SED1_YEAST
ID SED1_YEAST Reviewed; 338 AA.
AC Q01589; D6VS63; Q6Q5U8; Q8J057; Q8J270; Q8J271; Q8J272; Q8J273; Q8J274;
AC Q8J275;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cell wall protein SED1;
DE AltName: Full=Glycoprotein GP260;
DE Flags: Precursor;
GN Name=SED1; OrderedLocusNames=YDR077W; ORFNames=D4431;
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], AND FUNCTION.
RX PubMed=1327759; DOI=10.1002/j.1460-2075.1992.tb05512.x;
RA Hardwick K.G., Boothroyd J.C., Rudner A.D., Pelham H.R.B.;
RT "Genes that allow yeast cells to grow in the absence of the HDEL
RT receptor.";
RL EMBO J. 11:4187-4195(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632;
RX PubMed=12406735; DOI=10.1128/aem.68.11.5437-5444.2002;
RA Mannazzu I., Simonetti E., Marinangeli P., Guerra E., Budroni M.,
RA Thangavelu M., Clementi F.;
RT "SED1 gene length and sequence polymorphisms in feral strains of
RT Saccharomyces cerevisiae.";
RL Appl. Environ. Microbiol. 68:5437-5444(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7483840; DOI=10.1002/yea.320110708;
RA Coster F., Jonniaux J.-L., Goffeau A.;
RT "Analysis of a 32.8 kb segment of yeast chromosome IV reveals 21 open
RT reading frames, including TPS2, PPH3, RAD55, SED1, PDC2, AFR1, SSS1, SLU7
RT and a tRNA for arginine.";
RL Yeast 11:673-679(1995).
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 [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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 20-32, PROTEIN SEQUENCE OF 243-276 AND 292-301,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9642191; DOI=10.1128/jb.180.13.3381-3387.1998;
RA Shimoi H., Kitagaki H., Ohmori H., Iimura Y., Ito K.;
RT "Sed1p is a major cell wall protein of Saccharomyces cerevisiae in the
RT stationary phase and is involved in lytic enzyme resistance.";
RL J. Bacteriol. 180:3381-3387(1998).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8980634; DOI=10.1016/s0304-4165(96)00067-0;
RA van der Vaart J.M., van Schagen F.S., Mooren A.T.A., Chapman J.W.,
RA Klis F.M., Verrips C.T.;
RT "The retention mechanism of cell wall proteins in Saccharomyces cerevisiae.
RT Wall-bound Cwp2p is beta-1,6-glucosylated.";
RL Biochim. Biophys. Acta 1291:206-214(1996).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9023939; DOI=10.1128/aem.63.2.615-620.1997;
RA Van der Vaart J.M., te Biesebeke R., Chapman J.W., Toschka H.Y., Klis F.M.,
RA Verrips C.T.;
RT "Comparison of cell wall proteins of Saccharomyces cerevisiae as anchors
RT for cell surface expression of heterologous proteins.";
RL Appl. Environ. Microbiol. 63:615-620(1997).
RN [10]
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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15093776; DOI=10.1016/j.femsyr.2004.02.006;
RA Bowen S., Wheals A.E.;
RT "Incorporation of Sed1p into the cell wall of Saccharomyces cerevisiae
RT involves KRE6.";
RL FEMS Yeast Res. 4:731-735(2004).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15165243; DOI=10.1111/j.1365-2958.2004.04064.x;
RA Hagen I., Ecker M., Lagorce A., Francois J.M., Sestak S., Rachel R.,
RA Grossmann G., Hauser N.C., Hoheisel J.D., Tanner W., Strahl S.;
RT "Sed1p and Srl1p are required to compensate for cell wall instability in
RT Saccharomyces cerevisiae mutants defective in multiple GPI-anchored
RT mannoproteins.";
RL Mol. Microbiol. 52:1413-1425(2004).
RN [13]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Component of the cell wall. Major cell wall protein in
CC stationary phase cells. Required to stabilize the cell wall in the
CC absence of multiple GPI-anchored mannoproteins.
CC {ECO:0000269|PubMed:1327759, ECO:0000269|PubMed:15165243}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP).
CC -!- INDUCTION: Induced in stationary phase and under conditions of stress
CC and starvation (at protein level). {ECO:0000269|PubMed:9642191}.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SED1 family. {ECO:0000305}.
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DR EMBL; X66838; CAA47314.1; -; Genomic_DNA.
DR EMBL; AF510219; AAN62891.1; -; Genomic_DNA.
DR EMBL; AF510220; AAN62892.1; -; Genomic_DNA.
DR EMBL; AF510221; AAN62893.1; -; Genomic_DNA.
DR EMBL; AF510222; AAN62894.1; -; Genomic_DNA.
DR EMBL; AF510223; AAN62895.1; -; Genomic_DNA.
DR EMBL; AF510224; AAN62896.1; -; Genomic_DNA.
DR EMBL; AF510225; AAN62897.1; -; Genomic_DNA.
DR EMBL; AF510226; AAN62898.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57604.1; -; Genomic_DNA.
DR EMBL; Z46796; CAA86799.1; -; Genomic_DNA.
DR EMBL; Z74373; CAA98896.1; -; Genomic_DNA.
DR EMBL; AY557693; AAS56019.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11923.1; -; Genomic_DNA.
DR PIR; S28004; S28004.
DR RefSeq; NP_010362.3; NM_001180385.3.
DR AlphaFoldDB; Q01589; -.
DR BioGRID; 32132; 108.
DR DIP; DIP-1613N; -.
DR IntAct; Q01589; 2.
DR MINT; Q01589; -.
DR STRING; 4932.YDR077W; -.
DR iPTMnet; Q01589; -.
DR MaxQB; Q01589; -.
DR PaxDb; Q01589; -.
DR PRIDE; Q01589; -.
DR EnsemblFungi; YDR077W_mRNA; YDR077W; YDR077W.
DR GeneID; 851649; -.
DR KEGG; sce:YDR077W; -.
DR SGD; S000002484; SED1.
DR VEuPathDB; FungiDB:YDR077W; -.
DR eggNOG; ENOG502S7XK; Eukaryota.
DR HOGENOM; CLU_054260_0_0_1; -.
DR InParanoid; Q01589; -.
DR OMA; IPAWTAN; -.
DR BioCyc; YEAST:G3O-29682-MON; -.
DR PRO; PR:Q01589; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q01589; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR InterPro; IPR038843; Sed1/Spi1.
DR PANTHER; PTHR35523; PTHR35523; 4.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT CHAIN 19..318
FT /note="Cell wall protein SED1"
FT /id="PRO_0000022292"
FT PROPEP 319..338
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022293"
FT REPEAT 58..65
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 66..79
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 80..93
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 94..101
FT /note="1-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 102..115
FT /note="1-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 116..123
FT /note="1-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 124..137
FT /note="1-7"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 169..211
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 220..262
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 20..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..137
FT /note="7 X approximate tandem repeats"
FT REGION 169..262
FT /note="2 X 43 AA repeats"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 318
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 80..93
FT /note="Missing (in strain: CBS 1171 and in allele SED1-1,
FT SED1-2, SED1-3, SED1-4, SED1-5, SED1-6 and SED1-7)"
FT VARIANT 94
FT /note="T -> TSTEAPTTDTTSEAPTTAIPTNG (in allele SED1-2)"
FT VARIANT 94
FT /note="T -> TSTEAPTTDTTTEAPTTAIPTNG (in allele SED1-5)"
FT VARIANT 94
FT /note="T -> TSTEAPTTDTTTEAPTTALPTNGTSTEAPTDTTTEAPTTALPTNG
FT (in allele SED1-3 and SED1-6)"
FT VARIANT 212
FT /note="P -> PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPC
FT TIEK (in allele SED1-4, SED1-5 and SED1-6)"
FT VARIANT 212
FT /note="P -> PTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPC
FT TIEKPTTTSTTEYTVVTEYTTYCPEPTTFTTNGKTYTVTEPTTLTITDCPCTIEK (in
FT allele SED1-7)"
FT CONFLICT 309
FT /note="S -> P (in Ref. 6; AAS56019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 34431 MW; F0CA9B6AA4B040F6 CRC64;
MKLSTVLLSA GLASTTLAQF SNSTSASSTD VTSSSSISTS SGSVTITSSE APESDNGTST
AAPTETSTEA PTTAIPTNGT STEAPTTAIP TNGTSTEAPT DTTTEAPTTA LPTNGTSTEA
PTDTTTEAPT TGLPTNGTTS AFPPTTSLPP SNTTTTPPYN PSTDYTTDYT VVTEYTTYCP
EPTTFTTNGK TYTVTEPTTL TITDCPCTIE KPTTTSTTEY TVVTEYTTYC PEPTTFTTNG
KTYTVTEPTT LTITDCPCTI EKSEAPESSV PVTESKGTTT KETGVTTKQT TANPSLTVST
VVPVSSSASS HSVVINSNGA NVVVPGALGL AGVAMLFL
