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TM117_MOUSE
ID   TM117_MOUSE             Reviewed;         514 AA.
AC   Q8BH18; Q8C6X8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Transmembrane protein 117;
GN   Name=Tmem117;
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=Cerebellum, Head, and Heart;
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   TISSUE=Olfactory epithelium;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453, AND IDENTIFICATION BY
RP   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 expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Involved in endoplasmic reticulum (ER) stress-induced cell
CC       death pathway. {ECO:0000250|UniProtKB:Q9H0C3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H0C3};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the TMEM117 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35210.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK047437; BAC33060.1; -; mRNA.
DR   EMBL; AK048597; BAC33384.1; -; mRNA.
DR   EMBL; AK052935; BAC35210.1; ALT_INIT; mRNA.
DR   EMBL; BC051178; AAH51178.1; -; mRNA.
DR   CCDS; CCDS27774.1; -.
DR   RefSeq; NP_848904.1; NM_178789.4.
DR   AlphaFoldDB; Q8BH18; -.
DR   STRING; 10090.ENSMUSP00000079038; -.
DR   GlyGen; Q8BH18; 2 sites.
DR   iPTMnet; Q8BH18; -.
DR   PhosphoSitePlus; Q8BH18; -.
DR   PaxDb; Q8BH18; -.
DR   PRIDE; Q8BH18; -.
DR   ProteomicsDB; 259522; -.
DR   Antibodypedia; 25193; 93 antibodies from 18 providers.
DR   DNASU; 320709; -.
DR   Ensembl; ENSMUST00000080141; ENSMUSP00000079038; ENSMUSG00000063296.
DR   GeneID; 320709; -.
DR   KEGG; mmu:320709; -.
DR   UCSC; uc007xjn.1; mouse.
DR   CTD; 84216; -.
DR   MGI; MGI:2444580; Tmem117.
DR   VEuPathDB; HostDB:ENSMUSG00000063296; -.
DR   eggNOG; ENOG502QXR1; Eukaryota.
DR   GeneTree; ENSGT00390000013052; -.
DR   HOGENOM; CLU_047657_0_0_1; -.
DR   InParanoid; Q8BH18; -.
DR   OMA; GSMGAYI; -.
DR   OrthoDB; 801372at2759; -.
DR   PhylomeDB; Q8BH18; -.
DR   TreeFam; TF336012; -.
DR   BioGRID-ORCS; 320709; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Tmem117; mouse.
DR   PRO; PR:Q8BH18; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8BH18; protein.
DR   Bgee; ENSMUSG00000063296; Expressed in otolith organ and 158 other tissues.
DR   Genevisible; Q8BH18; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   InterPro; IPR029370; TMEM117.
DR   PANTHER; PTHR31226; PTHR31226; 1.
DR   Pfam; PF15113; TMEM117; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..514
FT                   /note="Transmembrane protein 117"
FT                   /id="PRO_0000251205"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..65
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..198
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        220..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..394
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..514
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   REGION          430..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         453
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H0C3"
SQ   SEQUENCE   514 AA;  60356 MW;  5912873BC472C8B8 CRC64;
     MGKDFRYYFQ HPWSRMIVAY LVIFFNFLIF AEDPVSHSQT EANVIVVGNC FSFVTNKYPR
     GVGWRILKVL LWLLAILIGL IAGKFLFHQR LFGQLLRLKM FREDHGSWMT MFFSTILFLF
     IFSHIYNTIL LMDGNMGAYL ITDYMGIRNE SFMKLAAVGT WMGDFVTAWM VTDMMLQDKP
     YPDWGKSARA FWKKGNVRII LFWTVLFTLT SVVVLVITTD WISWDKLNRG FLPSDEVSRA
     FLASFILVFD LLIVMQDWEF PHFMGDVDVN LPGLHTPHMQ FKIPFFQKIF KEEYRIHITG
     KWFNYGIIFL VLILDLNMWK NQIFYKPHEY GQYIGPGQKI YTVKDSESLK DLNRTKLSWE
     WRSNHTNPQT NKTYVEGDMF LHSRFIGASL DVKCLAFVPS LIAFVWFGFF IWFFGRFLKN
     EQGMENQDKT YTRMKRKSPS EHSKDMGITR ENTQVSVEDP LNDPALVCIR SDFNEIVYKS
     SHLTSENLSL HLKESTSEVE AEQEPAASQR MRTN
 
 
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