TBCD7_HUMAN
ID TBCD7_HUMAN Reviewed; 293 AA.
AC Q9P0N9; E7EV96; Q2TU37; Q53F44; Q5SZL7; Q86VM8; Q96MB8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=TBC1 domain family member 7;
DE AltName: Full=Cell migration-inducing protein 23;
GN Name=TBC1D7; Synonyms=TBC7; ORFNames=HSPC239;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Kim J.W.;
RT "Identification of a migration-inducing gene.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kim J.W.;
RT "Identification of a human cell proliferation inducing gene.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFPORMS 1 AND 2).
RC TISSUE=Eye, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH TSC1.
RX PubMed=17658474; DOI=10.1016/j.bbrc.2007.07.011;
RA Nakashima A., Yoshino K., Miyamoto T., Eguchi S., Oshiro N., Kikkawa U.,
RA Yonezawa K.;
RT "Identification of TBC7 having TBC domain as a novel binding protein to
RT TSC1-TSC2 complex.";
RL Biochem. Biophys. Res. Commun. 361:218-223(2007).
RN [11]
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).
RN [12]
RP INVOLVEMENT IN MGCPH.
RX PubMed=23687350; DOI=10.1136/jmedgenet-2013-101680;
RA Capo-Chichi J.M., Tcherkezian J., Hamdan F.F., Decarie J.C.,
RA Dobrzeniecka S., Patry L., Nadon M.A., Mucha B.E., Major P., Shevell M.,
RA Bencheikh B.O., Joober R., Samuels M.E., Rouleau G.A., Roux P.P.,
RA Michaud J.L.;
RT "Disruption of TBC1D7, a subunit of the TSC1-TSC2 protein complex, in
RT intellectual disability and megalencephaly.";
RL J. Med. Genet. 50:740-744(2013).
RN [13]
RP INVOLVEMENT IN MGCPH.
RX PubMed=24515783; DOI=10.1002/humu.22529;
RA Alfaiz A.A., Micale L., Mandriani B., Augello B., Pellico M.T., Chrast J.,
RA Xenarios I., Zelante L., Merla G., Reymond A.;
RT "TBC1D7 mutations are associated with intellectual disability, macrocrania,
RT patellar dislocation and celiac disease.";
RL Hum. Mutat. 35:447-451(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RG Structural genomics consortium (SGC);
RT "Crystal structure of human tbc1 domain family member 7.";
RL Submitted (JUN-2011) to the PDB data bank.
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:17658474, ECO:0000269|PubMed:22795129}.
CC -!- INTERACTION:
CC Q9P0N9; P09917: ALOX5; NbExp=3; IntAct=EBI-3258000, EBI-79934;
CC Q9P0N9; O95429: BAG4; NbExp=5; IntAct=EBI-3258000, EBI-2949658;
CC Q9P0N9; Q9H2G9: BLZF1; NbExp=8; IntAct=EBI-3258000, EBI-2548012;
CC Q9P0N9; Q9UJC3: HOOK1; NbExp=7; IntAct=EBI-3258000, EBI-746704;
CC Q9P0N9; Q0VD86: INCA1; NbExp=3; IntAct=EBI-3258000, EBI-6509505;
CC Q9P0N9; Q14145: KEAP1; NbExp=3; IntAct=EBI-3258000, EBI-751001;
CC Q9P0N9; P08727: KRT19; NbExp=7; IntAct=EBI-3258000, EBI-742756;
CC Q9P0N9; Q92764: KRT35; NbExp=3; IntAct=EBI-3258000, EBI-1058674;
CC Q9P0N9; O95751: LDOC1; NbExp=6; IntAct=EBI-3258000, EBI-740738;
CC Q9P0N9; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-3258000, EBI-1216080;
CC Q9P0N9; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-3258000, EBI-741037;
CC Q9P0N9; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-3258000, EBI-2548751;
CC Q9P0N9; Q9H3L0: MMADHC; NbExp=3; IntAct=EBI-3258000, EBI-11111575;
CC Q9P0N9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3258000, EBI-79165;
CC Q9P0N9; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-3258000, EBI-1050213;
CC Q9P0N9; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-3258000, EBI-749607;
CC Q9P0N9; O43805: SSNA1; NbExp=7; IntAct=EBI-3258000, EBI-2515299;
CC Q9P0N9; Q9BUZ4: TRAF4; NbExp=9; IntAct=EBI-3258000, EBI-3650647;
CC Q9P0N9; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-3258000, EBI-6929619;
CC Q9P0N9; P23025: XPA; NbExp=3; IntAct=EBI-3258000, EBI-295222;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:17658474}. Note=Localizes in the cytoplasmic
CC vesicles of the endomembrane in association with TSC1-TSC2 complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P0N9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0N9-2; Sequence=VSP_041480;
CC Name=3;
CC IsoId=Q9P0N9-3; Sequence=VSP_044186;
CC Name=4;
CC IsoId=Q9P0N9-4; Sequence=VSP_044892;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, and slightly in kidney,
CC liver and placenta. {ECO:0000269|PubMed:17658474}.
CC -!- DISEASE: Macrocephaly/megalencephaly syndrome, autosomal recessive
CC (MGCPH) [MIM:248000]: An autosomal recessive disorder characterized by
CC abnormal enlargement of the cerebral hemispheres, intellectual
CC disability, large head, optic atrophy and underdeveloped skeletal
CC musculature. Head enlargement may be evident at birth or the head may
CC become abnormally large in the early years of life. Additional clinical
CC features include behavioral abnormalities, psychosis, learning
CC difficulties, prognathism, myopia and astigmatism.
CC {ECO:0000269|PubMed:23687350, ECO:0000269|PubMed:24515783}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: Was initially identified as a negative regulator of the TSC1-
CC TSC2 complex (PubMed:17658474). However, it was later shown that TBC1D7
CC is part of the TSC-TBC complex and participates in GTPase-activating
CC protein activity, leading to inhibition of the TOR signaling cascade
CC (PubMed:22795129). The differences between 2 reports might be explained
CC by experimental conditions in the initial report, in which they
CC overexpressed the TBC1D7 subunit, possibly leading to disrupt the
CC stoichiometric complex and its downstream functions.
CC {ECO:0000305|PubMed:17658474, ECO:0000305|PubMed:22795129}.
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DR EMBL; AB449888; BAH16631.1; -; mRNA.
DR EMBL; AY826820; AAX18640.1; -; mRNA.
DR EMBL; AK057228; BAB71389.1; -; mRNA.
DR EMBL; AF151073; AAF36159.1; -; mRNA.
DR EMBL; AY542308; AAT08177.1; -; mRNA.
DR EMBL; AK223445; BAD97165.1; -; mRNA.
DR EMBL; AL008729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55325.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55323.1; -; Genomic_DNA.
DR EMBL; BC050465; AAH50465.1; -; mRNA.
DR EMBL; BC007054; AAH07054.1; -; mRNA.
DR CCDS; CCDS4523.1; -. [Q9P0N9-1]
DR CCDS; CCDS47376.1; -. [Q9P0N9-2]
DR CCDS; CCDS58995.1; -. [Q9P0N9-4]
DR RefSeq; NP_001137436.1; NM_001143964.3. [Q9P0N9-1]
DR RefSeq; NP_001137437.1; NM_001143965.3. [Q9P0N9-1]
DR RefSeq; NP_001137438.1; NM_001143966.3. [Q9P0N9-2]
DR RefSeq; NP_001245386.1; NM_001258457.2. [Q9P0N9-4]
DR RefSeq; NP_001305734.1; NM_001318805.1. [Q9P0N9-1]
DR RefSeq; NP_001305738.1; NM_001318809.1. [Q9P0N9-1]
DR RefSeq; NP_057579.1; NM_016495.5. [Q9P0N9-1]
DR PDB; 3QWL; X-ray; 1.90 A; A=1-293.
DR PDB; 4Z6Y; X-ray; 2.81 A; A/B/E/G=21-293.
DR PDB; 5EJC; X-ray; 3.10 A; A/B=18-293.
DR PDB; 5ULO; X-ray; 2.14 A; C/D=115-126.
DR PDB; 7DL2; EM; 4.40 A; E=21-287.
DR PDBsum; 3QWL; -.
DR PDBsum; 4Z6Y; -.
DR PDBsum; 5EJC; -.
DR PDBsum; 5ULO; -.
DR PDBsum; 7DL2; -.
DR AlphaFoldDB; Q9P0N9; -.
DR SMR; Q9P0N9; -.
DR BioGRID; 119412; 59.
DR ComplexPortal; CPX-6142; TSC1-TSC2 complex.
DR CORUM; Q9P0N9; -.
DR IntAct; Q9P0N9; 33.
DR MINT; Q9P0N9; -.
DR STRING; 9606.ENSP00000475727; -.
DR iPTMnet; Q9P0N9; -.
DR PhosphoSitePlus; Q9P0N9; -.
DR BioMuta; TBC1D7; -.
DR DMDM; 37538019; -.
DR EPD; Q9P0N9; -.
DR jPOST; Q9P0N9; -.
DR MassIVE; Q9P0N9; -.
DR MaxQB; Q9P0N9; -.
DR PaxDb; Q9P0N9; -.
DR PeptideAtlas; Q9P0N9; -.
DR PRIDE; Q9P0N9; -.
DR ProteomicsDB; 61499; -.
DR ProteomicsDB; 77329; -.
DR ProteomicsDB; 83587; -. [Q9P0N9-1]
DR ProteomicsDB; 83588; -. [Q9P0N9-2]
DR TopDownProteomics; Q9P0N9-1; -. [Q9P0N9-1]
DR Antibodypedia; 24944; 103 antibodies from 20 providers.
DR DNASU; 51256; -.
DR Ensembl; ENST00000343141.8; ENSP00000343100.4; ENSG00000145979.18. [Q9P0N9-4]
DR Ensembl; ENST00000356436.8; ENSP00000348813.4; ENSG00000145979.18. [Q9P0N9-1]
DR Ensembl; ENST00000379300.8; ENSP00000368602.3; ENSG00000145979.18. [Q9P0N9-1]
DR Ensembl; ENST00000379307.6; ENSP00000368609.2; ENSG00000145979.18. [Q9P0N9-2]
DR Ensembl; ENST00000606214.5; ENSP00000475727.1; ENSG00000145979.18. [Q9P0N9-1]
DR GeneID; 107080638; -.
DR GeneID; 51256; -.
DR KEGG; hsa:107080638; -.
DR KEGG; hsa:51256; -.
DR MANE-Select; ENST00000379300.8; ENSP00000368602.3; NM_016495.6; NP_057579.1.
DR UCSC; uc003nal.5; human. [Q9P0N9-1]
DR CTD; 107080638; -.
DR CTD; 51256; -.
DR DisGeNET; 107080638; -.
DR DisGeNET; 51256; -.
DR GeneCards; TBC1D7; -.
DR HGNC; HGNC:21066; TBC1D7.
DR HPA; ENSG00000145979; Low tissue specificity.
DR MalaCards; TBC1D7; -.
DR MIM; 248000; phenotype.
DR MIM; 612655; gene.
DR neXtProt; NX_Q9P0N9; -.
DR OpenTargets; ENSG00000145979; -.
DR Orphanet; 268920; Isolated megalencephaly.
DR PharmGKB; PA134929978; -.
DR VEuPathDB; HostDB:ENSG00000145979; -.
DR eggNOG; ENOG502QPZD; Eukaryota.
DR GeneTree; ENSGT00390000009122; -.
DR HOGENOM; CLU_082520_0_0_1; -.
DR InParanoid; Q9P0N9; -.
DR OMA; VMHTMWL; -.
DR PhylomeDB; Q9P0N9; -.
DR TreeFam; TF323655; -.
DR PathwayCommons; Q9P0N9; -.
DR Reactome; R-HSA-8854214; TBC/RABGAPs.
DR SignaLink; Q9P0N9; -.
DR BioGRID-ORCS; 107080638; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 51256; 22 hits in 1091 CRISPR screens.
DR Pharos; Q9P0N9; Tbio.
DR PRO; PR:Q9P0N9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P0N9; protein.
DR Bgee; ENSG00000145979; Expressed in cortical plate and 167 other tissues.
DR ExpressionAtlas; Q9P0N9; baseline and differential.
DR Genevisible; Q9P0N9; HS.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033596; C:TSC1-TSC2 complex; IPI:ComplexPortal.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IDA:ComplexPortal.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0070848; P:response to growth factor; IMP:UniProtKB.
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 3D-structure; Alternative splicing; Cytoplasmic vesicle; GTPase activation;
KW Reference proteome.
FT CHAIN 1..293
FT /note="TBC1 domain family member 7"
FT /id="PRO_0000208031"
FT DOMAIN 50..231
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT VAR_SEQ 1..73
FT /note="MTEDSQRNFRSVYYEKVGFRGVEEKKSLEILLKDDRLDTEKLCTFSQRFPLP
FT SMYRALVWKVLLGILPPHHES -> MEGASRNLASTPRV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044186"
FT VAR_SEQ 38..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_041480"
FT VAR_SEQ 127..172
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044892"
FT VARIANT 67
FT /note="L -> W (in dbSNP:rs543580)"
FT /id="VAR_052537"
FT VARIANT 136
FT /note="A -> T (in dbSNP:rs9381921)"
FT /id="VAR_052538"
FT CONFLICT 59
FT /note="V -> I (in Ref. 6; BAD97165)"
FT /evidence="ECO:0000305"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3QWL"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 74..94
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3QWL"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4Z6Y"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:3QWL"
FT TURN 164..169
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:3QWL"
FT TURN 210..214
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3QWL"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:3QWL"
SQ SEQUENCE 293 AA; 33972 MW; C2F35E10F10D00C2 CRC64;
MTEDSQRNFR SVYYEKVGFR GVEEKKSLEI LLKDDRLDTE KLCTFSQRFP LPSMYRALVW
KVLLGILPPH HESHAKVMMY RKEQYLDVLH ALKVVRFVSD ATPQAEVYLR MYQLESGKLP
RSPSFPLEPD DEVFLAIAKA MEEMVEDSVD CYWITRRFVN QLNTKYRDSL PQLPKAFEQY
LNLEDGRLLT HLRMCSAAPK LPYDLWFKRC FAGCLPESSL QRVWDKVVSG SCKILVFVAV
EILLTFKIKV MALNSAEKIT KFLENIPQDS SDAIVSKAID LWHKHCGTPV HSS
