EAR1_YEAST
ID EAR1_YEAST Reviewed; 550 AA.
AC Q03212; D6VZZ3; Q03830;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein EAR1;
DE AltName: Full=Endosomal adapter of RSP5;
GN Name=EAR1; OrderedLocusNames=YMR171C; ORFNames=YM8010.01C, YM8520.20C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Components of the endosome-vacuole trafficking pathway that
CC regulates nutrient transport. May be involved in processes which
CC determine whether plasma membrane proteins are degraded or routed to
CC the plasma membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305}; Single-pass type
CC II membrane protein {ECO:0000305}. Vacuole membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SSH4 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; Z49808; CAA89904.1; -; Genomic_DNA.
DR EMBL; Z49705; CAA89807.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10067.1; -; Genomic_DNA.
DR PIR; S55118; S55118.
DR RefSeq; NP_013894.1; NM_001182675.1.
DR AlphaFoldDB; Q03212; -.
DR SMR; Q03212; -.
DR BioGRID; 35349; 78.
DR IntAct; Q03212; 1.
DR MINT; Q03212; -.
DR STRING; 4932.YMR171C; -.
DR iPTMnet; Q03212; -.
DR MaxQB; Q03212; -.
DR PaxDb; Q03212; -.
DR PRIDE; Q03212; -.
DR EnsemblFungi; YMR171C_mRNA; YMR171C; YMR171C.
DR GeneID; 855207; -.
DR KEGG; sce:YMR171C; -.
DR SGD; S000004781; EAR1.
DR VEuPathDB; FungiDB:YMR171C; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000158675; -.
DR HOGENOM; CLU_016552_3_0_1; -.
DR InParanoid; Q03212; -.
DR OMA; SPYPYFR; -.
DR BioCyc; YEAST:G3O-32859-MON; -.
DR PRO; PR:Q03212; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03212; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IGI:SGD.
DR CDD; cd12910; SPRY_SSH4_like; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035780; SPRY_Ssh4-like.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Endosome; Glycoprotein; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..550
FT /note="Protein EAR1"
FT /id="PRO_0000203316"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..550
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 172..375
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 479..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 550 AA; 62532 MW; 6B1C6EE9F9A889FA CRC64;
MSFKFLIESL LLGSISGQIR CGRSSVIPRG DVSYGGDDTD ELNMDIMLFA FGTLIVVYIV
ICIVYFFTKQ IATRLITAYY NEHGPGQRIS LFSDYDENNA HVHSRRLMEN MSLRWPNNLD
DADEVRDKLA QLSPEEQFYY KQGEEYIKQN PPFLLNQGLL QQSEDSNPDT TREDPIMNEQ
TRQYIQEEGA YAWEFSPNPD MPNHTVIVEN KTEVSFLNYN YDASISTNLP IPCINKVYYC
EFKIFETDGP LNSDENVSKG VISFGLSTQP YPYFRLPGRH HHSIAYDSNG ARRFNDSFKL
NEQLRTLFPQ CEKGDIVGIG YRSRSGTVFF TRNGKKLNEK SVGGHIRGWK FQYLYPIIGS
NVPCQIHVNF GTYGFVYIEA NVKKWGYAKS NGIKLPPPSY EDYGKDTLLE SGGEDNDFDE
DFSDGDSDNI AAGSTTNLND DIIIRNGEIL PPPPGFEFTM SPPTGKKIIN EEINLDSLPM
LPPSYSDDEH HSKNDKSAIS GRIIGTSRNL ITDEASFDSV DNDNEDENDH ERDPEQFSEF
DDYESRMHGI
