SBE2_YEAST
ID SBE2_YEAST Reviewed; 864 AA.
AC P42223; D6VSY1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein SBE2;
DE AltName: Full=Suppressor of BEM4 protein 2;
GN Name=SBE2; OrderedLocusNames=YDR351W; ORFNames=D9476.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-864.
RA Nishimura K., Toh-e A., Matsui Y.;
RT "Yeast Saccharomyces cerevisiae genes, SBE2 and SBE22, are required for bud
RT growth.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10679005; DOI=10.1091/mbc.11.2.435;
RA Santos B., Snyder M.;
RT "Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell
RT wall formation.";
RL Mol. Biol. Cell 11:435-452(2000).
RN [5]
RP FUNCTION.
RX PubMed=12045225; DOI=10.1242/jcs.115.12.2549;
RA Rodriguez-Pena J.M., Rodriguez C., Alvarez A., Nombela C., Arroyo J.;
RT "Mechanisms for targeting of the Saccharomyces cerevisiae GPI-anchored cell
RT wall protein Crh2p to polarised growth sites.";
RL J. Cell Sci. 115:2549-2558(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-532, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-83 AND SER-532, 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: With SBE22, is involved in cell wall integrity and polarity
CC processes like bud growth, through the transport of CHS3 and UTR2 to
CC sites of growth. {ECO:0000269|PubMed:10679005,
CC ECO:0000269|PubMed:12045225}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10679005}.
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DR EMBL; U28372; AAB64787.1; -; Genomic_DNA.
DR EMBL; D50084; BAA08788.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12191.1; -; Genomic_DNA.
DR PIR; S61148; S61148.
DR RefSeq; NP_010638.3; NM_001180659.3.
DR AlphaFoldDB; P42223; -.
DR BioGRID; 32408; 55.
DR DIP; DIP-4091N; -.
DR IntAct; P42223; 4.
DR MINT; P42223; -.
DR STRING; 4932.YDR351W; -.
DR iPTMnet; P42223; -.
DR MaxQB; P42223; -.
DR PaxDb; P42223; -.
DR PRIDE; P42223; -.
DR EnsemblFungi; YDR351W_mRNA; YDR351W; YDR351W.
DR GeneID; 851953; -.
DR KEGG; sce:YDR351W; -.
DR SGD; S000002759; SBE2.
DR VEuPathDB; FungiDB:YDR351W; -.
DR eggNOG; ENOG502QR4N; Eukaryota.
DR GeneTree; ENSGT00940000176432; -.
DR HOGENOM; CLU_019068_0_0_1; -.
DR InParanoid; P42223; -.
DR OMA; SSTRPIW; -.
DR BioCyc; YEAST:G3O-29905-MON; -.
DR PRO; PR:P42223; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P42223; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR031403; Sbe2/Sbe22.
DR Pfam; PF17076; SBE2; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Golgi apparatus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..864
FT /note="Protein SBE2"
FT /id="PRO_0000097602"
FT REGION 16..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 864 AA; 98971 MW; 9491912ECF6F9406 CRC64;
MTARRLINIV PNTSKLDPLK EEDSTHLKQN QPKKFSTKEL MLSEYTERKS CSLPLSKSRS
GSSASSSTTG SNGKNIGTRR PSSNLDFNFA SQDVVKNVLG NNNPHVPTAK CIRPISDDSI
GTSSTEIFSS SHSNTTSDSL CTSDISSEEG EIANSKMEDN CFFKSMREAD HRSNITPLKK
SRPGSILQKT RTASSADKTI CSMSTITTCI PSRQNSVSTP KLSRTVGLPG SSNTTNSIAA
SQTSFISEND SPLKHHCMST ATIQEPKLMP ITKTPYVHSN STSVILPYKT TQLTPSQRYR
LRKEQNDQSL RKAIKMKEKF YEDQDVNLEL QEGDVDGSLI WNIPMASLST SSFLTLSKFN
RKEMSLDSAR GDEEILIQEN NCEGKQHSSS ALCVDKTFHQ VHSTRKHTSN SSNTLKESCL
DYKELPPTCI PGISPVSDSQ YIQDTMKNLS QIYLHSSEKI SKSILSGRSR SVQSLPLEFK
EASSQGMEDL MLVSEDKLKA VSHFRPSWLP PKDFKERKLQ DKQIYKNIDL ASMEELQKNK
ERDEKAKKNE QNKVKFQHLL DRGITRNSSL SELKKIIWET PLISKVRLQI YSQLLQSDNC
LITKCFIESF EEVMQLLNKM DFPKDKEFEI RQLIEHDVQE KVFYKNGTDK QVVSDLMLLL
QLKSISQQGL VTGDEMLFYH FLTDQSFGTL KETWEMVNLI QMTCFSEICK EKYDSRILNP
RGIVAHLLRK DEFKNEFNGG CLNSNTWWNI LQRMDHKLFM WVMDVIIVHN GQNFANYPVK
MEIFKDKVWE YYRSKKVIVN YKILVSLTVN VLLNYHFGYD NLKHLSDLDD KHFCIPLYTE
DSIEEENLNN IFTKWWLHYY RKLR
