CC       spleen. {ECO:0000269|PubMed:11967007}.
CC   -!- INDUCTION: Up-regulated in kidney upon proteinuria.
CC       {ECO:0000269|PubMed:11967007}.
CC   -!- SIMILARITY: Belongs to the TMEM176 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE29671.1; Type=Frameshift; Positions=228; Evidence={ECO:0000305};
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DR   EMBL; AB063313; BAB97230.1; -; mRNA.
DR   EMBL; AK002546; BAB22177.2; -; mRNA.
DR   EMBL; AK079378; BAC37625.1; -; mRNA.
DR   EMBL; AK150576; BAE29671.1; ALT_FRAME; mRNA.
DR   EMBL; AK165660; BAE38322.1; -; mRNA.
DR   EMBL; CT010190; CAJ18398.1; -; mRNA.
DR   EMBL; BC010831; AAH10831.2; -; mRNA.
DR   CCDS; CCDS39482.1; -.
DR   RefSeq; NP_001091741.1; NM_001098271.1.
DR   RefSeq; NP_079602.4; NM_025326.4.
DR   UniGene; Mm.27061; -.
DR   STRING; 10090.ENSMUSP00000098969; -.
DR   iPTMnet; Q9DCS1; -.
DR   PhosphoSitePlus; Q9DCS1; -.
DR   MaxQB; Q9DCS1; -.
DR   PaxDb; Q9DCS1; -.
DR   PeptideAtlas; Q9DCS1; -.
DR   PRIDE; Q9DCS1; -.
DR   Ensembl; ENSMUST00000101426; ENSMUSP00000098969; ENSMUSG00000023367.
DR   Ensembl; ENSMUST00000168406; ENSMUSP00000131775; ENSMUSG00000023367.
DR   Ensembl; ENSMUST00000204482; ENSMUSP00000145101; ENSMUSG00000023367.
DR   GeneID; 66058; -.
DR   KEGG; mmu:66058; -.
DR   UCSC; uc009bvw.1; mouse.
DR   CTD; 55365; -.
DR   MGI; MGI:1913308; Tmem176a.
DR   eggNOG; ENOG410IX21; Eukaryota.
DR   eggNOG; ENOG410Z9YG; LUCA.
DR   GeneTree; ENSGT00530000064074; -.
DR   HOGENOM; HOG000290691; -.
DR   HOVERGEN; HBG094019; -.
DR   InParanoid; Q9DCS1; -.
DR   OMA; SWVMQIV; -.
DR   OrthoDB; EOG091G0VIE; -.
DR   PhylomeDB; Q9DCS1; -.
DR   TreeFam; TF335389; -.
DR   ChiTaRS; Tmem176a; mouse.
DR   PRO; PR:Q9DCS1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000023367; -.
DR   CleanEx; MM_TMEM176A; -.
DR   ExpressionAtlas; Q9DCS1; baseline and differential.
DR   Genevisible; Q9DCS1; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:2001199; P:negative regulation of dendritic cell differentiation; IMP:MGI.
DR   InterPro; IPR007237; CD20-like.
DR   InterPro; IPR009281; TMEM176A/TMEM176B.
DR   PANTHER; PTHR15756; PTHR15756; 1.
DR   Pfam; PF04103; CD20; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    244       Transmembrane protein 176A.
FT                                /FTId=PRO_0000279873.
FT   TRANSMEM     60     80       Helical. {ECO:0000255}.
FT   TRANSMEM     92    112       Helical. {ECO:0000255}.
FT   TRANSMEM    122    142       Helical. {ECO:0000255}.
FT   TRANSMEM    204    224       Helical. {ECO:0000255}.
FT   MOD_RES      42     42       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT    218    218       P -> H (in Ref. 2; BAC37625).
FT                                {ECO:0000305}.
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CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        64    222       ipfam:CD20 [T]
SQ   SEQUENCE   244 AA;  26596 MW;  515A3988A6243CCA CRC64;
     MSTDMETAVV GKVDPEAPQP THIDVHIHQE SALAKLLLAG CSLLRIPASA STQSQGSSRV
     LVASWVVQTV LGALSVVLGG TLYIGHYLAM YSEGAPFWTG IVAMLAGAVA FLHKKRGGTC
     WALMRTLLVL ASFCTAVAAI VIGSRELNFY WYFLGDDVCQ RDSSYGWSTM PRTTPVPEEA
     DRIALCIYYT SMLKTLLMSL QAMLLGIWVL LLLASLTPVC VYIWKRFFTK AETEEKKLLG
     AAVI
//