ID   KRE1_YEAST              Reviewed;         313 AA.
AC   P17260; D6W0M4;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Protein KRE1;
DE   AltName: Full=Killer toxin-resistance protein 1;
DE   Flags: Precursor;
GN   Name=KRE1; OrderedLocusNames=YNL322C; ORFNames=N0336;
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].
RC   STRAIN=S288c / GRF88;
RX   PubMed=2186051; DOI=10.1083/jcb.110.5.1833;
RA   Boone C., Sommer S.S., Hensel A., Bussey H.;
RT   "Yeast KRE genes provide evidence for a pathway of cell wall beta-glucan
RT   assembly.";
RL   J. Cell Biol. 110:1833-1843(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1676;
RX   PubMed=7645347; DOI=10.1002/yea.320110606;
RA   Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT   "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
RT   identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames.";
RL   Yeast 11:567-572(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S288c / FY1676;
RX   PubMed=7502583; DOI=10.1002/yea.320111109;
RA   Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT   "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT   identifies six known genes, a new member of the hexose transporter family
RT   and ten new open reading frames.";
RL   Yeast 11:1077-1085(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [5]
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   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7500943; DOI=10.1007/bf00290368;
RA   Roemer T., Bussey H.;
RT   "Yeast Kre1p is a cell surface O-glycoprotein.";
RL   Mol. Gen. Genet. 249:209-216(1995).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11853673; DOI=10.1016/s0092-8674(02)00634-7;
RA   Breinig F., Tipper D.J., Schmitt M.J.;
RT   "Kre1p, the plasma membrane receptor for the yeast K1 viral toxin.";
RL   Cell 108:395-405(2002).
RN   [8]
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   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15470101; DOI=10.1099/mic.0.27175-0;
RA   Breinig F., Schleinkofer K., Schmitt M.J.;
RT   "Yeast Kre1p is GPI-anchored and involved in both cell wall assembly and
RT   architecture.";
RL   Microbiology 150:3209-3218(2004).
CC   -!- FUNCTION: Involved in a late stage of cell wall 1,6-beta-glucan
CC       synthesis and assembly. Has a structural, rather than enzymic, function
CC       within cell wall 1,6-beta-glucan assembly and architecture, possibly by
CC       being involved in covalently cross-linking 1,6-beta-glucans to other
CC       cell wall components such as 1,3-beta-glucan, chitin and certain
CC       mannoproteins. Acts as the plasma membrane receptor for the yeast K1
CC       viral toxin. {ECO:0000269|PubMed:11853673,
CC       ECO:0000269|PubMed:15470101}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC       Secreted, cell wall. Note=Identified as GPI-anchored plasma membrane
CC       protein (GPI-PMP) as well as component of the cell wall. Concentrated
CC       at the surface of mother cells.
CC   -!- PTM: Extensively modified; probably through addition of O-linked
CC       mannose residues.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the KRE1 family. {ECO:0000305}.
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DR   EMBL; X51729; CAA36017.1; -; Genomic_DNA.
DR   EMBL; Z46259; CAA86375.1; -; Genomic_DNA.
DR   EMBL; Z71598; CAA96253.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10240.1; -; Genomic_DNA.
DR   PIR; A34677; A34677.
DR   RefSeq; NP_014077.1; NM_001183160.1.
DR   AlphaFoldDB; P17260; -.
DR   BioGRID; 35518; 293.
DR   IntAct; P17260; 1.
DR   MINT; P17260; -.
DR   STRING; 4932.YNL322C; -.
DR   PaxDb; 4932-YNL322C; -.
DR   PeptideAtlas; P17260; -.
DR   EnsemblFungi; YNL322C_mRNA; YNL322C; YNL322C.
DR   GeneID; 855394; -.
DR   KEGG; sce:YNL322C; -.
DR   AGR; SGD:S000005266; -.
DR   SGD; S000005266; KRE1.
DR   VEuPathDB; FungiDB:YNL322C; -.
DR   eggNOG; ENOG502S1TV; Eukaryota.
DR   HOGENOM; CLU_083995_0_0_1; -.
DR   InParanoid; P17260; -.
DR   OMA; RAPTSMW; -.
DR   OrthoDB; 2039460at2759; -.
DR   BioCyc; YEAST:G3O-33307-MONOMER; -.
DR   BioGRID-ORCS; 855394; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P17260; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P17260; Protein.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005199; F:structural constituent of cell wall; TAS:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; TAS:SGD.
DR   InterPro; IPR031452; Kre1.
DR   Pfam; PF17056; KRE1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..288
FT                   /note="Protein KRE1"
FT                   /id="PRO_0000021561"
FT   PROPEP          289..313
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021562"
FT   REPEAT          72..86
FT                   /note="1"
FT   REPEAT          127..141
FT                   /note="2"
FT   REGION          72..141
FT                   /note="2 X approximate repeats"
FT   REGION          94..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           288
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   313 AA;  32158 MW;  B01A5DA0D3781E88 CRC64;
     MMRRTLLHSF ATLLLSLSLW SAAVMAAVTT QVTVVTNVAG ALVTETTIWD PATAAAAATT
     TAQTGFFTTV FTTTNDVGTT VTLTQTVNRA TMLPTTTTST SSTGKTTTTV PTATSSLSSG
     LYLSTVTTTN DLGTTVTLTQ TFTHSSTSAT SSASSSVSSS VSSSGSSSSV KTTTSTGSAV
     AETGTRPDPS TDFTEPPVSA VTSLSIDSYI TITEGTTSTY TTTRAPTSMW VTVVRQGNTI
     TVQTTFVQRF SSQYVTVASP SVGSIGMGTL TGTVGVIKSA IKKTVSHNEA QHLGMSSFTS
     ILGGLLTVLI WFL
//