SHR3_YEAST
ID SHR3_YEAST Reviewed; 210 AA.
AC Q02774; D6VRE2; Q12413;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Secretory component protein SHR3;
GN Name=SHR3; OrderedLocusNames=YDL212W; ORFNames=D1022;
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=1423607; DOI=10.1016/0092-8674(92)90515-e;
RA Ljungdahl P.O., Gimeno C.J., Styles C.A., Fink G.R.;
RT "SHR3: a novel component of the secretory pathway specifically required for
RT localization of amino acid permeases in yeast.";
RL Cell 71:463-478(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [3]
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 [4]
RP GENOME REANNOTATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
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: Involved in amino acid permease processing and required for
CC the efficient translocation of structurally related amino acid
CC permeases from the endoplasmic reticulum to the plasma membrane. SHR3
CC may function as a permease-specific 'adaptor' molecule that functions
CC in conjunction with the SEC62/SEC63 complex. Yeast cells may require
CC SHR3 to expedite the processing of permeases to ensure their rapid
CC expression at the plasma membrane in response to changing environmental
CC conditions.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q02774; P38084: BAP2; NbExp=3; IntAct=EBI-17099, EBI-3414;
CC Q02774; P35206: CSG2; NbExp=3; IntAct=EBI-17099, EBI-2051140;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- MISCELLANEOUS: Present with 6510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L01264; AAA35035.1; -; Genomic_DNA.
DR EMBL; X99000; CAA67479.1; -; Genomic_DNA.
DR EMBL; Z74260; CAA98790.1; -; Genomic_DNA.
DR EMBL; AY693071; AAT93090.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11652.1; -; Genomic_DNA.
DR PIR; S67771; S67771.
DR RefSeq; NP_010069.1; NM_001180272.1.
DR AlphaFoldDB; Q02774; -.
DR SMR; Q02774; -.
DR BioGRID; 31833; 262.
DR DIP; DIP-1615N; -.
DR IntAct; Q02774; 33.
DR MINT; Q02774; -.
DR STRING; 4932.YDL212W; -.
DR MaxQB; Q02774; -.
DR PaxDb; Q02774; -.
DR PRIDE; Q02774; -.
DR TopDownProteomics; Q02774; -.
DR EnsemblFungi; YDL212W_mRNA; YDL212W; YDL212W.
DR GeneID; 851314; -.
DR KEGG; sce:YDL212W; -.
DR SGD; S000002371; SHR3.
DR VEuPathDB; FungiDB:YDL212W; -.
DR eggNOG; ENOG502RXJB; Eukaryota.
DR HOGENOM; CLU_080510_1_1_1; -.
DR InParanoid; Q02774; -.
DR OMA; GPTCFFL; -.
DR BioCyc; YEAST:G3O-29594-MON; -.
DR PRO; PR:Q02774; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q02774; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IGI:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR013248; Psh3/Shr3.
DR PANTHER; PTHR28228; PTHR28228; 1.
DR Pfam; PF08229; SHR3_chaperone; 1.
DR PIRSF; PIRSF029187; Shr3_AAP_chap; 1.
DR SMART; SM00786; SHR3_chaperone; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..210
FT /note="Secretory component protein SHR3"
FT /id="PRO_0000097740"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..59
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..130
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 178..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 125..129
FT /note="GEVTE -> EKLR (in Ref. 1; AAA35035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23512 MW; BA154889746F3EB5 CRC64;
MFSYSDFCSI GTAMILSATT FLMGVFFSNM PYDYHLLFNP NSTQEHFDLA LRHYQILHET
PLPVIVTLCV VAGIGLVGGT IKVFKPNPEL QMFEYCSLGL YVLAICVFLT NVKTGIDCSV
SHNWGEVTEN QGLAVIASSN IILLVMFAGV IILQIGLWYS NWDLQKRLKE FYAQEEREAA
NAGKKTEKVD NAKKNDNKSK GAQKRKNAKK
