VPS51_DANRE
ID VPS51_DANRE Reviewed; 827 AA.
AC Q155U0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE AltName: Full=Protein fat-free;
GN Name=vps51; Synonyms=ffr;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16581006; DOI=10.1016/j.cmet.2006.03.001;
RA Ho S.-Y., Lorent K., Pack M., Farber S.A.;
RT "Zebrafish fat-free is required for intestinal lipid absorption and Golgi
RT apparatus structure.";
RL Cell Metab. 3:289-300(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in retrograde transport from early and late
CC endosomes to the late Golgi. The GARP complex is required for the
CC maintenance of protein retrieval from endosomes to the TGN, acid
CC hydrolase sorting, lysosome function, endosomal cholesterol traffic and
CC autophagy (PubMed:16581006). Acts as component of the EARP complex that
CC is involved in endocytic recycling (By similarity).
CC {ECO:0000250|UniProtKB:Q9UID3, ECO:0000269|PubMed:16581006}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex Component of the endosome-associated retrograde protein (EARP)
CC complex. {ECO:0000250|UniProtKB:Q9UID3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:16581006}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9UID3}. Note=Also localizes in perinuclear
CC region (PubMed:16581006). Localizes to the trans-Golgi network as part
CC of the GARP complex, while it localizes to recycling endosomes as part
CC of the EARP complex (By similarity). {ECO:0000250|UniProtKB:Q9UID3,
CC ECO:0000269|PubMed:16581006}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult.
CC {ECO:0000269|PubMed:16581006}.
CC -!- DISRUPTION PHENOTYPE: Larvae are morphologically indistinguishable from
CC wild-type sibling larvae, but their absorption of lipids is severely
CC impaired. {ECO:0000269|PubMed:16581006}.
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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DR EMBL; DQ641948; ABG23689.1; -; mRNA.
DR EMBL; BC162801; AAI62801.1; -; mRNA.
DR EMBL; BC162802; AAI62802.1; -; mRNA.
DR RefSeq; NP_001036200.1; NM_001042735.1.
DR AlphaFoldDB; Q155U0; -.
DR SMR; Q155U0; -.
DR STRING; 7955.ENSDARP00000083577; -.
DR PaxDb; Q155U0; -.
DR Ensembl; ENSDART00000188688; ENSDARP00000156118; ENSDARG00000110076.
DR GeneID; 559339; -.
DR KEGG; dre:559339; -.
DR CTD; 738; -.
DR ZFIN; ZDB-GENE-030131-6008; vps51.
DR eggNOG; KOG2346; Eukaryota.
DR InParanoid; Q155U0; -.
DR OrthoDB; 1305393at2759; -.
DR PhylomeDB; Q155U0; -.
DR PRO; PR:Q155U0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000110076; Expressed in multicellular organism.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:1990745; C:EARP complex; ISS:UniProtKB.
DR GO; GO:0000938; C:GARP complex; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:ZFIN.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:ZFIN.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:ZFIN.
DR GO; GO:0044241; P:lipid digestion; IMP:ZFIN.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0007041; P:lysosomal transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010517; P:regulation of phospholipase activity; IMP:ZFIN.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
DR Pfam; PF15469; Sec5; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Golgi apparatus; Lipid transport; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..827
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000361540"
FT REGION 279..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..131
FT /evidence="ECO:0000255"
FT COILED 254..278
FT /evidence="ECO:0000255"
FT COMPBIAS 281..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 92316 MW; 4F49EC87721A801D CRC64;
MSSATTPPDS DPAQRRRVHS MLKLYYGLNE EGKATEQAES LDPCDINGPH FDPEIYLNKL
RKECSLTELM DHESCMVKQI RSLDSDMQTL VYENYNKFIS ATDTIRKMKN DFKKMEDEMD
CLSANMAAIT EFSARISGTL QDQHAQITKL SGVHTLLRKL QFLFELPARL NKCLELQAYA
QAVSSHRRAR CVLQQYSHMP SFRGIQDDCH VIMEQLAQQL RQKFRDGGSS AKDLSECVEL
LLQLDEPAEE LCDKFLSHAQ SRLEADLQGL EAELKDSAVT DTGAGSVQKT SPGSNPVSPS
SSVSNPFLSP AAGTDILEFI DRGCNEFVSN LCLVIASYQE LFINRPQESE LASKNIPEMA
NGKLHVFVDT LAARYFSLVE RRIQEEKGVG DNSLLVRALD RFHRRLQAIS KLLPGSAVPS
QGTEIVVRAA RERIKQYLSA LQTFYHDSLT DVRQALAAPR LSVGGASASG GGALVGGASS
KDAPPSLPEL LTSLSNFILN QLKSVLASVH LFTAKDITFS NKPYFKGEFC SQGVREGLVV
SFIKFICQSS RQYCESAGDR GGSTPPALLL LLSRLCLDYE TSTISYILTL TDEQFLVQHH
TPVTPVTALC AEAREAAQKL LNHYVKVQGL IISQMLRKSV ETRDWVNTIE PRNVRAVMKR
VVEDTTSIDV QVGLLYEEGV RKAHSSDSSK RTFSVYSSSR QQIRYAPSYT PSAPMDTNLL
SNIHKLFSER IDIFSPVEFN KVSVLTGIIK ISLKTFLECV RLRTFGRYGL QQIQVDCHYL
QMYLWRFVSD ENLVHFLLDE IVGSAAHRCL DPSPMEQSVI EVICERG
