TBC15_MOUSE
ID TBC15_MOUSE Reviewed; 671 AA.
AC Q9CXF4; Q3UI41;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=TBC1 domain family member 15;
DE AltName: Full=GTPase-activating protein RAB7;
DE Short=GAP for RAB7;
DE Short=Rab7-GAP;
GN Name=Tbc1d15;
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=Colon, Kidney, and Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16055087; DOI=10.1016/j.bbrc.2005.07.070;
RA Zhang X.M., Walsh B., Mitchell C.A., Rowe T.;
RT "TBC domain family, member 15 is a novel mammalian Rab GTPase-activating
RT protein with substrate preference for Rab7.";
RL Biochem. Biophys. Res. Commun. 335:154-161(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [6]
RP FUNCTION.
RX PubMed=20363736; DOI=10.1074/jbc.m110.111633;
RA Peralta E.R., Martin B.C., Edinger A.L.;
RT "Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation
RT state, lysosomal morphology, and growth factor dependence.";
RL J. Biol. Chem. 285:16814-16821(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=33536340; DOI=10.1073/pnas.2018355118;
RA Shimada K., Park S., Miyata H., Yu Z., Morohoshi A., Oura S., Matzuk M.M.,
RA Ikawa M.;
RT "ARMC12 regulates spatiotemporal mitochondrial dynamics during
RT spermiogenesis and is required for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not act
CC on RAB4, RAB5 or RAB6. {ECO:0000269|PubMed:16055087,
CC ECO:0000269|PubMed:20363736}.
CC -!- SUBUNIT: Interacts with non-phosphorylated form of RAB8A;
CC phosphorylation of RAB8A at 'Thr-72' disrupts this interaction (By
CC similarity). Interacts with ARMC12 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TC07}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16055087}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart, liver
CC and testis and lower expression in brain, spleen, lung, kidney and
CC skeletal muscle. {ECO:0000269|PubMed:16055087,
CC ECO:0000269|PubMed:33536340}.
CC -!- CAUTION: PubMed:16055087 showns that TBC1D15 can also functions as
CC GTPase activating for RAB11 at a lower extent than for RAB7A, however
CC this function is not confirmed by PubMed:20363736. {ECO:0000305}.
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DR EMBL; AK014477; BAB29380.1; -; mRNA.
DR EMBL; AK078875; BAC37435.1; -; mRNA.
DR EMBL; AK147085; BAE27665.1; -; mRNA.
DR CCDS; CCDS24176.1; -.
DR RefSeq; NP_079982.3; NM_025706.3.
DR AlphaFoldDB; Q9CXF4; -.
DR SMR; Q9CXF4; -.
DR BioGRID; 211646; 2.
DR IntAct; Q9CXF4; 2.
DR STRING; 10090.ENSMUSP00000020339; -.
DR iPTMnet; Q9CXF4; -.
DR PhosphoSitePlus; Q9CXF4; -.
DR SwissPalm; Q9CXF4; -.
DR EPD; Q9CXF4; -.
DR jPOST; Q9CXF4; -.
DR MaxQB; Q9CXF4; -.
DR PaxDb; Q9CXF4; -.
DR PRIDE; Q9CXF4; -.
DR ProteomicsDB; 254650; -.
DR Antibodypedia; 2850; 97 antibodies from 17 providers.
DR Ensembl; ENSMUST00000020339; ENSMUSP00000020339; ENSMUSG00000020130.
DR GeneID; 66687; -.
DR KEGG; mmu:66687; -.
DR UCSC; uc007hax.2; mouse.
DR CTD; 64786; -.
DR MGI; MGI:1913937; Tbc1d15.
DR VEuPathDB; HostDB:ENSMUSG00000020130; -.
DR eggNOG; KOG2197; Eukaryota.
DR GeneTree; ENSGT00940000156429; -.
DR HOGENOM; CLU_004457_2_2_1; -.
DR InParanoid; Q9CXF4; -.
DR OMA; SVVEWTP; -.
DR OrthoDB; 1495285at2759; -.
DR PhylomeDB; Q9CXF4; -.
DR TreeFam; TF314296; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 66687; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Tbc1d15; mouse.
DR PRO; PR:Q9CXF4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CXF4; protein.
DR Bgee; ENSMUSG00000020130; Expressed in secondary oocyte and 258 other tissues.
DR Genevisible; Q9CXF4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
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 Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT CHAIN 2..671
FT /note="TBC1 domain family member 15"
FT /id="PRO_0000208043"
FT DOMAIN 329..539
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 650..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC07"
SQ SEQUENCE 671 AA; 76527 MW; A822B14AE4268FDE CRC64;
MAAAGVVSGK IIYEQEGVYI HSSCGKANDQ DSLISGILRV LEKDAEVIVD WRPLDDALDS
SSILCAGKDS SSVVEWTQAP KERAHRGSDQ QSSYEAEWDM VTTVSFKKKP HTNGDAPGHR
NGKSKWSFLF SLADLKSVKQ SKEGMGWSYL VFCLKDDVML PALHFHQGDS KLLIESLEKY
VVLCESPQDS RTLLVNCQNK SLSQSFENLL DEPAYGLIQK IKKDPYTATM VGFSKVTNYI
FDSLRGSDPS THQRPPSEMA DFLSDAIPGL KINQQEEPGF EVITRIDLGE RPVVQRREPV
SLEEWNKSLD PEGRLVAVES MKQKIFRGGL SHSLRKQAWK FLLGYFPWDS TKEERTQLQK
QKTDEYFRMK LQWKSVSEAQ EKRNSRLRDY RSLIEKDVNR TDRTNKFYEG QDNPGLILLH
DILMTYCMYD FDLGYVQGMS DLLSPLLYVM ENEVDAFWCF ASYMDQMHQN FEEQMQGMKT
QLIQLSTLLR LLDSGFCSYL ESQDSGYLYF CFRWLLIRFK REFSFLDILR LWEVMWTELP
CKNFHLLLCC AILESEKQQI MAKHYGFNEI LKHINELSMK IDVEDILCKA EAISLQMAQC
KELPQAVCEI LGLQDSEITT PDSDTDENVG SPCPVSAFPS STLPILAASE AKDDSPTQTL
ASPNACRLTP A
