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VPS52_RAT
ID   VPS52_RAT               Reviewed;         723 AA.
AC   O55166;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Vacuolar protein sorting-associated protein 52 homolog;
DE   AltName: Full=SAC2 suppressor of actin mutations 2-like protein;
GN   Name=Vps52; Synonyms=Are1, Sacm2l;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LEW.1W/GUN;
RX   PubMed=9790748; DOI=10.1006/geno.1998.5463;
RA   Walter L., Guenther E.;
RT   "Identification of a novel highly conserved gene in the centromeric part of
RT   the major histocompatibility complex.";
RL   Genomics 52:298-304(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
RN   [3]
RP   INTERACTION WITH EIPR1.
RX   PubMed=27440922; DOI=10.1091/mbc.e16-04-0209;
RA   Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
RT   "TSSC1 is novel component of the endosomal retrieval machinery.";
RL   Mol. Biol. Cell 27:2867-2878(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). 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 (By similarity). The EARP complex interacts with EIPR1
CC       (PubMed:27440922). EIPR1 interacts with GARP complex and mediates its
CC       recruitment to the trans-Golgi network. Interacts with RAB6A and STX10.
CC       Interacts with UHRF1BP1L (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N1B4, ECO:0000269|PubMed:27440922}.
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   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15060004}.
CC   -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
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DR   EMBL; AJ223830; CAA11566.1; -; mRNA.
DR   EMBL; BX883042; CAE83926.1; -; Genomic_DNA.
DR   RefSeq; NP_149088.1; NM_033097.2.
DR   AlphaFoldDB; O55166; -.
DR   BioGRID; 247260; 2.
DR   DIP; DIP-61630N; -.
DR   IntAct; O55166; 1.
DR   STRING; 10116.ENSRNOP00000000549; -.
DR   jPOST; O55166; -.
DR   PaxDb; O55166; -.
DR   PRIDE; O55166; -.
DR   Ensembl; ENSRNOT00000000549; ENSRNOP00000000549; ENSRNOG00000000470.
DR   GeneID; 25218; -.
DR   KEGG; rno:25218; -.
DR   UCSC; RGD:3618; rat.
DR   CTD; 6293; -.
DR   RGD; 3618; Vps52.
DR   eggNOG; KOG1961; Eukaryota.
DR   GeneTree; ENSGT00390000008815; -.
DR   HOGENOM; CLU_010797_0_0_1; -.
DR   InParanoid; O55166; -.
DR   OMA; IHVVMVE; -.
DR   OrthoDB; 158568at2759; -.
DR   PhylomeDB; O55166; -.
DR   TreeFam; TF314937; -.
DR   Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   PRO; PR:O55166; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000470; Expressed in frontal cortex and 20 other tissues.
DR   ExpressionAtlas; O55166; baseline and differential.
DR   Genevisible; O55166; RN.
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; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR   GO; GO:0010668; P:ectodermal cell differentiation; ISO:RGD.
DR   GO; GO:0048611; P:embryonic ectodermal digestive tract development; ISO:RGD.
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; ISO:RGD.
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   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_0000213317"
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;  82103 MW;  1346002ADF55A839 CRC64;
     MAAAATMAAA ARELVLRAGA SDMEEEEGPL GAGSGLQEPL QLGELDITSD EFILDEVDVH
     IQANLEDELV KEALKTGVDL RHYSKQVELE LQQIEQKSIR DYIQESENIA SLHNQITACD
     AVLERMEQML GAFQSDLSSI SCEIRTLQEQ SGAMNIRLRN RQAVRGKLGE LVDGLVVPSA
     LVTAILEAPV TEPRFLEQLQ ELDAKAAAVR EQEARGTAAC ADVRGVLDRL RVKAVTKIRE
     FILQKIYSFR KPMTNYQIPQ TALLKYRFFY QFLLGNERAT AKEVRDEYVE TLSKIYLSYY
     RSYVGRLMKV QYEEVAEKDD LMGVEDTAKK GFFSKPSLRS RNTIFTLGTR GAVISPAELE
     APILVPHTAQ RGEQRYPFEA LFRSQHYALL DNSCREYLFI CEFFVVSGPA AHDLFHAVMG
     RTLSMTLKHL ESYLADCYDA IAVFLCIHIV LRFRNIAAKR DVPALDRYWE QVLALLWPRF
     ELILEMNVQS VRSTDPQRLG GLDTRPHYIT RRYAEFSSAL VSINQTIPNE RTLQLLGQLQ
     VEVENFVLRV AAEFSSRKEQ LVFLINNYDM MLGVLMERAA DDSKEVESFQ QLLNARTQEF
     IEELLSPPFG GLVAFVKEAE ALIERGQAER LRGEEARVTQ LIRGFGSSWK ASVESLSQDV
     MRSFTNFRNG TSIIQGALTQ LIQLYHRFHR VLSQPQLRAL PARAELINIH HLMVELKKHK
     PNF
 
 
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