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VPS52_CANLF
ID   VPS52_CANLF             Reviewed;         723 AA.
AC   Q5TJF0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Vacuolar protein sorting-associated protein 52 homolog;
GN   Name=VPS52;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Doberman pinscher;
RX   PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA   Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA   Ollier W.E.R., Binns M.M.;
RT   "Genomic sequence of the class II region of the canine MHC: comparison with
RT   the MHC of other mammalian species.";
RL   Genomics 85:48-59(2005).
CC   -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC       retrograde transport from early and late endosomes to the trans-Golgi
CC       network (TGN). The GARP complex is required for the maintenance of the
CC       cycling of mannose 6-phosphate receptors between the TGN and endosomes,
CC       this cycling is necessary for proper lysosomal sorting of acid
CC       hydrolases such as CTSD. Acts as component of the EARP complex that is
CC       involved in endocytic recycling. The EARP complex associates with Rab4-
CC       positive endosomes and promotes recycling of internalized transferrin
CC       receptor (TFRC) to the plasma membrane. {ECO:0000250|UniProtKB:Q8N1B4}.
CC   -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC       complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC       VPS52, VPS53 and VPS54. Component of the endosome-associated retrograde
CC       protein (EARP) complex, composed of VPS51, VPS52, VPS53 and
CC       VPS50/Syndetin. EIPR1 interacts with both EARP and GARP complexes and
CC       mediates the recruitment of the GARP complex to the trans-Golgi
CC       network. Interacts with RAB6A and STX10. Interacts with UHRF1BP1L.
CC       {ECO:0000250|UniProtKB:Q8N1B4}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8N1B4}. Endosome membrane
CC       {ECO:0000250|UniProtKB:Q8N1B4}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q8N1B4}. Recycling endosome
CC       {ECO:0000250|UniProtKB:Q8N1B4}. Note=Localizes to the trans-Golgi
CC       network as part of the GARP complex, while it localizes to recycling
CC       endosomes as part of the EARP complex. {ECO:0000250|UniProtKB:Q8N1B4}.
CC   -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
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DR   EMBL; AJ630366; CAI11438.1; -; Genomic_DNA.
DR   RefSeq; NP_001041553.1; NM_001048088.1.
DR   AlphaFoldDB; Q5TJF0; -.
DR   STRING; 9612.ENSCAFP00000001355; -.
DR   PaxDb; Q5TJF0; -.
DR   Ensembl; ENSCAFT00030024657; ENSCAFP00030021529; ENSCAFG00030013308.
DR   Ensembl; ENSCAFT00040038554; ENSCAFP00040033627; ENSCAFG00040020822.
DR   Ensembl; ENSCAFT00845036564; ENSCAFP00845028611; ENSCAFG00845020730.
DR   GeneID; 474871; -.
DR   KEGG; cfa:474871; -.
DR   CTD; 6293; -.
DR   VEuPathDB; HostDB:ENSCAFG00845020730; -.
DR   eggNOG; KOG1961; Eukaryota.
DR   GeneTree; ENSGT00390000008815; -.
DR   HOGENOM; CLU_010797_0_0_1; -.
DR   InParanoid; Q5TJF0; -.
DR   OMA; IHVVMVE; -.
DR   OrthoDB; 158568at2759; -.
DR   TreeFam; TF314937; -.
DR   Reactome; R-CFA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Proteomes; UP000002254; Chromosome 12.
DR   Bgee; ENSCAFG00000000941; Expressed in granulocyte and 47 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000938; C:GARP complex; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0007041; P:lysosomal transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   InterPro; IPR007258; Vps52.
DR   PANTHER; PTHR14190; PTHR14190; 1.
DR   Pfam; PF04129; Vps52; 1.
PE   3: Inferred from homology;
KW   Acetylation; Coiled coil; Endosome; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1B4"
FT   CHAIN           2..723
FT                   /note="Vacuolar protein sorting-associated protein 52
FT                   homolog"
FT                   /id="PRO_0000213314"
FT   REGION          21..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          107..127
FT                   /evidence="ECO:0000255"
FT   COILED          194..215
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1B4"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N1B4"
SQ   SEQUENCE   723 AA;  82238 MW;  68783D7623EFB52D CRC64;
     MAAAATMAAA ARELLLRAGT SDMEEEEGPL GGGPGLQEPL PLGELDISSD EFILDEVDVH
     IQANLEDELV KEALKTGVDL RHYSKQVELE LQQIEQKSIR DYIQESENIA SLHNQITACD
     AVLERMEQML GAFQSDLSSI SSEIRTLQEQ SGAMNIRLRN RQAVRGKLGE LVDGLIVPSA
     LIMAILEAPV TEPRFLEQLQ ELDAKAAAVR EQEARGTAAC ADVRGILDRL RVKAVTKIRE
     FILQKIYSFR KPMTNYQIPQ TALLKYRFFY QFLLGNERAT AKEIRDEYVE TLSKIYLSYY
     RSYLGRLMKV QYEEVAEKDD LMGVEDTAKK GFFSKPSLRS RNTIFTLGTR GSVISPTELE
     APILVPHTAQ RGEQRYPFEA LFRSQHYALL DNSCREYLFI CEFFVVSGSA AHDLFHAVMG
     RTLGMTLKHL ESYLTDCYDA IAVFLCIHIV LRFRNIAAKR DVPALDRYWE QVLALLWPRF
     ELILEMNVQS VRSTDPQRLG GLDTRPHYIT RRYAEFSSAL VSINQTVPNE RTMQLLGQLQ
     VEVENFVLRV AAEFSSRKEQ LVFLINNYDM MLGVLMERAA DDSKEVESFQ QLLNARTQEF
     IEELLSPPFG GLVAFVKEAE ALIERGQAER LRGEEARVTQ LIRGFGSSWK SSVESLSQDV
     MRSFTNFRNG TSIIQGALTQ LIQLYHRFHR VLSQPQLRAL PARAELINIH HLMVELKKHK
     PNF
 
 
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