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   27-MAR-2024, entry version 154.
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; 234.
DR   DIP; DIP-4575N; -.
DR   IntAct; P40533; 1.
DR   MINT; P40533; -.
DR   STRING; 4932.YIL039W; -.
DR   GlyCosmos; P40533; 5 sites, No reported glycans.
DR   GlyGen; P40533; 5 sites.
DR   MaxQB; P40533; -.
DR   PaxDb; 4932-YIL039W; -.
DR   PeptideAtlas; P40533; -.
DR   EnsemblFungi; YIL039W_mRNA; YIL039W; YIL039W.
DR   GeneID; 854772; -.
DR   KEGG; sce:YIL039W; -.
DR   AGR; SGD:S000001301; -.
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; GLKEQNH; -.
DR   OrthoDB; 9507at2759; -.
DR   BioCyc; YEAST:G3O-31311-MONOMER; -.
DR   BioGRID-ORCS; 854772; 3 hits in 10 CRISPR screens.
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: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   CDD; cd08164; MPP_Ted1; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR033308; PGAP5/Cdc1/Ted1.
DR   InterPro; IPR033307; Ted1_MPase_dom.
DR   PANTHER; PTHR13315; METALLO PHOSPHOESTERASE RELATED; 1.
DR   PANTHER; PTHR13315:SF1; PROTEIN TED1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 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
//