ERD1_YEAST
ID ERD1_YEAST Reviewed; 362 AA.
AC P16151; D6VT45;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein ERD1;
GN Name=ERD1; OrderedLocusNames=YDR414C; ORFNames=D9461.4;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2178921; DOI=10.1002/j.1460-2075.1990.tb08154.x;
RA Hardwick K., Lewis M., Semenza J., Dean N., Pelham H.;
RT "ERD1, a yeast gene required for the retention of luminal endoplasmic
RT reticulum proteins, affects glycoprotein processing in the Golgi
RT apparatus.";
RL EMBO J. 9:623-630(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 168.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Required for the retention of luminal endoplasmic reticulum
CC proteins, affects glycoprotein processing in the Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the ERD1 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; U33007; AAB64888.1; -; Genomic_DNA.
DR EMBL; X51949; CAA36211.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12255.2; -; Genomic_DNA.
DR PIR; S69698; S69698.
DR RefSeq; NP_010702.4; NM_001180722.4.
DR AlphaFoldDB; P16151; -.
DR BioGRID; 32473; 400.
DR DIP; DIP-7316N; -.
DR IntAct; P16151; 36.
DR MINT; P16151; -.
DR STRING; 4932.YDR414C; -.
DR TCDB; 2.A.94.1.7; the phosphate permease (pho1) family.
DR PaxDb; P16151; -.
DR PRIDE; P16151; -.
DR EnsemblFungi; YDR414C_mRNA; YDR414C; YDR414C.
DR GeneID; 852023; -.
DR KEGG; sce:YDR414C; -.
DR SGD; S000002822; ERD1.
DR VEuPathDB; FungiDB:YDR414C; -.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_765368_0_0_1; -.
DR InParanoid; P16151; -.
DR OMA; WIFLRVE; -.
DR BioCyc; YEAST:G3O-29956-MON; -.
DR PRO; PR:P16151; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P16151; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006621; P:protein retention in ER lumen; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004342; EXS_C.
DR Pfam; PF03124; EXS; 1.
DR PROSITE; PS51380; EXS; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..362
FT /note="Protein ERD1"
FT /id="PRO_0000087009"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 181..362
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
FT CONFLICT 168
FT /note="A -> G (in Ref. 2; CAA36211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 43230 MW; 8995C2BF2B789C7F CRC64;
MEKSESNSEG LYLQNILNVP PPQRFIVLII LALWIWTWIL KFFLHSNLDV SQVILTRVPH
DIRPGYTLQQ LHRTARNFAL KITRIIIPFH FATVFLFEFM NIIEGPLKNI ILIVYFLPLI
QCVTIFWFLL KECQIIKYCT RRCLLIESSP RSLRNTYILI SDTLTSFAKP LIDFTLFTSL
IFREPFTHFD LSVALLPVLV RLLQCLREYR LLHEATLLFN ALKYSCNLPI LFCTWRSRVY
EGSINEERLH HVQRWFMLIN SSYTLFWDVR MDWSLDSLTS LRSRSKSAVT LKKKMYHSAI
LVDFLLRFWW LWVYLSQNLK LVAADSDYIF FQGEMQYFEV IRRGIWVVFK LDAEYYIKFA
SK
