TBC14_BOVIN
ID TBC14_BOVIN Reviewed; 692 AA.
AC A6H7I8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=TBC1 domain family member 14;
GN Name=TBC1D14;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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=AAI46263.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC146262; AAI46263.1; ALT_INIT; mRNA.
DR RefSeq; NP_001092646.1; NM_001099176.1.
DR RefSeq; XP_005208403.1; XM_005208346.3.
DR AlphaFoldDB; A6H7I8; -.
DR SMR; A6H7I8; -.
DR STRING; 9913.ENSBTAP00000039183; -.
DR PaxDb; A6H7I8; -.
DR PRIDE; A6H7I8; -.
DR Ensembl; ENSBTAT00000039389; ENSBTAP00000039183; ENSBTAG00000005493.
DR Ensembl; ENSBTAT00000073510; ENSBTAP00000067079; ENSBTAG00000005493.
DR GeneID; 618286; -.
DR KEGG; bta:618286; -.
DR CTD; 57533; -.
DR VEuPathDB; HostDB:ENSBTAG00000005493; -.
DR VGNC; VGNC:35628; TBC1D14.
DR eggNOG; KOG2223; Eukaryota.
DR GeneTree; ENSGT00940000157250; -.
DR HOGENOM; CLU_015133_1_1_1; -.
DR InParanoid; A6H7I8; -.
DR OMA; MANTAHD; -.
DR OrthoDB; 798837at2759; -.
DR TreeFam; TF313318; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000005493; Expressed in neutrophil and 104 other tissues.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0071955; P:recycling endosome to Golgi transport; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Golgi apparatus; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..692
FT /note="TBC1 domain family member 14"
FT /id="PRO_0000319417"
FT DOMAIN 400..610
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 270..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M4"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2M4"
SQ SEQUENCE 692 AA; 78025 MW; A7DDC78A3C09FF29 CRC64;
MTDGNLSTST NGVALMGILD SRPGNHIQNL QHLTLKAPRS LSLPEYGPKL KLSALEDRHS
LQSVDSGIPT LEIGNPEPVP CSVVHVRRKP SESEIVPERA CQSACLLPSY APPAPAGAER
EQSVRKSSTF PRTGYDSVKL YSPASQTLQR SDNVSVCSVS SLSTELSTTL SVSNEDILDL
VVTSSSSAIV TLENDDDPQF TDVTLSSTRE TRDLQRDCAG ETEEGRKLRL LGPFSHFFTR
NSLARKQNAR LDKQSDLGWK LFGKVPLGEN AQKDAKKLQK EYEDKAGRPS KPPSPKQNVR
KNLDFEPLST TALILEDRPA NLPAKPAEEA QKHRQQYEEM VVQAKKRELK EAQRRKKQLE
ERCRLEESIG NAVLTWNNEI LPNWETMWCS RKVRDLWWQG IPPSVRGKVW SLAIGNELNI
THELFDICLA RAKERWRSFS TGGSEAETED AGFSAADREA SLELIKLDIS RTFPSLCIFQ
QGGPYHDMLH SVLGAYTCYR PDVGYVQGMS FIAAVLILNL DTADAFIAFS NLLNKPCQMA
FFRVDHGLML TYFAAFEVFF EENLPKLFAH FKKNNLTPDI YLIDWIFTLY SKSLPLDLAC
RVWDVFCRDG EEFLFRTALG LLRLFQDVLT RMDFIHVAQF LTRLPEDLPA EEFFASIASI
QMQSRNKKWA QVLTALQKDS REMEKGSPSL RH