ID   EIPR1_MACFA             Reviewed;         387 AA.
AC   Q4R571;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
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}; ORFNames=QccE-16240;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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}.
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DR   EMBL; AB169673; BAE01754.1; -; mRNA.
DR   AlphaFoldDB; Q4R571; -.
DR   SMR; Q4R571; -.
DR   STRING; 9541.XP_005576683.1; -.
DR   eggNOG; KOG1007; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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..387
FT                   /note="EARP and GARP complex-interacting protein 1"
FT                   /id="PRO_0000051299"
FT   REPEAT          132..172
FT                   /note="WD 1"
FT   REPEAT          180..222
FT                   /note="WD 2"
FT   REPEAT          226..266
FT                   /note="WD 3"
FT   REPEAT          270..310
FT                   /note="WD 4"
FT   REPEAT          345..385
FT                   /note="WD 5"
FT   REGION          310..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..334
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         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q53HC9"
SQ   SEQUENCE   387 AA;  43545 MW;  85B1967996786F69 CRC64;
     MEDDAPVIYG LEFQARALTP QTAETDAIRF LVGTQSLKYD NQIHIIDFDD ENNIINKNVL
     LHQAGEIWHI SASPADRGVL ATCYNRTSDS KVLTCAAVWR MPKELESGSH ESPDDSSSTA
     QTLELLCHLD NTAHSNMACV VWEPMGDGKK IISLADNHIL LWDLQESSSQ AVLASSASLG
     GKGQLKFTSG RWSPHHNCTQ VATANDTTLR GWDTRTMSQI YCIENAHGQL VRDLDFNPNK
     QYYLASCGDD CKVKFWDTRN VTEPVKTLEE HSHWVWNVRY NHSHDQLVLT GSSDSRVILS
     NMVSISSEPF GHLVDDDDIS DQEDHRSEEK SKEPLQDNVI ATYEEHEDSV YAVDWSSADP
     WLFASLSYDG RLVINRVPRA LKYHILL