ID   SBE22_YEAS7             Reviewed;         852 AA.
AC   A6ZT11;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Protein SBE22;
GN   Name=SBE22; ORFNames=SCY_2495;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SBE2 family. {ECO:0000305}.
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DR   EMBL; AAFW02000082; EDN62342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZT11; -.
DR   PRIDE; A6ZT11; -.
DR   EnsemblFungi; EDN62342; EDN62342; SCY_2495.
DR   HOGENOM; CLU_019068_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR031403; Sbe2/Sbe22.
DR   Pfam; PF17076; SBE2; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Cytoplasm; Golgi apparatus;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN           1..852
FT                   /note="Protein SBE22"
FT                   /id="PRO_0000320510"
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:0000250|UniProtKB:P38814"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38814"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38814"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38814"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38814"
SQ   SEQUENCE   852 AA;  96397 MW;  9C2EF34484022FF7 CRC64;
     MTSIQERGTS AHLHSLKEGE ASDRSSEMLP KQRSIIGSHV QRPPSQTTLG RSRAGSNTMN
     KVSGLDIARR PSENLLSNMN CSDNGNGGNM LNSFVNSALP PPKVNPAQTR RERPASNSSI
     GTKTTEVFSS TSASSSLGDT SDEGEGSDAD KSKINTFPSI LMEKATQGRG ANGNGMRSAS
     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