EIPR1_HUMAN
ID EIPR1_HUMAN Reviewed; 387 AA.
AC Q53HC9; D6W4Y1; O43179; Q53S19; Q53SG2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=EARP and GARP complex-interacting protein 1 {ECO:0000305|PubMed:27440922};
DE AltName: Full=Endosome-associated recycling protein-interacting protein {ECO:0000305|PubMed:27440922};
DE AltName: Full=Golgi-associated retrograde protein-interacting protein {ECO:0000305|PubMed:27440922};
DE AltName: Full=Tumor-suppressing STF cDNA 1 protein;
DE AltName: Full=Tumor-suppressing subchromosomal transferable fragment candidate gene 1 protein {ECO:0000303|PubMed:27440922};
GN Name=EIPR1 {ECO:0000312|HGNC:HGNC:12383};
GN Synonyms=TSSC1 {ECO:0000303|PubMed:27440922, ECO:0000312|HGNC:HGNC:12383};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9403053; DOI=10.1006/geno.1997.4981;
RA Hu R.-J., Lee M.P., Connors T.D., Johnson L.A., Burn T.C., Su K.,
RA Landes G.M., Feinberg A.P.;
RT "A 2.5-Mb transcript map of a tumor-suppressing subchromosomal transferable
RT fragment from 11p15.5, and isolation and sequence analysis of three novel
RT genes.";
RL Genomics 46:9-17(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EARP COMPLEX, INTERACTION
RP WITH GARP COMPLEX, AND INTERACTION WITH SNAP29.
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 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 (PubMed:27440922). 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(PubMed:27440922). Promotes the recycling of
CC internalized transferrin receptor (TFRC) to the plasma membrane through
CC interaction with endosome-associated recycling protein (EARP) complex
CC (PubMed:27440922). 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:Q5PPK9, ECO:0000269|PubMed:27440922}.
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:0000269|PubMed:27440922}.
CC -!- INTERACTION:
CC Q53HC9; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-1055422, EBI-17490746;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:27440922}.
CC -!- SIMILARITY: Belongs to the WD repeat EIPR1 family. {ECO:0000305}.
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DR EMBL; AF019952; AAC51911.1; -; mRNA.
DR EMBL; AK222652; BAD96372.1; -; mRNA.
DR EMBL; AC019118; AAY24338.1; -; Genomic_DNA.
DR EMBL; AC073502; AAY24193.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01070.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01071.1; -; Genomic_DNA.
DR EMBL; BC002485; AAH02485.1; -; mRNA.
DR CCDS; CCDS1651.1; -.
DR RefSeq; NP_003301.1; NM_003310.3.
DR AlphaFoldDB; Q53HC9; -.
DR SMR; Q53HC9; -.
DR BioGRID; 113111; 97.
DR IntAct; Q53HC9; 39.
DR STRING; 9606.ENSP00000371559; -.
DR GlyGen; Q53HC9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q53HC9; -.
DR PhosphoSitePlus; Q53HC9; -.
DR BioMuta; EIPR1; -.
DR DMDM; 84029603; -.
DR OGP; O43179; -.
DR EPD; Q53HC9; -.
DR jPOST; Q53HC9; -.
DR MassIVE; Q53HC9; -.
DR MaxQB; Q53HC9; -.
DR PaxDb; Q53HC9; -.
DR PeptideAtlas; Q53HC9; -.
DR PRIDE; Q53HC9; -.
DR ProteomicsDB; 62505; -.
DR Antibodypedia; 26290; 194 antibodies from 26 providers.
DR DNASU; 7260; -.
DR Ensembl; ENST00000382125.9; ENSP00000371559.4; ENSG00000032389.13.
DR GeneID; 7260; -.
DR KEGG; hsa:7260; -.
DR MANE-Select; ENST00000382125.9; ENSP00000371559.4; NM_003310.5; NP_003301.1.
DR UCSC; uc002qxj.3; human.
DR CTD; 7260; -.
DR DisGeNET; 7260; -.
DR GeneCards; EIPR1; -.
DR HGNC; HGNC:12383; EIPR1.
DR HPA; ENSG00000032389; Low tissue specificity.
DR MIM; 608998; gene.
DR neXtProt; NX_Q53HC9; -.
DR OpenTargets; ENSG00000032389; -.
DR PharmGKB; PA37051; -.
DR VEuPathDB; HostDB:ENSG00000032389; -.
DR eggNOG; KOG1007; Eukaryota.
DR GeneTree; ENSGT00730000111137; -.
DR HOGENOM; CLU_050772_0_0_1; -.
DR InParanoid; Q53HC9; -.
DR OMA; HQFLALH; -.
DR OrthoDB; 814890at2759; -.
DR PhylomeDB; Q53HC9; -.
DR TreeFam; TF105847; -.
DR PathwayCommons; Q53HC9; -.
DR SignaLink; Q53HC9; -.
DR BioGRID-ORCS; 7260; 67 hits in 1088 CRISPR screens.
DR ChiTaRS; TSSC1; human.
DR GeneWiki; TSSC1; -.
DR GenomeRNAi; 7260; -.
DR Pharos; Q53HC9; Tbio.
DR PRO; PR:Q53HC9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53HC9; protein.
DR Bgee; ENSG00000032389; Expressed in prefrontal cortex and 167 other tissues.
DR ExpressionAtlas; Q53HC9; baseline and differential.
DR Genevisible; Q53HC9; HS.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IDA:UniProtKB.
DR GO; GO:1905281; P:positive regulation of retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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 1: Evidence at protein 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_0000051298"
FT REPEAT 4..48
FT /note="WD 1"
FT REPEAT 55..101
FT /note="WD 2"
FT REPEAT 124..164
FT /note="WD 3"
FT REPEAT 172..214
FT /note="WD 4"
FT REPEAT 219..258
FT /note="WD 5"
FT REPEAT 263..302
FT /note="WD 6"
FT REPEAT 338..379
FT /note="WD 7"
FT REGION 310..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CONFLICT 58
FT /note="N -> S (in Ref. 2; BAD96372)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="T -> A (in Ref. 2; BAD96372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43603 MW; 7B1CCD35B7C38780 CRC64;
MEDDAPVIYG LEFQARALTP QTAETDAIRF LVGTQSLKYD NQIHIIDFDD ENNIINKNVL
LHQAGEIWHI SASPADRGVL TTCYNRTSDS KVLTCAAVWR MPKELESGSH ESPDDSSSTA
QTLELLCHLD NTAHGNMACV VWEPMGDGKK IISLADNHIL LWDLQESSSQ AVLASSASLE
GKGQLKFTSG RWSPHHNCTQ VATANDTTLR GWDTRSMSQI YCIENAHGQL VRDLDFNPNK
QYYLASCGDD CKVKFWDTRN VTEPVKTLEE HSHWVWNVRY NHSHDQLVLT GSSDSRVILS
NMVSISSEPF GHLVDDDDIS DQEDHRSEEK SKEPLQDNVI ATYEEHEDSV YAVDWSSADP
WLFASLSYDG RLVINRVPRA LKYHILL
