TBCD7_MOUSE
ID TBCD7_MOUSE Reviewed; 293 AA.
AC Q9D0K0; B7ZNC1; Q05AE0; Q3U0V0;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=TBC1 domain family member 7;
GN Name=Tbc1d7;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE TSC-TBC COMPLEX, AND INTERACTION WITH TSC1.
RX PubMed=22795129; DOI=10.1016/j.molcel.2012.06.009;
RA Dibble C.C., Elis W., Menon S., Qin W., Klekota J., Asara J.M., Finan P.M.,
RA Kwiatkowski D.J., Murphy L.O., Manning B.D.;
RT "TBC1D7 is a third subunit of the TSC1-TSC2 complex upstream of mTORC1.";
RL Mol. Cell 47:535-546(2012).
CC -!- FUNCTION: Component of the TSC-TBC complex, that contains TBC1D7 in
CC addition to the TSC1-TSC2 complex and consists of the functional
CC complex possessing GTPase-activating protein (GAP) activity toward RHEB
CC in response to alterations in specific cellular growth conditions. The
CC small GTPase RHEB is a direct activator of the protein kinase activity
CC of mTORC1 and the TSC-TBC complex acts as a negative regulator of
CC mTORC1 signaling cascade by acting as a GAP for RHEB. Participates in
CC the proper sensing of growth factors and glucose, but not amino acids,
CC by mTORC1. It is unclear whether TBC1D7 acts as a GTPase-activating
CC protein and additional studies are required to answer this question.
CC {ECO:0000269|PubMed:22795129}.
CC -!- SUBUNIT: Component of the TSC-TBC complex (also named Rhebulator
CC complex), composed of the TSC1-TSC2 heterodimer and TBC1D7. Interacts
CC with TSC1 (via C-terminal half of the coiled-coil domain).
CC {ECO:0000269|PubMed:22795129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Note=Localizes
CC in the cytoplasmic vesicles of the endomembrane in association with
CC TSC1-TSC2 complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D0K0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0K0-2; Sequence=VSP_044187;
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DR EMBL; AK011356; BAB27564.1; -; mRNA.
DR EMBL; AK156543; BAE33751.1; -; mRNA.
DR EMBL; CH466546; EDL40988.1; -; Genomic_DNA.
DR EMBL; CH466546; EDL40989.1; -; Genomic_DNA.
DR EMBL; BC125307; AAI25308.1; -; mRNA.
DR EMBL; BC125309; AAI25310.1; -; mRNA.
DR EMBL; BC145156; AAI45157.1; -; mRNA.
DR EMBL; BC145157; AAI45158.1; -; mRNA.
DR CCDS; CCDS26476.1; -. [Q9D0K0-1]
DR CCDS; CCDS88446.1; -. [Q9D0K0-2]
DR RefSeq; NP_001239568.1; NM_001252639.1. [Q9D0K0-1]
DR RefSeq; NP_001239569.1; NM_001252640.1. [Q9D0K0-2]
DR RefSeq; NP_080211.1; NM_025935.3. [Q9D0K0-1]
DR AlphaFoldDB; Q9D0K0; -.
DR SMR; Q9D0K0; -.
DR BioGRID; 211900; 12.
DR IntAct; Q9D0K0; 11.
DR STRING; 10090.ENSMUSP00000137280; -.
DR PhosphoSitePlus; Q9D0K0; -.
DR EPD; Q9D0K0; -.
DR MaxQB; Q9D0K0; -.
DR PaxDb; Q9D0K0; -.
DR PRIDE; Q9D0K0; -.
DR ProteomicsDB; 263077; -. [Q9D0K0-1]
DR ProteomicsDB; 263078; -. [Q9D0K0-2]
DR Antibodypedia; 24944; 103 antibodies from 20 providers.
DR Ensembl; ENSMUST00000021797; ENSMUSP00000021797; ENSMUSG00000021368. [Q9D0K0-1]
DR Ensembl; ENSMUST00000179852; ENSMUSP00000137280; ENSMUSG00000021368. [Q9D0K0-1]
DR Ensembl; ENSMUST00000220787; ENSMUSP00000152358; ENSMUSG00000021368. [Q9D0K0-2]
DR GeneID; 67046; -.
DR KEGG; mmu:67046; -.
DR UCSC; uc007qfu.2; mouse. [Q9D0K0-1]
DR UCSC; uc011yyt.2; mouse. [Q9D0K0-2]
DR CTD; 51256; -.
DR MGI; MGI:1914296; Tbc1d7.
DR VEuPathDB; HostDB:ENSMUSG00000021368; -.
DR eggNOG; ENOG502QPZD; Eukaryota.
DR GeneTree; ENSGT00390000009122; -.
DR HOGENOM; CLU_082520_0_0_1; -.
DR InParanoid; Q9D0K0; -.
DR OMA; VMHTMWL; -.
DR OrthoDB; 1440539at2759; -.
DR PhylomeDB; Q9D0K0; -.
DR TreeFam; TF323655; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 67046; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Tbc1d7; mouse.
DR PRO; PR:Q9D0K0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D0K0; protein.
DR Bgee; ENSMUSG00000021368; Expressed in lens of camera-type eye and 178 other tissues.
DR ExpressionAtlas; Q9D0K0; baseline and differential.
DR Genevisible; Q9D0K0; MM.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0033596; C:TSC1-TSC2 complex; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0070848; P:response to growth factor; ISO:MGI.
DR Gene3D; 1.10.8.680; -; 1.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR039842; TBC1D7.
DR InterPro; IPR043039; TBC1D7_dom2.
DR PANTHER; PTHR13530; PTHR13530; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; GTPase activation;
KW Reference proteome.
FT CHAIN 1..293
FT /note="TBC1 domain family member 7"
FT /id="PRO_0000208032"
FT DOMAIN 50..231
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT VAR_SEQ 228..265
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044187"
SQ SEQUENCE 293 AA; 33826 MW; D71D019F574BDA89 CRC64;
MTDDSQRNFR SVYYEKVGFR GVEEKKSLEI LLKDDRLDIE KLCTFSQRFP LPSMYRALVW
KALLGILPPH HDTHSQVMAY RKDQYHDILH ALTVVRFISD ATPQAEVYLR MYQLESGKLP
RSPSFPLEPE DEVFLAIAKA MEEMVEDSVD CYWISRCFVK QLNNKYRDAL PQLPKAFEQY
LNLEDSRLLS HLKTCSAVSK LPYDLWFQRC FAGCLPESSL QRVWDKVVSG SCKILVFVAV
EILLTFKIKV MALNSAEKIT KFLENIPQDS SDAIVSKAID LWHKHCGTPV HSA
