TBC14_MOUSE
ID TBC14_MOUSE Reviewed; 694 AA.
AC Q8CGA2; Q3V2L6; Q4VAC6; Q8CHA5;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=TBC1 domain family member 14;
GN Name=Tbc1d14; Synonyms=D5Ertd110e, Kiaa1322;
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=Czech II; TISSUE=Olfactory epithelium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-242.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-694.
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Plays a role in the regulation of starvation-induced
CC autophagosome formation. Together with the TRAPPIII complex, regulates
CC a constitutive trafficking step from peripheral recycling endosomes to
CC the early Golgi, maintaining the cycling pool of ATG9 required for
CC initiation of autophagy. {ECO:0000250|UniProtKB:Q9P2M4}.
CC -!- SUBUNIT: Interacts with ULK1. May interact with RAB11A and RAB11B, but
CC does not exhibit any GTPase-activating activity toward these proteins.
CC Interacts with TRAPPC8. {ECO:0000250|UniProtKB:Q9P2M4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:Q9P2M4}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9P2M4}. Note=After amino acid starvation, Golgi
CC apparatus-associated protein levels increase compared with fed
CC conditions. May be cycling between the Golgi apparatus and an endosomal
CC pool, redistributing to the Golgi apparatus upon starvation.
CC {ECO:0000250|UniProtKB:Q9P2M4}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH96446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE20781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC096446; AAH96446.1; ALT_INIT; mRNA.
DR EMBL; BC042515; AAH42515.1; ALT_INIT; mRNA.
DR EMBL; AK131724; BAE20781.1; ALT_INIT; mRNA.
DR EMBL; AB093293; BAC41476.1; -; mRNA.
DR CCDS; CCDS19240.2; -.
DR RefSeq; NP_001106833.1; NM_001113362.1.
DR RefSeq; NP_001106835.1; NM_001113364.1.
DR RefSeq; NP_598671.3; NM_133910.3.
DR AlphaFoldDB; Q8CGA2; -.
DR SMR; Q8CGA2; -.
DR STRING; 10090.ENSMUSP00000116519; -.
DR iPTMnet; Q8CGA2; -.
DR PhosphoSitePlus; Q8CGA2; -.
DR EPD; Q8CGA2; -.
DR MaxQB; Q8CGA2; -.
DR PaxDb; Q8CGA2; -.
DR PRIDE; Q8CGA2; -.
DR ProteomicsDB; 254822; -.
DR DNASU; 100855; -.
DR GeneID; 100855; -.
DR KEGG; mmu:100855; -.
DR CTD; 57533; -.
DR MGI; MGI:1098708; Tbc1d14.
DR eggNOG; KOG2223; Eukaryota.
DR InParanoid; Q8CGA2; -.
DR OrthoDB; 798837at2759; -.
DR PhylomeDB; Q8CGA2; -.
DR Reactome; R-MMU-8854214; TBC/RABGAPs.
DR BioGRID-ORCS; 100855; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Tbc1d14; mouse.
DR PRO; PR:Q8CGA2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CGA2; protein.
DR GO; GO:0005776; C:autophagosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0071955; P:recycling endosome to Golgi transport; ISO:MGI.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:MGI.
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 Golgi apparatus; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..694
FT /note="TBC1 domain family member 14"
FT /id="PRO_0000208041"
FT DOMAIN 402..612
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 272..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M4"
FT CONFLICT 46
FT /note="E -> D (in Ref. 1; AAH96446 and 2; BAE20781)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="H -> Q (in Ref. 1; AAH42515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 694 AA; 78315 MW; C696A829263CA33E CRC64;
MTDGNLSTSM NGVALMGILD GRQGDSLQDL QHLSIKAAPR SLSVPEYGPS LKLGALEDRH
SLQSVDSGIP TLEIGNPEPV PCSVVHVKRK QSESEIVPER AFQSACPLPS CTPSAPTCSE
REQVVRKSST FPRTGYDSVK LYSPTSKALS RSDNVSVCSV SSLGTELSTT LSVSNEDILD
LMVTSNSSAI VTLENDDDPQ FTDVTLSSIN ETSDLHQQDC VAETEEGRKL KLLHPFSHFF
TRNLLARKQN ARLDRQRDLG WKLFGKVPLR ETAQKDSKKT QKEYEDKAGR PSRPPSPKQN
VRKNLDFEPL STTALILEDR PANLPAKPAE EAQKHRQQYE EMVLQAKKRE LKEAQRRRKQ
LEERCKVEES IGNAVLTWNN EILPNWETMW CSKKVRDLWW QGIPPSVRGK VWSLAIGNEL
NITHELFDIC LARAKERWRS LSTGGSEVEN EDAGFSAADR EASLELIKLD ISRTFPNLCI
FQQGGPYHDM LHSILGAYTC YRPDVGYVQG MSFIAAVLIL NLDTADAFIA FSNLLNKPCQ
MAFFRVDHGL MLTYFAAFEV FFEENLPKLF AHFKKNNLTA DIYLIDWIFT LYSKSLPLDL
ACRIWDVFCR DGEEFLFRTA LGILKLFEDI LTRMDFIHSA QFLTRLPEDL PADEVFAAIS
TVQMQSRNKK WAQVLSALQK DSREMEKGSP SLRH
