SBE22_YEAST
ID SBE22_YEAST Reviewed; 852 AA.
AC P38814; D3DL53;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein SBE22;
GN Name=SBE22; OrderedLocusNames=YHR103W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION.
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 [4]
RP FUNCTION.
RX PubMed=12121919; DOI=10.1128/aac.46.8.2462-2469.2002;
RA Osherov N., May G.S., Albert N.D., Kontoyiannis D.P.;
RT "Overexpression of Sbe2p, a Golgi protein, results in resistance to
RT caspofungin in Saccharomyces cerevisiae.";
RL Antimicrob. Agents Chemother. 46:2462-2469(2002).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-520, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-459; SER-517 AND
RP SER-520, AND 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 SBE2, 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, ECO:0000269|PubMed:12121919}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi
CC apparatus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SBE2 family. {ECO:0000305}.
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DR EMBL; U00059; AAB68859.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06797.1; -; Genomic_DNA.
DR PIR; S48945; S48945.
DR RefSeq; NP_011971.1; NM_001179233.1.
DR AlphaFoldDB; P38814; -.
DR BioGRID; 36536; 52.
DR DIP; DIP-5948N; -.
DR IntAct; P38814; 2.
DR MINT; P38814; -.
DR STRING; 4932.YHR103W; -.
DR iPTMnet; P38814; -.
DR MaxQB; P38814; -.
DR PaxDb; P38814; -.
DR PRIDE; P38814; -.
DR EnsemblFungi; YHR103W_mRNA; YHR103W; YHR103W.
DR GeneID; 856503; -.
DR KEGG; sce:YHR103W; -.
DR SGD; S000001145; SBE22.
DR VEuPathDB; FungiDB:YHR103W; -.
DR eggNOG; ENOG502QR4N; Eukaryota.
DR GeneTree; ENSGT00940000176432; -.
DR HOGENOM; CLU_019068_0_0_1; -.
DR InParanoid; P38814; -.
DR OMA; WWNILER; -.
DR BioCyc; YEAST:G3O-31148-MON; -.
DR PRO; PR:P38814; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38814; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; Cytoplasm; Golgi apparatus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..852
FT /note="Protein SBE22"
FT /id="PRO_0000202909"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 852 AA; 96398 MW; 4F561FD7EDD06862 CRC64;
MTSIQERGTS AHLHSLKEGE ASDRSSEMLP KQRSIIGSHV QRPPSQTTLG RSRAGSNTMN
KVSGLDIARR PSENLLSNMN CSDNGNGGNM LNSFVNSALP PPKVNPAQTR RERPASNSSI
GTKTTEVFSS TSASSSLGDT SDEGEGSDAD KSKINTFPSI LMEKATQGRG ADGNGMRSAS
NNTIVEATTD GSKMALQKSM SFDDTAAEKT MNKSRHSYQE QFSSKKSQSS LLNSKQRSRA
KSQTCSSTGY NNSSILKTFG ISSKISNSSD RIEASSLEFN VPSQKPLNCK PLTPSQKYRL
RKEQSEMNLR NTIKRKEKFY DSQEQILELQ EGDVDDSLIW NVPMASLSTN SFLASAKPDD
MNNLAGKNDL SEYTGGLVND NSEISYTKQN HRYSNISFAS TTSNASLLDF NEMPTSPIPG
LNKVTDFQFI QDTTKSLASV YLHSSNRLSR SKLSERTKSS DFLPIELKEA QNQGMEDLIL
VSENKLDVVS HSRPSWLPPK DRQEKKLHER QINKSMSVAS LDQLGKNKDR EEKLIRDETN
RQKYVLLLDR DITRNSSLQS LSKMVWDTPF SDETRSTIYS EILQSKTRFI TKNYIQPFHE
LQELLTKMGD FPKNKEIEIS QLIETSLRRK VSGLHDICPD LMLLLKIKSI SSQGIVTGDE
LLFHHFLVSE SFQNLGLNEI WNIVNLVQMT CFNDLCKEKF DAKVLERKGV VAGYLSQNEE
FKDEFNTECI NSTTWWNILE RIDHKLFMWI MDIIVVNNSQ SYKNSPINED EFVNKDWEYY
RSKKVVINYK ILISFALNVL LNYHFGFTDL RSLCNVNDQR FCIPVFINDE FVDADTVNAV
FIKKWAHYYK KF
