TBC12_RAT
ID TBC12_RAT Reviewed; 693 AA.
AC M0R7T9;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=TBC1 domain family member 12;
GN Name=Tbc1d12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28384198; DOI=10.1371/journal.pone.0174883;
RA Oguchi M.E., Noguchi K., Fukuda M.;
RT "TBC1D12 is a novel Rab11-binding protein that modulates neurite outgrowth
RT of PC12 cells.";
RL PLoS ONE 12:E0174883-E0174883(2017).
CC -!- FUNCTION: RAB11A-binding protein that plays a role in neurite
CC outgrowth. {ECO:0000269|PubMed:28384198}.
CC -!- SUBUNIT: Interacts with RAB11A; this interaction recruits TBC1D12 to
CC RAB11A-positive recycling endosomes. {ECO:0000250|UniProtKB:O60347}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:O60347}.
CC -!- DISRUPTION PHENOTYPE: Knock-down promotes neurite outgrowth in a
CC RAB11A-dependent manner. {ECO:0000269|PubMed:28384198}.
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DR EMBL; AABR07006771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07006778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07072049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003753443.1; XM_003753395.4.
DR RefSeq; XP_008758607.1; XM_008760385.2.
DR AlphaFoldDB; M0R7T9; -.
DR SMR; M0R7T9; -.
DR STRING; 10116.ENSRNOP00000065523; -.
DR PaxDb; M0R7T9; -.
DR PRIDE; M0R7T9; -.
DR Ensembl; ENSRNOT00000078738; ENSRNOP00000070589; ENSRNOG00000036598.
DR GeneID; 685933; -.
DR CTD; 23232; -.
DR RGD; 1587841; LOC685933.
DR RGD; 9377071; Tbc1d12.
DR eggNOG; KOG2223; Eukaryota.
DR GeneTree; ENSGT00940000156410; -.
DR InParanoid; M0R7T9; -.
DR OMA; GQSARDH; -.
DR OrthoDB; 798837at2759; -.
DR PRO; PR:M0R7T9; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000036598; Expressed in cerebellum and 18 other tissues.
DR ExpressionAtlas; M0R7T9; baseline and differential.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
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:2000785; P:regulation of autophagosome assembly; IBA:GO_Central.
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 3: Inferred from homology;
KW Acetylation; Coiled coil; Endosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..693
FT /note="TBC1 domain family member 12"
FT /id="PRO_0000448234"
FT DOMAIN 402..610
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60347"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6A039"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60347"
SQ SEQUENCE 693 AA; 76674 MW; 6607C4A1B7CE7A3B CRC64;
MMGPEDAGAC SGRNAELLPV PGPMGQDGKT VPATGGFSGG AVAAEPPGEA GEEEAPPPRQ
LLQRYLAAAA GPLQPGLGGV EAEAAAVPAA RGSGMTNGDS GFLLLQDRRG PEEARRRRTC
GRPCLAEPAD EGVDGAGGLD DWAAPLEDPL RSCCLAAGDT DDPDPTATTS AGRDVGSAES
SLGLPDARFG SRNTFEVSRR QSAGDLLPSA GQSAPLPAAE QGPGGTTVRA RRSGGFADFF
ARNLFPKRTK ELKSVVHSAP GWKLFGKVPP RENLQKTSKI IQQEYEARTG RTCKVPPQSS
RRKNFEFEPL STTALILEDR PSNLPAKSVE EALRHRQEYD EMVAEAKKRE IKEAHKRKRI
MKERFKQEES IASAMVIWIN EILPNWEVMR STRRVRELWW QGLPPSVRGK VWSLAVGNEL
NITPELYEIF LSRAKERWKS FSESSSDSDM EGLSVADREA SLELIKLDIS RTFPSLYIFQ
KGGPYHDVLH SILGAYTCYR PDVGYVQGMS FIAAVLILNL EEADAFIAFA NLLNRPCQLA
FFRVDHSMML KYFATFEVFF EENLSKLFLH FKSYNLTPDI YLIDWIFTLY SKSLPLDLAC
RVWDVFCRDG EEFLFRTGLG ILRLYEDILL QMDFIHIAQF LTKLPEDITS EKLFSCIAAI
QMQNSTKKWT QVFASVTKDI KEGDKNNSPA LKS
