TED1_YEAST
ID TED1_YEAST Reviewed; 473 AA.
AC P40533; D6VVP3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein TED1;
DE AltName: Full=Trafficking of EMP24/ERV25-dependent cargo disrupted protein 1;
GN Name=TED1; OrderedLocusNames=YIL039W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17989219; DOI=10.1073/pnas.0708765104;
RA Haass F.A., Jonikas M., Walter P., Weissman J.S., Jan Y.-N., Jan L.Y.,
RA Schuldiner M.;
RT "Identification of yeast proteins necessary for cell-surface function of a
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18079-18084(2007).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Acts together with EMP24 and ERV25 in cargo exit from the
CC endoplasmic reticulum. {ECO:0000269|PubMed:17989219}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46861; CAA86912.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08509.1; -; Genomic_DNA.
DR PIR; S49939; S49939.
DR RefSeq; NP_012225.1; NM_001179389.1.
DR AlphaFoldDB; P40533; -.
DR BioGRID; 34951; 220.
DR DIP; DIP-4575N; -.
DR IntAct; P40533; 1.
DR MINT; P40533; -.
DR STRING; 4932.YIL039W; -.
DR MaxQB; P40533; -.
DR PaxDb; P40533; -.
DR PRIDE; P40533; -.
DR EnsemblFungi; YIL039W_mRNA; YIL039W; YIL039W.
DR GeneID; 854772; -.
DR KEGG; sce:YIL039W; -.
DR SGD; S000001301; TED1.
DR VEuPathDB; FungiDB:YIL039W; -.
DR eggNOG; KOG3662; Eukaryota.
DR GeneTree; ENSGT00390000013236; -.
DR HOGENOM; CLU_021690_1_0_1; -.
DR InParanoid; P40533; -.
DR OMA; WSRPTHV; -.
DR BioCyc; YEAST:G3O-31311-MON; -.
DR PRO; PR:P40533; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40533; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR InterPro; IPR033307; Ted1.
DR PANTHER; PTHR13315; PTHR13315; 1.
DR PANTHER; PTHR13315:SF1; PTHR13315:SF1; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Protein TED1"
FT /id="PRO_0000202993"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..451
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 54928 MW; 3D8AF321C9BAFDE8 CRC64;
MLRCAVKKFA YFATFLTIVA NIYIYTYPSF HPEQCSWNCS NKNAPLQKDL TFVDKVKNYF
SDVREQWHGS HASAGNDEDI HILAFGDPQI KGIWPKTPYV SRLDTYGNDY YLGHIYDMMQ
QRLKPQVVTV MGDLFSSQWI GDSEFHNRTK RYISRIFKRD PTSIENIKQQ NLDEKGQYKA
NWPEWGDRFN EILDNVKENE ADNQELSFGF GYENIHSWNP DLEDFLIINI TGNHDVGYSG
DATYQHMTRF HDLFGKDNYW IEYETNTTHP WRIVVLNDLL LEGPALQPEF VEATWIFLNQ
LNERKFNGST VLLTHVPFYK REGLCVDGPD TRYYPDAHAP ESYKSGLLRS QNHLSESVSN
QVLNMIFENG KPGIILTGHD HEGCETVYNK KSTSTWEATK NIESDVFVKE ITVKSMMGEF
NGNTGLVTGH FNTDSMTWEW TFSLCPFAIQ HVWWFAKVSL LVTIFTWSSL LFV
