ID   SKG1_YEAS6              Reviewed;         355 AA.
AC   B5VMP1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Suppressor of lethality of KEX2 GAS1 double null mutant protein 1;
GN   Name=SKG1; ORFNames=AWRI1631_113220;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- FUNCTION: Plays a role in cell wall integrity. Affects the cell wall
CC       polymer composition in the growing region of the cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bud
CC       membrane {ECO:0000250}; Single-pass type III membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes on the
CC       inner surface of the plasma membrane at the bud and in the daughter
CC       cell. Localizes at an incipient bud site in the cells with emerging
CC       buds, a bud tip in small- or medium-budded cells, and a cell periphery
CC       in large-budded cells. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SKG1 family. {ECO:0000305}.
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DR   EMBL; ABSV01001521; EDZ70802.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VMP1; -.
DR   Proteomes; UP000008988; Unassembled WGS sequence.
DR   GO; GO:0033101; C:cellular bud membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Membrane; Phosphoprotein;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..355
FT                   /note="Suppressor of lethality of KEX2 GAS1 double null
FT                   mutant protein 1"
FT                   /id="PRO_0000399674"
FT   TOPO_DOM        1..8
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          70..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P36169"
FT   MOD_RES         273
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P36169"
SQ   SEQUENCE   355 AA;  39866 MW;  D576DBDF794C35CA CRC64;
     MTASTSVAVG CAVGIPVGVG IIIAVCFWFN LQKRYKREEQ DDRELERAIY DESGFVSFDN
     FGPLRDSKDE AALASSELKN PDHTSGSSEG SAHPEEKDGK SRDQEKPLGK KNSKYYVPAY
     RRKINLLQVR NNNYGNNARQ KSVVDLPSIN NSSNVSLSSS QRHITKRQIS VYDQMVPVIS
     DEGPKFFADP SSDTNTSNDQ NKASMIELKH NTRQSINENL IRKLQNQDFG SYYPRRASSS
     FLNGNISNAS FHTRNSSITS VNKRDALEDV FATPKSAAQS QLPNTFDKDN EGIDADHSVK
     DSRSAITDKD KDIYKLQNNY DVGNIGEIAE EDQYENEFTN YSQSKREFIE SLRPK