EIPR1_PONAB
ID EIPR1_PONAB Reviewed; 414 AA.
AC Q5RE10;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=EARP and GARP complex-interacting protein 1 {ECO:0000250|UniProtKB:Q53HC9};
DE AltName: Full=Endosome-associated recycling protein-interacting protein {ECO:0000250|UniProtKB:Q53HC9};
DE AltName: Full=Golgi-associated retrograde protein-interacting protein {ECO:0000250|UniProtKB:Q53HC9};
DE AltName: Full=Tumor-suppressing STF cDNA 1 protein;
DE AltName: Full=Tumor-suppressing subchromosomal transferable fragment candidate gene 1 protein {ECO:0000250|UniProtKB:Q53HC9};
GN Name=EIPR1 {ECO:0000250|UniProtKB:Q53HC9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a component of endosomal retrieval machinery that is
CC involved in protein transport from early endosomes to either recycling
CC endosomes or the trans-Golgi network (By similarity). Mediates the
CC recruitment of Golgi-associated retrograde protein (GARP) complex to
CC the trans-Golgi network and controls early endosome-to-Golgi transport
CC of internalized protein (By similarity). Promotes the recycling of
CC internalized transferrin receptor (TFRC) to the plasma membrane through
CC interaction with endosome-associated recycling protein (EARP) complex
CC (By similarity). Controls proper insulin distribution and secretion,
CC and retention of cargo in mature dense core vesicles (By similarity).
CC Required for the stability of the endosome-associated retrograde
CC protein (EARP) complex subunits and for proper localization and
CC association of EARP with membranes (By similarity).
CC {ECO:0000250|UniProtKB:Q53HC9, ECO:0000250|UniProtKB:Q5PPK9}.
CC -!- SUBUNIT: Interacts with two multisubunit tethering complexes: EARP
CC composed of VPS50, VPS51, VPS52 and VPS53 subunits and GARP complex
CC composed of VPS51, VPS52, VPS53 and VPS54 subunits. Interacts with
CC SNAP29. {ECO:0000250|UniProtKB:Q53HC9}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q53HC9}.
CC -!- SIMILARITY: Belongs to the WD repeat EIPR1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR857729; CAH89997.1; -; mRNA.
DR RefSeq; NP_001124947.1; NM_001131475.1.
DR AlphaFoldDB; Q5RE10; -.
DR SMR; Q5RE10; -.
DR STRING; 9601.ENSPPYP00000014159; -.
DR Ensembl; ENSPPYT00000014734; ENSPPYP00000014159; ENSPPYG00000012685.
DR GeneID; 100171819; -.
DR KEGG; pon:100171819; -.
DR CTD; 7260; -.
DR eggNOG; KOG1007; Eukaryota.
DR GeneTree; ENSGT00730000111137; -.
DR InParanoid; Q5RE10; -.
DR OrthoDB; 814890at2759; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:1990745; C:EARP complex; IEA:Ensembl.
DR GO; GO:0000938; C:GARP complex; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:1905281; P:positive regulation of retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR040323; EIPR1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR PANTHER; PTHR14205; PTHR14205; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Golgi apparatus; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..414
FT /note="EARP and GARP complex-interacting protein 1"
FT /id="PRO_0000051301"
FT REPEAT 159..199
FT /note="WD 1"
FT REPEAT 209..249
FT /note="WD 2"
FT REPEAT 253..293
FT /note="WD 3"
FT REPEAT 297..337
FT /note="WD 4"
FT REPEAT 372..412
FT /note="WD 5"
FT REGION 337..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53HC9"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HC9"
SQ SEQUENCE 414 AA; 46334 MW; 8850B0D6FCD38104 CRC64;
MEDDAPVIYG LEFQARALTP QTAETDAIRF LVGTQSLKYD NQIHIIDFDD ENNIINKNVL
LHQVGEIWHI SASPADRGVL ATCYNRTFCC VLSLDSFGAL GKSSAQLFIA LATSSDSKVL
TCAAVWRMPK ELESGSHESP DDSSSTAQTL ELLCHLDNTA HGNMACVVWE PMGDGKKIIS
LADNHILLWD LQESSSQAVL ASSASLEGKG QLKFTSGRWS PHHNCTQVAT ANDTTLRGWD
TRSMSQIYCI ENAHGQLVRD LDFNPNKQYY LASCGDDCKV KFWDTRNVTE PVKTLEEHSH
WVWNVRYNHS HDQLVLTGSS DSRVILSNMV SISSEPFGHL VDDDDISDQE DHRSEEKSKE
PLQDNVIATY EEHEDSVYAV DWSSADPWLF ASLSYDGRLV INRVPRALKY HILL