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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};
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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
 
 
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