EIPR1_CAEEL
ID EIPR1_CAEEL Reviewed; 362 AA.
AC Q9U1Q0;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=EARP-interacting protein 1 {ECO:0000303|PubMed:27191843};
DE AltName: Full=Endosome-associated recycling protein-interacting protein {ECO:0000303|PubMed:27191843};
GN Name=eipr-1 {ECO:0000312|WormBase:Y87G2A.11};
GN ORFNames=Y87G2A.11 {ECO:0000312|WormBase:Y87G2A.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Plays a role in the trafficking of cargo to dense-core
CC vesicles, probably through association with the endosome-associated
CC recycling protein (EARP) complex. Important for neuronal function.
CC {ECO:0000269|PubMed:27191843}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27191843}. Note=The
CC cytoplasmic localization is supported by the over-expression of an
CC eipr-1-GFP fusion protein.
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis and the pharynx.
CC {ECO:0000269|PubMed:27191843}.
CC -!- DISRUPTION PHENOTYPE: Defective egg-laying and slow, but coordinated
CC locomotion when stimulated. Reduced levels of both unprocessed and
CC processed luminal and transmembrane cargo in the motor neuron axons of
CC the dorsal nerve cord. Double knockout with either rab-2, rund-1 or
CC vps-50 results in reduced levels of both unprocessed and processed
CC luminal and transmembrane cargo in the motor neuron axons of the dorsal
CC nerve cord. {ECO:0000269|PubMed:27191843}.
CC -!- SIMILARITY: Belongs to the WD repeat EIPR1 family. {ECO:0000305}.
CC -!- CAUTION: The subcellular location of endogenous eipr-1 could not be
CC identified; diffuse expression of a eipr-1 construct in the cytoplasm
CC may be an artifact due to over-expression of the construct.
CC {ECO:0000303|PubMed:27191843}.
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DR EMBL; BX284601; CAB60432.1; -; Genomic_DNA.
DR RefSeq; NP_493383.1; NM_060982.4.
DR AlphaFoldDB; Q9U1Q0; -.
DR SMR; Q9U1Q0; -.
DR STRING; 6239.Y87G2A.11; -.
DR PaxDb; Q9U1Q0; -.
DR PeptideAtlas; Q9U1Q0; -.
DR EnsemblMetazoa; Y87G2A.11.1; Y87G2A.11.1; WBGene00013599.
DR GeneID; 190778; -.
DR KEGG; cel:CELE_Y87G2A.11; -.
DR UCSC; Y87G2A.11; c. elegans.
DR CTD; 190778; -.
DR WormBase; Y87G2A.11; CE24682; WBGene00013599; eipr-1.
DR eggNOG; KOG1007; Eukaryota.
DR GeneTree; ENSGT00730000111137; -.
DR HOGENOM; CLU_050772_0_0_1; -.
DR InParanoid; Q9U1Q0; -.
DR OMA; GMDCEAR; -.
DR OrthoDB; 814890at2759; -.
DR PhylomeDB; Q9U1Q0; -.
DR PRO; PR:Q9U1Q0; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013599; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1904811; P:positive regulation of dense core granule transport; IMP:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; 1.
DR SMART; SM00320; WD40; 4.
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 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..362
FT /note="EARP-interacting protein 1"
FT /id="PRO_0000437441"
FT REPEAT 61..108
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 206..246
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 250..290
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 319..359
FT /note="WD 4"
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 40954 MW; CF7AC7AE53B13488 CRC64;
MSECLMFGMD CEARCMTSMT ADEENICFLV GTNNIKNDKN QVNKLFMDPE ASRLMSKTFR
HPAGEVRAIA AHPTKSTILA TCTADFSSLG GTHSITIWNI EEDKRTLETV SRLPTEQVMS
CLEWEPNSMK CAAMTPFRPE IQLLNMENGP EIVQNLKIPL ENEEDEMFSA TWSPHHDGNM
LGVTGGRTAW CIDCRTDNEY LKIRDAHIHR TISMDFNPNL QHVIATCGDD GYVRIWDTRS
TSSALTSLHP HAHWVWSVRF HPVHDQLLLT GGSDASVVLS CAQSVSSEQQ IEFRDDEEEE
EDDDLVEKLQ DGQLERIDEH EDSVYACAWS SADPWTFASL SYDGRMIVSN VSRKHKYALM
QL
