TBC17_MOUSE
ID TBC17_MOUSE Reviewed; 645 AA.
AC Q8BYH7; Q3TCA5;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=TBC1 domain family member 17;
GN Name=Tbc1d17;
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, and NOD; TISSUE=Epididymis, and Spinal cord;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: Probable GTPase-activating protein for Rab8; its transient
CC association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated
CC endocytic trafficking, such as of transferrin receptor (TfR) and
CC reduces Rab8 recruitnment to tubules emanating from the endocytic
CC recycling compartment (ERC). Involved in regulation of autophagy.
CC Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-
CC 50; the function requires its catalytic activity, however, the involved
CC Rab is not known (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with OPTN.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
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DR EMBL; AK136705; BAE23103.1; -; mRNA.
DR EMBL; AK170821; BAE42052.1; -; mRNA.
DR EMBL; AK039566; BAC30387.1; -; mRNA.
DR EMBL; CH466603; EDL22756.1; -; Genomic_DNA.
DR CCDS; CCDS39944.1; -.
DR RefSeq; NP_001036120.1; NM_001042655.1.
DR AlphaFoldDB; Q8BYH7; -.
DR SMR; Q8BYH7; -.
DR BioGRID; 231386; 28.
DR STRING; 10090.ENSMUSP00000048260; -.
DR iPTMnet; Q8BYH7; -.
DR PhosphoSitePlus; Q8BYH7; -.
DR EPD; Q8BYH7; -.
DR MaxQB; Q8BYH7; -.
DR PaxDb; Q8BYH7; -.
DR PRIDE; Q8BYH7; -.
DR ProteomicsDB; 254651; -.
DR Antibodypedia; 62898; 23 antibodies from 12 providers.
DR Ensembl; ENSMUST00000047085; ENSMUSP00000048260; ENSMUSG00000038520.
DR GeneID; 233204; -.
DR KEGG; mmu:233204; -.
DR UCSC; uc009grc.1; mouse.
DR CTD; 79735; -.
DR MGI; MGI:2449973; Tbc1d17.
DR VEuPathDB; HostDB:ENSMUSG00000038520; -.
DR eggNOG; KOG2197; Eukaryota.
DR GeneTree; ENSGT00940000158989; -.
DR HOGENOM; CLU_004457_2_2_1; -.
DR InParanoid; Q8BYH7; -.
DR OMA; FAILMER; -.
DR OrthoDB; 1523119at2759; -.
DR PhylomeDB; Q8BYH7; -.
DR TreeFam; TF314296; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 233204; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Tbc1d17; mouse.
DR PRO; PR:Q8BYH7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BYH7; protein.
DR Bgee; ENSMUSG00000038520; Expressed in hindlimb stylopod muscle and 246 other tissues.
DR ExpressionAtlas; Q8BYH7; baseline and differential.
DR Genevisible; Q8BYH7; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR021935; SGSM1/2_RBD.
DR Pfam; PF12068; PH_RBD; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasmic vesicle; GTPase activation; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..645
FT /note="TBC1 domain family member 17"
FT /id="PRO_0000208046"
FT DOMAIN 310..520
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..309
FT /note="Required for interaction with OPTN"
FT /evidence="ECO:0000250"
FT REGION 596..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 377
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 418
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA65"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA65"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA65"
FT MOD_RES 615
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA65"
FT CONFLICT 75
FT /note="E -> Q (in Ref. 1; BAC30387)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="S -> F (in Ref. 1; BAC30387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 72860 MW; B0C3FC3C0F4A27E9 CRC64;
MEGSSYRVVF EKGGVYLHTS ARKHQDPDSL IAGVIRVVEK DSDVFLHWAP VEEAGDPTQI
LFKKDPSRGE PSTSEEEPTF DPGYEPDWAV ISTVRPQPHL AEPRKGAEPS SSRSSWAFSV
SLGELKSIRR SKPGLSWAYL VLVTQAGGSL PALHFHRGGT RALLRVLSRY LLLASSPQDS
RLYLVFPQDP SALSDSFHHL QLFDQDSSNV VSRFLQDPYS TTFSSFSRVT NFFRGALQPH
PEGASSPNLP PLPDDEPEPG FEVISCVELG QRPTVERAPP VTEEEWNRYV GPEGRLQNVP
ELKNRIFSGG LSPGLRREAW KFLLGYLSWE SSAEEHKAHV RKKTDEYFRM KLQWKSVSAE
QERRNSLLHG YRSLIERDVS RTDRTNKFYE GPENPGLSLL HDILLTYCMY HFDLGYVQGM
SDLLSPILFV VQNEVDAFWC FCGFMELVHG NFEESQETMK RQLGQLLLLL RVLDQPLCDF
LDSQDSGSLC FCFRWLLIWF KREFPFPDVL RLWEVLWTGL PGPNLHLLVA CAILDMERDT
LMLSGFGSNE ILKHINELTM KLSVEDVLTR AEALYRQLTA CPELPHNVQE ILGLAQPEEP
SSPSPPVSPM PLSPTRAPLP PPLPEEVIPQ PDSSLEILPE DEDGA
