KRE5_YEAST
ID KRE5_YEAST Reviewed; 1365 AA.
AC P22023; D6W331; Q12190;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Killer toxin-resistance protein 5;
DE Flags: Precursor;
GN Name=KRE5; OrderedLocusNames=YOR336W;
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].
RX PubMed=2188106; DOI=10.1128/mcb.10.6.3013-3019.1990;
RA Meaden P., Hill K., Wagner J., Slipetz D., Sommer S.S., Bussey H.;
RT "The yeast KRE5 gene encodes a probable endoplasmic reticulum protein
RT required for (1-->6)-beta-D-glucan synthesis and normal cell growth.";
RL Mol. Cell. Biol. 10:3013-3019(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 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).
CC -!- FUNCTION: Required for (1->6)-beta-D-glucan synthesis and normal cell
CC growth.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- MISCELLANEOUS: Present with 815 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To D.melanogaster UGGG. {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; M33556; AAA34725.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89981.1; -; Genomic_DNA.
DR EMBL; Z75244; CAA99659.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11097.1; -; Genomic_DNA.
DR PIR; S62066; BVBYK5.
DR RefSeq; NP_014981.1; NM_001183756.1.
DR AlphaFoldDB; P22023; -.
DR SMR; P22023; -.
DR BioGRID; 34719; 251.
DR DIP; DIP-5326N; -.
DR MINT; P22023; -.
DR STRING; 4932.YOR336W; -.
DR CAZy; GT24; Glycosyltransferase Family 24.
DR iPTMnet; P22023; -.
DR MaxQB; P22023; -.
DR PaxDb; P22023; -.
DR PRIDE; P22023; -.
DR EnsemblFungi; YOR336W_mRNA; YOR336W; YOR336W.
DR GeneID; 854514; -.
DR KEGG; sce:YOR336W; -.
DR SGD; S000005863; KRE5.
DR VEuPathDB; FungiDB:YOR336W; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_0_1; -.
DR InParanoid; P22023; -.
DR OMA; NGEIYPF; -.
DR BioCyc; YEAST:G3O-33811-MON; -.
DR PRO; PR:P22023; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22023; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IMP:SGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR PANTHER; PTHR11226; PTHR11226; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1365
FT /note="Killer toxin-resistance protein 5"
FT /id="PRO_0000021563"
FT REGION 1334..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1362..1365
FT /note="Prevents secretion from ER"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1091
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 582
FT /note="Missing (in Ref. 1; AAA34725)"
FT /evidence="ECO:0000305"
FT CONFLICT 780..794
FT /note="HLDQNEVPETEHFEA -> ILIKMKCQKQNISKAK (in Ref. 1;
FT AAA34725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1365 AA; 156477 MW; D0F5851175CC0333 CRC64;
MRLLALVLLL LCAPLRAWTY SLRYGIPESA QVWSILVHLL GDVDNQLLTN LYPLVTGLDD
EIDIQENLVA LTSNVLRERY DKEDVADLLE LYASLYPMGM IQHDISSNAE QDDANSSYFV
LNGNRYEKPD DVFYLKSKDL TIQQKVPDVD VIQPYDVVIG TNSEAPILIL YGCPTVIDSD
FEEFNRNLFM EAMNGEGKFR FIWRSTCSLD GKSVEYPLTH PLEITLQNGS RMSSIPQLKK
ILYTVPKEIL VGADNDDQLH DLEPEELREL DLRVTSLISE FYQYKKDITA TLNFTKSIVN
NFPLISKQLI KVSSVNKDII TSNEELNSKG FDYNMLGLYI NGQNWKITSL TPYNLLTALK
TEYQSLLKIT NLLQELEPSK CILDSKFLLN KFSQFSLGKL QNLQPIKMDL HTIPGFSESV
IYFNDIESDP QYDELVNSVQ AFFDKSKFGE LPEIKQNWSE IIFVIDFARL EDSEVKEALG
GLVRAVNVVS QGYPQRVGLL PFSSDSDKSV VNKIYELKNS TDNLTELKSF LETMLLADGL
SANAKHSKHI PVPDVFHLLD ELQIDETSII INGEIYPFRK NAWNYLIAKV IKKDTEFIRK
ELSNSSPKNK QISVRDLLHY KSANLRHNKY TPNYFADSVY SSVNNTALES VCSERIGYYT
KNEEYNLLHT ITLVDDFGSI HALKRLRNLL HTSFVGVRIR IIHVGDISDI WYQLRGSLSQ
KDPIGSINTF IDALKLKKVK SHTYKKSGLN QLGLHKWLPD IPLFELQKGS FIALNGRFIH
LDQNEVPETE HFEAIIKREA LRTIDSVFAL DLLFPGFSQE IINPDLIEMI SSILTRLFYQ
GTHIYNNGID YTTESSLPRM DLSEFFRPNN LTMFEDGKSA SIDLLLILDP LEERTQMILS
LVEQFRPLKF VNIQVILMPT LELNIVPIRR IYVDDADIVK SITSEDSRSD PEVDIEMDVP
NSFIVDNNYR IKKLLIELHS FSSKTVLSTG NIDGMGGVCL ALVDSAGNII DKTTTMKTFG
YGQFHTDKFL KGCYIKSCDS RYTVQSFSTD GHPDFIPSDS LDILSYNPQK IAVKISEEPT
HEEEYEEGRN NDTIINIFTI LESGPDEEER YMQMILSILS KCPETQKVNF FILDQPFISD
TLRKSCEYIN SSDEMRGNVI FLNYEWPQWL RPQRFSSRRR DVSRFLFLDV LLPQNISKVL
YMSPTEVPLD PFDIFQFQGL KRAPLGLFRM SGDGYWKEGY WEKMLRENNL EFYSTEPAFL
VNLERFRELD AGDKYRIHYQ RISTDAMSLV NIGQDLVNNL QLEVPIRFLK GSYKKKLVIN
DECVSEWKKK INKFASSPGD EDVPGESVSS KYQDSDNAAP LHDEL
