VPS51_CAEEL
ID VPS51_CAEEL Reviewed; 700 AA.
AC O01839;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE AltName: Full=Protein fat-free homolog;
GN Name=vps-51 {ECO:0000312|WormBase:B0414.8a};
GN ORFNames=B0414.8 {ECO:0000312|WormBase:B0414.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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 [2]
RP FUNCTION, IDENTIFICATION IN THE GARP COMPLEX, INTERACTION WITH VPS-53,
RP SUBCELLULAR LOCATION, 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 [3]
RP FUNCTION, AND DISRUPTION 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
CC (PubMed:21613545). {ECO:0000269|PubMed:21613545}.
CC -!- INTERACTION:
CC O01839; G5EFV8: vps-52; NbExp=6; IntAct=EBI-313277, EBI-318981;
CC O01839; P34561: vps-53; NbExp=2; IntAct=EBI-313277, EBI-6394890;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:21613545}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with particularly strong
CC expression in neuronal cells. {ECO:0000269|PubMed:21613545}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable but have enlarged lysosomes
CC (PubMed:21613545). Egg-laying defect, slow, but coordinated locomotion,
CC and reduced levels of unprocessed and processed cargo in the motor
CC neuron axon of the dorsal nerve cord (PubMed:27191843).
CC {ECO:0000269|PubMed:21613545, ECO:0000269|PubMed:27191843}.
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD61903.1; -; Genomic_DNA.
DR PIR; T15234; T15234.
DR RefSeq; NP_001020972.1; NM_001025801.3.
DR AlphaFoldDB; O01839; -.
DR SMR; O01839; -.
DR BioGRID; 37702; 17.
DR ComplexPortal; CPX-365; GARP complex.
DR DIP; DIP-26647N; -.
DR IntAct; O01839; 13.
DR MINT; O01839; -.
DR STRING; 6239.B0414.8a; -.
DR EPD; O01839; -.
DR PaxDb; O01839; -.
DR PeptideAtlas; O01839; -.
DR EnsemblMetazoa; B0414.8a.1; B0414.8a.1; WBGene00015176.
DR GeneID; 172247; -.
DR KEGG; cel:CELE_B0414.8; -.
DR UCSC; B0414.8b; c. elegans.
DR CTD; 172247; -.
DR WormBase; B0414.8a; CE30413; WBGene00015176; vps-51.
DR eggNOG; KOG2346; Eukaryota.
DR GeneTree; ENSGT00390000001738; -.
DR HOGENOM; CLU_020677_0_0_1; -.
DR InParanoid; O01839; -.
DR OMA; HTIEPRT; -.
DR OrthoDB; 1305393at2759; -.
DR PhylomeDB; O01839; -.
DR PRO; PR:O01839; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00015176; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O01839; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990745; C:EARP complex; IBA:GO_Central.
DR GO; GO:0000938; C:GARP complex; IPI:WormBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:WormBase.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle 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:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Reference proteome.
FT CHAIN 1..700
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000361543"
FT COILED 61..87
FT /evidence="ECO:0000255"
FT COILED 345..380
FT /evidence="ECO:0000255"
SQ SEQUENCE 700 AA; 78773 MW; 9BD7F172C2E2884B CRC64;
MSSVLDVTKP DFDVEAFVVK LLREKSLDGL VKEEEEMVSA VRRLDSDVHQ IVYENYNKFL
TATNTVRKIQ DEFTQLDSEM KSLSRSMSTI STLIGNLDGV LGEKRDDILQ LGSSYKVVNS
LKHIFDLPHV LRSEFDERNY GEVLRMFKLA EESLSQYKDV PTVQLVLQKS KKIYDMTENQ
LMDQLRNPAS GAELVSEAVD LLLTIGRDED EVQKVLLTCS EQSLRVDLKE LSANHSDVLD
LVDKASESFI PNLTLIATTH DRLFEDKRED LITVLKTEMN SLHALVSKVF LSSSDAKDCS
IVVRALDRYF RKISTCRYVI PGLDFLPLTI ELINAVSKHE IDLSLTRIKE ELKNGLNEVR
KALINEEKDL SALASKIEQV FVHQVKTALA NLLLFTASDV TFANLPPDEF RQSFSFNAHE
RLLVQAFHRF SELADEYESG AGEIRFVDPR VHLVFAVALQ HLSNKSAVYL LNLCREQFSL
SPDDGLTDIT VVMSEVKTRA QKLVRCYAEK TGLSMGETLI KGCAMLVQPA ATPSAVRASV
RRLVEEMNTC DSELTLLLGG DSKPKDSRVS RRPITTALDA ARDSLWCERI DFHLQIHFNR
ASIITVIVKV VLKIFIESIR LQTYSKFGVE QVQVDCYYLQ RCLAALVSDE VVVNSMVDQA
LSSALKRCQD PVLVHPSRLA QLCEQPPANR PSSQASSLGY
