SMI1_YEAST
ID SMI1_YEAST Reviewed; 505 AA.
AC P32566; D6VV09;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cell wall assembly regulator SMI1;
DE AltName: Full=Killer toxin-resistance protein 4;
GN Name=SMI1; Synonyms=KNR4, KTR4; OrderedLocusNames=YGR229C; ORFNames=G8553;
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=ATCC 208353 / W303-1A;
RX PubMed=8516310; DOI=10.1073/pnas.90.12.5623;
RA Fishel B.R., Sperry A.O., Garrard W.T.;
RT "Yeast calmodulin and a conserved nuclear protein participate in the in
RT vivo binding of a matrix association region.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5623-5627(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8289782; DOI=10.1128/mcb.14.2.1017-1025.1994;
RA Hong Z., Mann P., Brown N.H., Tran L.E., Shaw K.J., Didomenico B.J.;
RT "Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-
RT glucan synthesis.";
RL Mol. Cell. Biol. 14:1017-1025(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 FUNCTION.
RX PubMed=10206705; DOI=10.1099/13500872-145-1-249;
RA Martin H., Dagkessamanskaia A., Satchanska G., Dallies N., Francois J.;
RT "KNR4, a suppressor of Saccharomyces cerevisiae cwh mutants, is involved in
RT the transcriptional control of chitin synthase genes.";
RL Microbiology 145:249-258(1999).
RN [8]
RP INTERACTION WITH TYS1.
RX PubMed=11410349; DOI=10.1111/j.1574-6968.2001.tb10692.x;
RA Dagkessamanskaia A., Martin-Yken H., Basmaji F., Briza P., Francois J.;
RT "Interaction of Knr4 protein, a protein involved in cell wall synthesis,
RT with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces
RT cerevisiae.";
RL FEMS Microbiol. Lett. 200:53-58(2001).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-203; SER-381;
RP SER-394 AND SER-400, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-376; SER-381;
RP SER-394 AND SER-400, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Protein involved in the regulation of cell wall assembly and
CC 1,3-beta-glucan synthesis, possibly through the transcriptional
CC regulation of cell wall glucan and chitin synthesis.
CC {ECO:0000269|PubMed:10206705, ECO:0000269|PubMed:8289782}.
CC -!- SUBUNIT: Interacts with TYS1. {ECO:0000269|PubMed:11410349}.
CC -!- INTERACTION:
CC P32566; P36421: TYS1; NbExp=3; IntAct=EBI-17452, EBI-18843;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 5680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the KNR4/SMI1 family. {ECO:0000305}.
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DR EMBL; L15423; AAA35053.1; -; Genomic_DNA.
DR EMBL; L13164; AAA67469.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61178.1; -; Genomic_DNA.
DR EMBL; Z73013; CAA97257.1; -; Genomic_DNA.
DR EMBL; AY723820; AAU09737.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08320.1; -; Genomic_DNA.
DR PIR; A55923; A55923.
DR RefSeq; NP_011745.1; NM_001181358.1.
DR PDB; 5J1B; X-ray; 2.50 A; A/B=80-340.
DR PDB; 6QBM; X-ray; 2.50 A; A/B=80-340.
DR PDB; 6QBN; X-ray; 2.40 A; A/B=80-340.
DR PDB; 6QBO; X-ray; 2.75 A; A/B=80-340.
DR PDB; 6QBP; X-ray; 2.40 A; A/B=80-340.
DR PDB; 6QBQ; X-ray; 2.35 A; A/B=80-340.
DR PDB; 6QBR; X-ray; 2.15 A; A/B=80-340.
DR PDBsum; 5J1B; -.
DR PDBsum; 6QBM; -.
DR PDBsum; 6QBN; -.
DR PDBsum; 6QBO; -.
DR PDBsum; 6QBP; -.
DR PDBsum; 6QBQ; -.
DR PDBsum; 6QBR; -.
DR AlphaFoldDB; P32566; -.
DR SMR; P32566; -.
DR BioGRID; 33481; 559.
DR DIP; DIP-1635N; -.
DR IntAct; P32566; 58.
DR MINT; P32566; -.
DR STRING; 4932.YGR229C; -.
DR iPTMnet; P32566; -.
DR MaxQB; P32566; -.
DR PaxDb; P32566; -.
DR PRIDE; P32566; -.
DR EnsemblFungi; YGR229C_mRNA; YGR229C; YGR229C.
DR GeneID; 853144; -.
DR KEGG; sce:YGR229C; -.
DR SGD; S000003461; SMI1.
DR VEuPathDB; FungiDB:YGR229C; -.
DR eggNOG; ENOG502QTAZ; Eukaryota.
DR GeneTree; ENSGT00940000153571; -.
DR HOGENOM; CLU_027501_3_0_1; -.
DR InParanoid; P32566; -.
DR OMA; TQNDITH; -.
DR BioCyc; YEAST:G3O-30907-MON; -.
DR PRO; PR:P32566; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32566; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0032995; P:regulation of fungal-type cell wall biogenesis; IMP:SGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:SGD.
DR DisProt; DP02159; -.
DR Gene3D; 3.40.1580.10; -; 1.
DR InterPro; IPR009203; Knr4/Smi1.
DR InterPro; IPR018958; Knr4/Smi1-like_dom.
DR InterPro; IPR037883; Knr4/Smi1-like_sf.
DR Pfam; PF09346; SMI1_KNR4; 1.
DR PIRSF; PIRSF017023; KNR4; 1.
DR SMART; SM00860; SMI1_KNR4; 1.
DR SUPFAM; SSF160631; SSF160631; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..505
FT /note="Cell wall assembly regulator SMI1"
FT /id="PRO_0000209870"
FT REGION 343..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6QBR"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:6QBN"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 272..280
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6QBR"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:6QBR"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:6QBR"
FT HELIX 327..340
FT /evidence="ECO:0007829|PDB:6QBR"
SQ SEQUENCE 505 AA; 57079 MW; E1A4AE086C5137D7 CRC64;
MDLFKRKVKE WVYSLSTDDH YAEYNPDETP TFNMGKRLNS NNGQVNPSQM HLNSVDEEMS
MGFQNGVPSN EDINIDEFTS TESNDGVSET LLAWRHIDFW TSEHNPDLNA TLSDPCTQND
ITHAEEDLEV SFPNPVKASF KIHDGQEDLE SMTGTSGLFY GFQLMTLDQV VAMTQAWRNV
AKNLNKRSQQ GLSHVTSTGS SSSMERLNGN KFKLPNIPDQ KSIPPNAVQP VYAHPAWIPL
ITDNAGNHIG VDLAPGPNGK YAQIITFGRD FDTKFVIAEN WGEFLLSFAN DLEAGNWYLV
DDNDDYFSGD GELVFRDKKS NGPIQDYFEV LKRRTWIKYQ ENLRSQQQKS QPDTSLQEQK
YVPASQKKVA AEQPSTLNAE SIKGEDSGSA DVQSVQDHES VKIVKTEPSE AETTTVNTES
LGQAEHEIKA DNVDIKQESE RKEDEKQPKV EEKEHVENEH VTESAKKDDD VNKQTEEMNK
KEENEIRSDD AKVEEAREEF ENIAL
