MTL1_YEAST
ID MTL1_YEAST Reviewed; 551 AA.
AC P53214; D6VUF7; Q45U60;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein MTL1;
DE AltName: Full=MID two-like protein 1;
DE Flags: Precursor;
GN Name=MTL1; OrderedLocusNames=YGR023W;
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.
RC STRAIN=ATCC 204278 / EG123 / SM1058;
RX PubMed=10330137; DOI=10.1128/mcb.19.6.3969;
RA Rajavel M., Philip B., Buehrer B.M., Errede B., Levin D.E.;
RT "Mid2 is a putative sensor for cell integrity signaling in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 19:3969-3976(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
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 [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 [GENOMIC DNA] OF 414-551, AND VARIANT LYS-427.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [6]
RP IDENTIFICATION.
RX PubMed=10348843; DOI=10.1128/jb.181.11.3330-3340.1999;
RA Ketela T., Green R., Bussey H.;
RT "Saccharomyces cerevisiae mid2p is a potential cell wall stress sensor and
RT upstream activator of the PKC1-MPK1 cell integrity pathway.";
RL J. Bacteriol. 181:3330-3340(1999).
RN [7]
RP FUNCTION.
RX PubMed=11779787; DOI=10.1093/genetics/159.4.1435;
RA de Bettignies G., Thoraval D., Morel C., Peypouquet M.-F., Crouzet M.;
RT "Overactivation of the protein kinase C-signaling pathway suppresses the
RT defects of cells lacking the Rho3/Rho4-GAP Rgd1p in Saccharomyces
RT cerevisiae.";
RL Genetics 159:1435-1448(2001).
RN [8]
RP FUNCTION.
RX PubMed=12399379; DOI=10.1093/genetics/162.2.663;
RA Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K.,
RA Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.;
RT "Dissection of upstream regulatory components of the Rho1p effector, 1,3-
RT beta-glucan synthase, in Saccharomyces cerevisiae.";
RL Genetics 162:663-676(2002).
RN [9]
RP FUNCTION.
RX PubMed=15637049; DOI=10.1074/jbc.m411062200;
RA Vilella F., Herrero E., Torres J., de la Torre-Ruiz M.A.;
RT "Pkc1 and the upstream elements of the cell integrity pathway in
RT Saccharomyces cerevisiae, Rom2 and Mtl1, are required for cellular
RT responses to oxidative stress.";
RL J. Biol. Chem. 280:9149-9159(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481 AND SER-482, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Involved in cell integrity signaling during vegetative growth
CC at elevated temperature. Acts positively on the PKC1-MAPK pathway. Cell
CC membrane sensor of oxidative stress in the cell integrity pathway
CC upstream of PKC1. Required to transmit the oxidative signal to SLT2 and
CC to restore the correct actin organization following oxidative stress.
CC Multicopy suppressor of 1,3-beta-glucan synthase (GS) mutation. Also
CC suppresses RGD1 null mutations. {ECO:0000269|PubMed:10330137,
CC ECO:0000269|PubMed:11779787, ECO:0000269|PubMed:12399379,
CC ECO:0000269|PubMed:15637049}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MID2 like cell wall stress sensor family.
CC {ECO:0000305}.
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DR EMBL; Z72807; CAA97006.1; -; Genomic_DNA.
DR EMBL; DQ115389; AAZ22486.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08118.1; -; Genomic_DNA.
DR PIR; S64314; S64314.
DR RefSeq; NP_011537.1; NM_001181152.1.
DR AlphaFoldDB; P53214; -.
DR BioGRID; 33264; 79.
DR DIP; DIP-5509N; -.
DR STRING; 4932.YGR023W; -.
DR iPTMnet; P53214; -.
DR MaxQB; P53214; -.
DR PaxDb; P53214; -.
DR PRIDE; P53214; -.
DR EnsemblFungi; YGR023W_mRNA; YGR023W; YGR023W.
DR GeneID; 852905; -.
DR KEGG; sce:YGR023W; -.
DR SGD; S000003255; MTL1.
DR VEuPathDB; FungiDB:YGR023W; -.
DR eggNOG; ENOG502S2SW; Eukaryota.
DR GeneTree; ENSGT00940000176476; -.
DR HOGENOM; CLU_476680_0_0_1; -.
DR InParanoid; P53214; -.
DR OMA; LIYMFCV; -.
DR BioCyc; YEAST:G3O-30748-MON; -.
DR PRO; PR:P53214; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53214; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IBA:GO_Central.
DR InterPro; IPR007567; Mid2_dom.
DR Pfam; PF04478; Mid2; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Stress response;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..551
FT /note="Protein MTL1"
FT /id="PRO_0000202787"
FT TOPO_DOM 36..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 108..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 264
FT /note="S -> SSSSSSSSSSISLSSSSSSSSSSSSSSSS (in strain: ATCC
FT 204278)"
FT VARIANT 427
FT /note="R -> K (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
SQ SEQUENCE 551 AA; 57528 MW; 86D943341B319951 CRC64;
MASCNPTRKK SSASSLSMWR TILMALTTLP LSVLSQELVP ANSTTSSTAP SITSLSAVES
FTSSTDATSS ASLSTPSIAS VSFTSFPQSS SLLTLSSTLS SELSSSSMQV SSSSTSSSSS
EVTSSSSSSS ISPSSSSSTI ISSSSSLPTF TVASTSSTVA SSTLSTSSSL VISTSSSTFT
FSSESSSSLI SSSISTSVST SSVYVPSSST SSPPSSSSEL TSSSYSSSSS SSTLFSYSSS
FSSSSSSSSS SSSSSSSSSS SSSSYFTLST SSSSSIYSSS SYPSFSSSSS SNPTSSITST
SASSSITPAS EYSNLAKTIT SIIEGQTILS NYYTTITYSP TASASSGKNS HHSGLSKKNR
NIIIGCVVGI GAPLILILLI LIYMFCVQPK KTDFIDSDGK IVTAYRSNIF TKIWYFLLGK
KIGETERFSS DSPIGSNNIQ NFGDIDPEDI LNNDNPYTPK HTNVEGYDDD DDDDANDENL
SSNFHNRGID DQYSPTKSAS YSMSNSNSQD YNDADEVMHD ENIHRVYDDS EASIDENYYT
KPNNGLNITN Y
