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VPS52_CAEEL
ID   VPS52_CAEEL             Reviewed;         702 AA.
AC   G5EFV8; G5EFV9;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Vacuolar protein sorting-associated protein 52 homolog {ECO:0000250|UniProtKB:O01839, ECO:0000303|PubMed:21613545};
GN   Name=vps-52 {ECO:0000312|WormBase:F08C6.3};
GN   Synonyms=tag-197 {ECO:0000312|WormBase:F08C6.3}; ORFNames=F08C6.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADO17797.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE GARP COMPLEX,
RP   INTERACTION WITH VPS-53; VPS-54; RAB-6.1 AND RAB-6.2, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=21613545; DOI=10.1091/mbc.e10-06-0493;
RA   Luo L., Hannemann M., Koenig S., Hegermann J., Ailion M., Cho M.K.,
RA   Sasidharan N., Zweckstetter M., Rensing S.A., Eimer S.;
RT   "The Caenorhabditis elegans GARP complex contains the conserved Vps51
RT   subunit and is required to maintain lysosomal morphology.";
RL   Mol. Biol. Cell 22:2564-2578(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=27191843; DOI=10.1371/journal.pgen.1006074;
RA   Topalidou I., Cattin-Ortola J., Pappas A.L., Cooper K., Merrihew G.E.,
RA   MacCoss M.J., Ailion M.;
RT   "The EARP complex and its interactor eipr-1 are required for cargo sorting
RT   to dense-core vesicles.";
RL   PLoS Genet. 12:E1006074-E1006074(2016).
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) (PubMed:21613545). The GARP complex facilitates tethering
CC       as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays
CC       a role in the trafficking of cargo to dense-core vesicles, probably
CC       through association with the EARP-interacting protein eipr-1
CC       (PubMed:27191843). Important for neuronal function (PubMed:27191843).
CC       {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
CC   -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC       complex, also called VFT (VPS fifty-three) complex, composed of vps-51,
CC       vps-52, vps-53 and vps-54. Within the complex interacts with vps-53 and
CC       vps-54 (PubMed:21613545). Interacts with the small GTPases rab-6.1 and
CC       rab-6.2 (PubMed:21613545). {ECO:0000269|PubMed:21613545}.
CC   -!- INTERACTION:
CC       G5EFV8; O01839: vps-51; NbExp=6; IntAct=EBI-318981, EBI-313277;
CC       G5EFV8; P34561: vps-53; NbExp=3; IntAct=EBI-318981, EBI-6394890;
CC       G5EFV8; Q22639: vps-54; NbExp=5; IntAct=EBI-318981, EBI-6395200;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000269|PubMed:21613545}. Perikaryon
CC       {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to
CC       perinuclear puncta in the perikaryon. Co-localizes with the small
CC       GTPases rab-6.1 and rab-6.2 at Golgi structures (PubMed:21613545).
CC       {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with particularly strong
CC       expression in neuronal cells (PubMed:21613545). Specifically expressed
CC       in head and tail neurons and in the pharynx and ventral cord motor
CC       neurons (PubMed:27191843). {ECO:0000269|PubMed:21613545,
CC       ECO:0000269|PubMed:27191843}.
CC   -!- DISRUPTION PHENOTYPE: Enlarged lysosomes (PubMed:21613545). Reduced
CC       brood size (PubMed:21613545). Egg-laying defect, slow, but coordinated
CC       locomotion, and reduced levels of unprocessed and processed cargo in
CC       the motor neuron axon of the dorsal nerve cord (PubMed:27191843).
CC       {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
CC   -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000255}.
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DR   EMBL; HQ237455; ADO17797.1; -; mRNA.
DR   EMBL; BX284606; CCD67346.2; -; Genomic_DNA.
DR   RefSeq; NP_509282.4; NM_076881.6.
DR   AlphaFoldDB; G5EFV8; -.
DR   SMR; G5EFV8; -.
DR   BioGRID; 45942; 19.
DR   ComplexPortal; CPX-365; GARP complex.
DR   IntAct; G5EFV8; 18.
DR   STRING; 6239.F08C6.3; -.
DR   EPD; G5EFV8; -.
DR   PaxDb; G5EFV8; -.
DR   PeptideAtlas; G5EFV8; -.
DR   EnsemblMetazoa; F08C6.3.1; F08C6.3.1; WBGene00007059.
DR   GeneID; 181018; -.
DR   KEGG; cel:CELE_F08C6.3; -.
DR   CTD; 181018; -.
DR   WormBase; F08C6.3; CE47824; WBGene00007059; vps-52.
DR   eggNOG; KOG1961; Eukaryota.
DR   GeneTree; ENSGT00390000008815; -.
DR   HOGENOM; CLU_010797_0_0_1; -.
DR   InParanoid; G5EFV8; -.
DR   OMA; IHVVMVE; -.
DR   OrthoDB; 158568at2759; -.
DR   PhylomeDB; G5EFV8; -.
DR   SignaLink; G5EFV8; -.
DR   PRO; PR:G5EFV8; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00007059; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0000938; C:GARP complex; IPI:WormBase.
DR   GO; GO:0005797; C:Golgi medial cisterna; IDA:WormBase.
DR   GO; GO:0000138; C:Golgi trans cisterna; IDA:WormBase.
DR   GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR   GO; GO:0019905; F:syntaxin binding; IPI:WormBase.
DR   GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
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:1904810; P:negative regulation of dense core granule transport; IMP:UniProtKB.
DR   GO; GO:1904811; P:positive regulation of dense core granule transport; IMP:UniProtKB.
DR   GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Golgi apparatus; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..702
FT                   /note="Vacuolar protein sorting-associated protein 52
FT                   homolog"
FT                   /id="PRO_0000421176"
FT   COILED          505..535
FT                   /evidence="ECO:0000255"
FT   CONFLICT        342
FT                   /note="A -> V (in Ref. 1; ADO17797)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   702 AA;  80708 MW;  ED057C30BA432C75 CRC64;
     MPRTRVNLQK SEANDRSFTI SSLEFCLSQL RKADPNLVKK AIASGDGLTE SKNDVSTRLS
     EAHRYSVQQC LDNSEQLAQL HNQLVHCDNV FERLQATLYS FQDNLGSIGQ DMKNLQLQSH
     HIHQELENRQ KVRVELSQFV DDIAVSQTMM KTINDTDAND RGFLEALHEL HHKITLILQR
     GNGDAVAVND TMPILEGLKL KAVVKVREWL LQKMFQFRKP LSNYQVFQHQ LLKCRFFYEF
     LLHHDLISAK ELQDEYIDTI SKMFFTYFKA YATRLFKLAM KDVATKEDAL GSIDFAKPAG
     LGAIFSSKQH VVRNKATVFS IGQRHQILSD DFLGALIVPH AATQNHQSYQ FEALFRSIQL
     AFVDHYSHEY LFITDFFLVS NDEAIELHNK AMARAMSVVL KSCEEQIALS WDAISLHLCI
     CLCDKFTEVL AEREVPEVSD YWNTVTSFLW TRLNLVMSQH YESVKSVDLK KLMHSGSLDA
     RPHFIVRRYA ELTSAHLMIA KASGKEMGAK MEAVLENSED SIEQLLTRMS AMQQTQKNKH
     VFLINNYDLI LSIIDNEESK HTKIYAIVHE LEQKSIDDFV EEMLEPHIGY MIKFVNECES
     LIVQGHTQLL VRYNDKVGTV VANFNAKWRP AVDSINSECI QLFTNFSLGT TILQTIFTKY
     VQYINRFTKI LSHDVFAKNP VCSQLVNVHQ VMLEIKRFKP AY
 
 
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