MSB2_YEAST
ID MSB2_YEAST Reviewed; 1306 AA.
AC P32334; D6VUF0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Signaling mucin MSB2;
DE AltName: Full=Multicopy suppressor of bud emergence 2;
DE AltName: Full=Osmosensor MSB2;
DE Flags: Precursor;
GN Name=MSB2; OrderedLocusNames=YGR014W;
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=1514328; DOI=10.1002/yea.320080409;
RA Bender A., Pringle J.R.;
RT "A Ser/Thr-rich multicopy suppressor of a cdc24 bud emergence defect.";
RL Yeast 8:315-323(1992).
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 FUNCTION.
RX PubMed=2690082; DOI=10.1073/pnas.86.24.9976;
RA Bender A., Pringle J.R.;
RT "Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and
RT three newly identified genes including the ras-related gene RSR1.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9976-9980(1989).
RN [6]
RP FUNCTION.
RX PubMed=12052881; DOI=10.1128/mcb.22.13.4739-4749.2002;
RA O'Rourke S.M., Herskowitz I.;
RT "A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2
RT protein and functions in parallel with the Sho1 branch.";
RL Mol. Cell. Biol. 22:4739-4749(2002).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC42 AND SHO1.
RX PubMed=15256499; DOI=10.1101/gad.1178604;
RA Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
RA Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
RT "A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous
RT growth pathway in yeast.";
RL Genes Dev. 18:1695-1708(2004).
RN [9]
RP FUNCTION.
RX PubMed=15713635; DOI=10.1128/mcb.25.5.1793-1803.2005;
RA Flatauer L.J., Zadeh S.F., Bardwell L.;
RT "Mitogen-activated protein kinases with distinct requirements for Ste5
RT scaffolding influence signaling specificity in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 25:1793-1803(2005).
RN [10]
RP FUNCTION.
RX PubMed=19439450; DOI=10.1091/mbc.e08-07-0760;
RA Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
RT "The signaling mucins Msb2 and Hkr1 differentially regulate the
RT filamentation mitogen-activated protein kinase pathway and contribute to a
RT multimodal response.";
RL Mol. Biol. Cell 20:3101-3114(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1300, AND IDENTIFICATION BY
RP 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: Plasma membrane signaling mucin that promotes activation of
CC the MAPK for the filamentous growth pathway. Partially redundant with
CC the SHO1 osmosensing branch for the activation of STE11.
CC {ECO:0000269|PubMed:12052881, ECO:0000269|PubMed:1514328,
CC ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:15713635,
CC ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:2690082}.
CC -!- SUBUNIT: Interacts with CDC42 and SHO1. {ECO:0000269|PubMed:15256499}.
CC -!- INTERACTION:
CC P32334; Q06810: OPY2; NbExp=3; IntAct=EBI-11328, EBI-2068557;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15256499};
CC Single-pass membrane protein {ECO:0000269|PubMed:15256499}.
CC Note=localized to polarized sites on the cell surface.
CC -!- PTM: O-glycosylated in the Ser/Thr-rich regions. {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HKR1/MSB2 family. {ECO:0000305}.
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DR EMBL; M77354; AAA34798.1; -; Genomic_DNA.
DR EMBL; Z72799; CAA96997.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08111.1; -; Genomic_DNA.
DR PIR; S25370; S25370.
DR RefSeq; NP_011528.3; NM_001181143.3.
DR AlphaFoldDB; P32334; -.
DR SMR; P32334; -.
DR BioGRID; 33257; 105.
DR ComplexPortal; CPX-1302; OPY2-MSB2 osmosensory complex.
DR DIP; DIP-1455N; -.
DR IntAct; P32334; 13.
DR MINT; P32334; -.
DR STRING; 4932.YGR014W; -.
DR iPTMnet; P32334; -.
DR MaxQB; P32334; -.
DR PaxDb; P32334; -.
DR PRIDE; P32334; -.
DR EnsemblFungi; YGR014W_mRNA; YGR014W; YGR014W.
DR GeneID; 852897; -.
DR KEGG; sce:YGR014W; -.
DR SGD; S000003246; MSB2.
DR VEuPathDB; FungiDB:YGR014W; -.
DR eggNOG; ENOG502QW7T; Eukaryota.
DR HOGENOM; CLU_262646_0_0_1; -.
DR InParanoid; P32334; -.
DR OMA; WIPTELI; -.
DR BioCyc; YEAST:G3O-30741-MON; -.
DR PRO; PR:P32334; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32334; protein.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005034; F:osmosensor activity; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IBA:GO_Central.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IDA:ComplexPortal.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR InterPro; IPR039295; MSB2.
DR PANTHER; PTHR35778; PTHR35778; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1306
FT /note="Signaling mucin MSB2"
FT /id="PRO_0000096589"
FT TOPO_DOM 22..1185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1186..1206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1207..1306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 698..714
FT /note="1"
FT REPEAT 715..731
FT /note="2"
FT REPEAT 732..748
FT /note="3"
FT REPEAT 749..765
FT /note="4"
FT REPEAT 766..782
FT /note="5"
FT REPEAT 783..799
FT /note="6"
FT REPEAT 800..816
FT /note="7"
FT REGION 248..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..816
FT /note="7 X 17 AA tandem repeats"
FT REGION 709..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 859
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1049
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1306 AA; 133115 MW; 67D5D984D5CA4A6D CRC64;
MQFPFACLLS TLVISGSLAR ASPFDFIFGN GTQQAQSQSE SQGQVSFTNE ASQDSSTTSL
VTAYSQGVHS HQSATIVSAT ISSLPSTWYD ASSTSQTSVS YASQESDYAV NQNSWSASTN
QLPSTSTTSY YAPTFSTSAD FAASSVNAAS DVSTASVPID TSANSIPFTT TSNIETTTSA
PLTSDTPLIS TSTMSAADNV FSSANPISAS LTTTDSSESF DQTSTAGAIP VQSSADFSSS
SEILVQSSAD FSSPSSPTTT DISLSAAPLQ TSESSSFTTA SAALPVSSTD VDGSSASPVV
SMSAAGQIAS SSSTDNPTMS ETFSLTSTEV DGSDVSSTVS ALLSAPFLQT STSNSFSIVS
PSVSFVPSQS SSDVASSSTA NVVSSSFSDI PPQTSTSGSV VSVAQSASAL AFQSSTEVYG
ASASSTMSSL LSTTSLQSTT LDSSSLASSS ASSSDLTDYG VSSTASIPLL SASEQASTSS
SFSVVSPSVS FVPSQSSSDV ASTSAPSVVS SSFSYTSLQA GGSSMTNPSS STIVYSSSTG
SSEESAASTA SATLSGSSST YMAGNLQSQP PSTSSLLSES QATSTSAVLA SSSVSTTSPY
TTAGGASTEA SSLISSTSAE TSQVSYSQST TALQTSSFAS SSTTEGSETS SQGFSTSSVL
VQMPSSISSE FSPSQTTTQM NSASSSSQYT ISSTGILSQV SDTSVSYTTS SSSVSQVSDT
PVSYTTSSSS VSQVSDTPVS YTTSSSSVSQ VSDTPVSYTT SSSSVSQVSD TPVSYTTSSS
SVSQVSDTSV PSTSSRSSVS QVSDTPVPST SSRSSVSQTS SSLQPTTTSS QRFTISTHGA
LSESSSVSQQ ASEITSSINA TASEYHSIQT TAATQSTTLS FTDANSSSAS APLEVATSTP
TPSSKASSLL LTPSTSSLSQ VATNTNVQTS LTTESTTVLE PSTTNSSSTF SLVTSSDNNW
WIPTELITQA PEAASTASST VGGTQTMTLP HAIAAATQVP EPEGYTLITI GFKKALNYEF
VVSEPKSSAQ IFGYLPEALN TPFKNVFTNI TVLQIVPLQD DSLNYLVSVA EVYFPTAEIE
ELSNLITNSS SAFYTDGMGT AKSMAAMVDS SIPLTGLLHD SNSNSGGSSD GSSSSNSNSG
SSGSGSNSNS GVSSSSGNSY QDAGTLEYSS KSNSNVSTSS KSKKKIIGLV IGVVVGGCLY
ILFMIFAFKY IIRRRIQSQE IIKNPEISSI SSSEFGGEKN YNNEKRMSVQ ESITQSMRIQ
NWMDDSYYGH GLTNNDSTPT RHNTSSSIPK ISRPIASQNS LGWNEV
