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 10-JUN-2026, entry version 103. 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_005208346.5. DR RefSeq; XP_024849207.1; XM_024993439.2. DR AlphaFoldDB; A6H7I8; -. DR SMR; A6H7I8; -. DR FunCoup; A6H7I8; 1345. DR STRING; 9913.ENSBTAP00000067079; -. DR PaxDb; 9913-ENSBTAP00000067079; -. DR Ensembl; ENSBTAT00000142216.1; ENSBTAP00000105864.1; ENSBTAG00000005493.8. DR Ensembl; ENSBTAT00090037945; ENSBTAP00090019435; ENSBTAG00090018707. 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; NTEREHR; -. DR OrthoDB; 294251at2759; -. DR Reactome; R-BTA-8854214; TBC/RABGAPs. DR Proteomes; UP000009136; Chromosome 6. DR Bgee; ENSBTAG00000005493; Expressed in neutrophil and 104 other cell types or tissues. DR ExpressionAtlas; A6H7I8; baseline. DR GO; GO:0005776; C:autophagosome; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IEA:UniProtKB-ARBA. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:2000785; P:regulation of autophagosome assembly; IBA:GO_Central. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-ARBA. DR FunFam; 1.10.8.270:FF:000008; Putative TBC1 domain family member 14; 1. DR FunFam; 1.10.10.750:FF:000005; TBC1 domain family member 14; 1. DR FunFam; 1.10.472.80:FF:000006; TBC1 domain family member 14; 1. DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1. DR Gene3D; 1.10.10.750; Ypt/Rab-GAP domain of gyp1p, domain 1; 1. DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1. DR InterPro; IPR000195; Rab-GAP-TBC_dom. DR InterPro; IPR035969; Rab-GAP_TBC_sf. DR InterPro; IPR050302; Rab_GAP_TBC_domain. DR PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1. DR PANTHER; PTHR47219:SF21; TBC1 DOMAIN FAMILY MEMBER 14; 1. DR Pfam; PF00566; RabGAP-TBC; 1. DR SMART; SM00164; TBC; 1. DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 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 271..287 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..335 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 //