TBC25_MOUSE
ID TBC25_MOUSE Reviewed; 742 AA.
AC A1A5B6; Q8BIM6; Q8BIW8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=TBC1 domain family member 25;
GN Name=Tbc1d25;
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=Aorta, and Medulla oblongata;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; THR-214 AND SER-560, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, and Spleen;
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 INTERACTION WITH MAP1LC3B; GABARAP AND GABARAPL2.
RX PubMed=21383079; DOI=10.1083/jcb.201008107;
RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal
RT maturation.";
RL J. Cell Biol. 192:839-853(2011).
CC -!- FUNCTION: Acts as a GTPase-activating protein specific for RAB33B.
CC Involved in the regulation of autophagosome maturation, the process in
CC which autophagosomes fuse with endosomes and lysosomes. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with MAP1LC3B, GABARAP and
CC GABARAPL2. {ECO:0000269|PubMed:21383079}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250}. Note=It is dispersed in the cytoplasm
CC under nutrient-rich conditions. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK040932; BAC30751.1; ALT_INIT; mRNA.
DR EMBL; AK078145; BAC37146.1; -; mRNA.
DR EMBL; AL663032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128566; AAI28567.1; -; mRNA.
DR RefSeq; NP_001159909.1; NM_001166437.1.
DR RefSeq; NP_766066.2; NM_172478.3.
DR AlphaFoldDB; A1A5B6; -.
DR SMR; A1A5B6; -.
DR BioGRID; 229113; 2.
DR STRING; 10090.ENSMUSP00000047838; -.
DR iPTMnet; A1A5B6; -.
DR PhosphoSitePlus; A1A5B6; -.
DR EPD; A1A5B6; -.
DR jPOST; A1A5B6; -.
DR MaxQB; A1A5B6; -.
DR PaxDb; A1A5B6; -.
DR PeptideAtlas; A1A5B6; -.
DR PRIDE; A1A5B6; -.
DR ProteomicsDB; 254652; -.
DR Antibodypedia; 54837; 45 antibodies from 16 providers.
DR DNASU; 209815; -.
DR Ensembl; ENSMUST00000039892; ENSMUSP00000047838; ENSMUSG00000039201.
DR GeneID; 209815; -.
DR KEGG; mmu:209815; -.
DR UCSC; uc009sog.2; mouse.
DR CTD; 4943; -.
DR MGI; MGI:2444862; Tbc1d25.
DR VEuPathDB; HostDB:ENSMUSG00000039201; -.
DR eggNOG; KOG2197; Eukaryota.
DR GeneTree; ENSGT00940000159173; -.
DR InParanoid; A1A5B6; -.
DR OMA; YYTARNE; -.
DR OrthoDB; 1495285at2759; -.
DR PhylomeDB; A1A5B6; -.
DR TreeFam; TF323518; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 209815; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Tbc1d25; mouse.
DR PRO; PR:A1A5B6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A1A5B6; protein.
DR Bgee; ENSMUSG00000039201; Expressed in lumbar dorsal root ganglion and 203 other tissues.
DR ExpressionAtlas; A1A5B6; baseline and differential.
DR Genevisible; A1A5B6; MM.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISS:UniProtKB.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
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; Cytoplasm; Cytoplasmic vesicle; GTPase activation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..742
FT /note="TBC1 domain family member 25"
FT /id="PRO_0000288509"
FT DOMAIN 282..488
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..663
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 115
FT /note="T -> A (in Ref. 1; BAC37146)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="S -> Y (in Ref. 1; BAC30751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 82575 MW; F1CD1A40BDB46F47 CRC64;
MRPPAQARWE GQGPTAPLRL RSGARWGRGR PHCWVYVRVR VTIGYHLDRD DSGGMATTSA
ASDSACSAAP PPVGGAQAAA AVEEEEREVV RVRVKKCESF LSPEFRSFAV DPQITSLDVL
QHILIRAFDL NGKKNFGISY LARDRLGQET FLSLLSDWDL STAFATASKP YLQLRVDIRP
SEDSPLLEDW DIISPKDVIG SDVLLAEKRS SLTTAALPFT QSILSQVGRT LSKVQQVLSW
SYGEDVKPFK PPLSDAEFHT YLNHEGQLSR PEELRLRIYH GGVEPSLRKV VWRYLLNVYP
DGLTGRERMD YMKRKSREYE QLKSEWAQRV NPEDLEFIRS TVLKDVLRTD RAHPYYAGPE
DGPHLRALHD LLTTYAVTHP QVSYCQGMSD LASPILAVMD HEGHAFVCFC GIMKRLAANF
HPDGRAMATK FAHLKLLLRH ADPDFYQYLQ EAGADDLFFC YRWLLLELKR EFAFDDALRM
LEVTWSSLPP DPPEHEVELV GPPSQVADTG FGSHRGRPVR QRHMLRPAGG GGGAFEDAVV
HLAASSQGPS GGGRLLRQAS LDGLQQLRDN MGLRKDHLVQ LSHPATLISS KSLSEPLLNS
PDPLLSTSSR PDSPSSSSPP STQEASPSGD IAVGSPLMQE VGSPRDPGKP VPPPPPMGLP
PPQEFGRGNP FMLFLCLAIL LEHRDHIMRN GLDYNELAMH FDRLVRKHHL GRVLRRAKAL
FADYLQSEVW DSEEGAEATA PS
