VPS51_BOVIN
ID VPS51_BOVIN Reviewed; 781 AA.
AC A6QQ47;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Vacuolar protein sorting-associated protein 51 homolog;
DE AltName: Full=Protein fat-free homolog;
GN Name=VPS51; Synonyms=FFR;
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=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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
CC protein retrieval from endosomes to the TGN, acid hydrolase sorting,
CC lysosome function, endosomal cholesterol traffic and autophagy. VPS51
CC participates in retrograde transport of acid hydrolase receptors,
CC likely by promoting tethering and SNARE-dependent fusion of endosome-
CC derived carriers to the TGN. Acts as component of the EARP complex that
CC is involved in endocytic recycling. The EARP complex associates with
CC Rab4-positive endosomes and promotes recycling of internalized
CC transferrin receptor (TFRC) to the plasma membrane.
CC {ECO:0000250|UniProtKB:Q9UID3}.
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 (By similarity). Component of the endosome-
CC associated retrograde protein (EARP) complex, composed of VPS51, VPS52,
CC VPS53 and VPS50/Syndetin (By similarity). EIPR1 interacts with both
CC EARP and GARP complexes and mediates the recruitment of the GARP
CC complex to the trans-Golgi network (By similarity). Interacts with STX6
CC (By similarity). Interacts with VPS50 and VPS54 in an EIPR1-independent
CC manner (By similarity). {ECO:0000250|UniProtKB:Q9UID3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9UID3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9UID3}. 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:Q9UID3}.
CC -!- SIMILARITY: Belongs to the VPS51 family. {ECO:0000305}.
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DR EMBL; BC149640; AAI49641.1; -; mRNA.
DR RefSeq; NP_001095563.1; NM_001102093.2.
DR AlphaFoldDB; A6QQ47; -.
DR STRING; 9913.ENSBTAP00000020600; -.
DR PaxDb; A6QQ47; -.
DR PRIDE; A6QQ47; -.
DR GeneID; 525567; -.
DR KEGG; bta:525567; -.
DR CTD; 738; -.
DR eggNOG; KOG2346; Eukaryota.
DR InParanoid; A6QQ47; -.
DR OrthoDB; 1305393at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
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:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR014812; Vps51.
DR PANTHER; PTHR15954; PTHR15954; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endosome; Golgi apparatus; Lipid transport; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..781
FT /note="Vacuolar protein sorting-associated protein 51
FT homolog"
FT /id="PRO_0000358912"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..146
FT /evidence="ECO:0000255"
FT COILED 269..291
FT /evidence="ECO:0000255"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UVL4"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UID3"
SQ SEQUENCE 781 AA; 85930 MW; A330B6D99C67FD30 CRC64;
MAAAAAAPGP GSGPGDSPEG PEAEGPERRR KAHGMLKLYY GLSEGEAAGR PSGPDPLDPT
DLNGAHFDPE VYLDKLRREC PLAQLMDSET DMVRQIRALD SDMQTLVYEN YNKFISATDT
IRKMKNDFRK MEDEMDRLAT NMAVITDFSA RISATLQDPH ERITKLAGVH ALLRKLQILF
ELPSRLTKCV ELGAYGQAVR YQGRARAVLQ QYQHLPSFRA IQDDCQVITA RLAQQLRQRF
REGGSGAPEQ AECVELLLAL GEPAEELCEE FLAHARGRLE EELRSLEAEL GPSPLAPDVL
EFTDHGGSGF VGGLCQVAAA YQELFAAQGP AGAEKLAAFA RELGSRYFAL VERRLAQEQG
SGDNSLLVRA LDRFHRRLRA PGALLAAAGL AEAATEIVER VARERLGHHL QGLQAAFLGS
LTDVRQALAA PRIAGKEGPG LAELLANVAS SILSHIKASL ASVHLFTAKE VSFSNKPYFR
GEFCSQGVRE SLIVGFIRSM CQTAQSFCDS PGEKGGATPP ALLLLLSRLC LDYETATISY
ILTLTDEQFL VQDQSPVTPV STLCAEARET ARRLLTHYVK VQGLVISQML RKSVETRDWL
STLEPRNVRA VMKRVVEDTT AIDVQVGLLY EEGVRKAQSS DSSKRTFSVY SSSRQQGRYA
PSYTPSAPMD TNLLSNIQKL FSERIDVFSP VEFNKVSVLT GIIKISLKTL LECVRLRTFG
RFGLQQVQVD CHFLQLYLWR FVADEELVHL LLDEVVASAA LRCPDPVPME PSVVEVICER
G
