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Signaling mucin MSB2 (Multicopy suppressor of bud emergence 2) (Osmosensor MSB2)

 MSB2_YEAST              Reviewed;        1306 AA.
P32334; D6VUF0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Signaling mucin MSB2;
AltName: Full=Multicopy suppressor of bud emergence 2;
AltName: Full=Osmosensor MSB2;
Flags: Precursor;
Name=MSB2; OrderedLocusNames=YGR014W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=1514328; DOI=10.1002/yea.320080409;
Bender A., Pringle J.R.;
"A Ser/Thr-rich multicopy suppressor of a cdc24 bud emergence
defect.";
Yeast 8:315-323(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9290212;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1077::AID-YEA152>3.3.CO;2-P;
Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
chromosome VII.";
Yeast 13:1077-1090(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=2690082; DOI=10.1073/pnas.86.24.9976;
Bender A., Pringle J.R.;
"Multicopy suppression of the cdc24 budding defect in yeast by CDC42
and three newly identified genes including the ras-related gene
RSR1.";
Proc. Natl. Acad. Sci. U.S.A. 86:9976-9980(1989).
[6]
FUNCTION.
PubMed=12052881; DOI=10.1128/MCB.22.13.4739-4749.2002;
O'Rourke S.M., Herskowitz I.;
"A third osmosensing branch in Saccharomyces cerevisiae requires the
Msb2 protein and functions in parallel with the Sho1 branch.";
Mol. Cell. Biol. 22:4739-4749(2002).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC42 AND SHO1.
PubMed=15256499; DOI=10.1101/gad.1178604;
Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
"A signaling mucin at the head of the Cdc42- and MAPK-dependent
filamentous growth pathway in yeast.";
Genes Dev. 18:1695-1708(2004).
[9]
FUNCTION.
PubMed=15713635; DOI=10.1128/MCB.25.5.1793-1803.2005;
Flatauer L.J., Zadeh S.F., Bardwell L.;
"Mitogen-activated protein kinases with distinct requirements for Ste5
scaffolding influence signaling specificity in Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 25:1793-1803(2005).
[10]
FUNCTION.
PubMed=19439450; DOI=10.1091/mbc.E08-07-0760;
Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
"The signaling mucins Msb2 and Hkr1 differentially regulate the
filamentation mitogen-activated protein kinase pathway and contribute
to a multimodal response.";
Mol. Biol. Cell 20:3101-3114(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1300, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Plasma membrane signaling mucin that promotes activation
of the MAPK for the filamentous growth pathway. Partially
redundant with the SHO1 osmosensing branch for the activation of
STE11. {ECO:0000269|PubMed:12052881, ECO:0000269|PubMed:1514328,
ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:15713635,
ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:2690082}.
-!- SUBUNIT: Interacts with CDC42 and SHO1.
{ECO:0000269|PubMed:15256499}.
-!- INTERACTION:
Q06810:OPY2; NbExp=3; IntAct=EBI-11328, EBI-2068557;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15256499};
Single-pass membrane protein {ECO:0000269|PubMed:15256499}.
Note=localized to polarized sites on the cell surface.
-!- PTM: O-glycosylated in the Ser/Thr-rich regions. {ECO:0000305}.
-!- MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the HKR1/MSB2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M77354; AAA34798.1; -; Genomic_DNA.
EMBL; Z72799; CAA96997.1; -; Genomic_DNA.
EMBL; BK006941; DAA08111.1; -; Genomic_DNA.
PIR; S25370; S25370.
RefSeq; NP_011528.3; NM_001181143.3.
ProteinModelPortal; P32334; -.
BioGrid; 33257; 78.
DIP; DIP-1455N; -.
IntAct; P32334; 14.
MINT; P32334; -.
STRING; 4932.YGR014W; -.
iPTMnet; P32334; -.
MaxQB; P32334; -.
PaxDb; P32334; -.
PRIDE; P32334; -.
EnsemblFungi; YGR014W; YGR014W; YGR014W.
GeneID; 852897; -.
KEGG; sce:YGR014W; -.
EuPathDB; FungiDB:YGR014W; -.
SGD; S000003246; MSB2.
GeneTree; ENSGT00770000121599; -.
InParanoid; P32334; -.
KO; K19849; -.
OMA; WIPTELI; -.
OrthoDB; EOG092C480G; -.
BioCyc; YEAST:G3O-30741-MONOMER; -.
PRO; PR:P32334; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IDA:SGD.
GO; GO:0005887; C:integral component of plasma membrane; IMP:SGD.
GO; GO:0030427; C:site of polarized growth; IDA:SGD.
GO; GO:0005034; F:osmosensor activity; IMP:SGD.
GO; GO:0000282; P:cellular bud site selection; IBA:GO_Central.
GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
GO; GO:0007232; P:osmosensory signaling pathway via Sho1 osmosensor; IGI:SGD.
GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycoprotein; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1306 Signaling mucin MSB2.
/FTId=PRO_0000096589.
TOPO_DOM 22 1185 Extracellular. {ECO:0000255}.
TRANSMEM 1186 1206 Helical. {ECO:0000255}.
TOPO_DOM 1207 1306 Cytoplasmic. {ECO:0000255}.
REPEAT 698 714 1.
REPEAT 715 731 2.
REPEAT 732 748 3.
REPEAT 749 765 4.
REPEAT 766 782 5.
REPEAT 783 799 6.
REPEAT 800 816 7.
REGION 698 816 7 X 17 AA tandem repeats.
COMPBIAS 37 956 Ser-rich.
COMPBIAS 1132 1150 Poly-Ser.
MOD_RES 1300 1300 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 859 859 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 885 885 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1049 1049 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1088 1088 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1175 1175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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