EIPR1_RAT
ID EIPR1_RAT Reviewed; 386 AA.
AC Q5PPK9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=EARP and GARP complex-interacting protein 1 {ECO:0000250|UniProtKB:Q53HC9};
DE AltName: Full=Endosome-associated recycling protein-interacting protein {ECO:0000303|PubMed:27191843};
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:0000303|PubMed:27191843, ECO:0000312|RGD:1305817};
GN Synonyms=Tssc1 {ECO:0000312|RGD:1305817};
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INTERACTION WITH EARP COMPLEX, AND TISSUE SPECIFICITY.
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).
RN [3]
RP INTERACTION WITH VPS50; VPS51 AND SNAP29.
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).
RN [4]
RP FUNCTION.
RX PubMed=3172165; DOI=10.3109/03091908809030166;
RA Topalidou I., Cattin-Ortola J., Hummer B., Asensio C.S., Ailion M.;
RT "EIPR1 controls dense-core vesicle cargo retention and EARP complex
RT localization in insulin-secreting cells.";
RL Mol. Biol. Cell 31:59-79(2020).
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 (PubMed:3172165).
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 (PubMed:3172165).
CC {ECO:0000250|UniProtKB:Q53HC9, ECO:0000269|PubMed:3172165}.
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 (PubMed:27440922,
CC PubMed:27191843). Interacts with SNAP29 (PubMed:27191843).
CC {ECO:0000269|PubMed:27191843, ECO:0000269|PubMed:27440922}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q53HC9}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, adipose
CC tissue, spleen and kidney (at protein level).
CC {ECO:0000269|PubMed:27440922}.
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; BC087633; AAH87633.1; -; mRNA.
DR RefSeq; NP_001012192.1; NM_001012192.1.
DR AlphaFoldDB; Q5PPK9; -.
DR SMR; Q5PPK9; -.
DR BioGRID; 263666; 4.
DR STRING; 10116.ENSRNOP00000056930; -.
DR iPTMnet; Q5PPK9; -.
DR PhosphoSitePlus; Q5PPK9; -.
DR jPOST; Q5PPK9; -.
DR PaxDb; Q5PPK9; -.
DR PRIDE; Q5PPK9; -.
DR Ensembl; ENSRNOT00000060185; ENSRNOP00000056930; ENSRNOG00000009285.
DR GeneID; 362721; -.
DR KEGG; rno:362721; -.
DR CTD; 7260; -.
DR RGD; 1305817; Eipr1.
DR eggNOG; KOG1007; Eukaryota.
DR GeneTree; ENSGT00730000111137; -.
DR InParanoid; Q5PPK9; -.
DR OrthoDB; 814890at2759; -.
DR PhylomeDB; Q5PPK9; -.
DR PRO; PR:Q5PPK9; -.
DR Proteomes; UP000002494; Chromosome 6.
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; IMP: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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0050796; P:regulation of insulin secretion; IMP: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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14205; PTHR14205; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..386
FT /note="EARP and GARP complex-interacting protein 1"
FT /id="PRO_0000051302"
FT REPEAT 132..172
FT /note="WD 1"
FT REPEAT 182..222
FT /note="WD 2"
FT REPEAT 226..266
FT /note="WD 3"
FT REPEAT 270..310
FT /note="WD 4"
FT REPEAT 344..384
FT /note="WD 5"
FT REGION 312..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q53HC9"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53HC9"
SQ SEQUENCE 386 AA; 43157 MW; 5E0CF8D34638E3D4 CRC64;
MEDDAPVIYG LEFQARALTP QTAETDAIRF LVGTQSLKYD NQIHIIDFDD ENNIINKNVL
LHQAGEIWHI SASPADKGVL ATCYNKTSDS RVQACAAVWR MPKELESGSH ESPEDPASTA
QTLELLCHLD NGAQGNVACV VWEPMGDGKK VISLADSHIL LWDLQPSSSQ AVLASSAALE
GRGQLKFTSG RWSPHHNCTQ VATASDTTLR GWDTRSMSQI YCIENAHGQL VRDLDFNPNK
QYYLASCGDD CKVKFWDTRN VTEPVKTLEE HSHWVWSVRY NHSHDQLVLT GSSDSRVILS
NMVSISSEPF GHLVDDDDVS DPEEHHTEKS KEPLQDNVIA TYEEHEDSVY AVDWASADPW
LFASLSYDGR LVINRVPRAL KYHILL
