SKG1_YEAST
ID SKG1_YEAST Reviewed; 355 AA.
AC P36169; D6VXG1; Q86ZT0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Suppressor of lethality of KEX2 GAS1 double null mutant protein 1;
GN Name=SKG1; OrderedLocusNames=YKR100C; ORFNames=YKR099C-A;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=15645486; DOI=10.1002/yea.1206;
RA Tomishige N., Noda Y., Adachi H., Shimoi H., Yoda K.;
RT "SKG1, a suppressor gene of synthetic lethality of kex2Deltagas1Delta
RT mutations, encodes a novel membrane protein that affects cell wall
RT composition.";
RL Yeast 22:141-155(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-266.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP 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: Plays a role in cell wall integrity. Affects the cell wall
CC polymer composition in the growing region of the cell.
CC {ECO:0000269|PubMed:15645486}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane
CC protein; Cytoplasmic side. Bud membrane; Single-pass type III membrane
CC protein; Cytoplasmic side. Note=Localizes on the inner surface of the
CC plasma membrane at the bud and in the daughter cell. Localizes at an
CC incipient bud site in the cells with emerging buds, a bud tip in
CC small- or medium-budded cells, and a cell periphery in large-budded
CC cells.
CC -!- SIMILARITY: Belongs to the SKG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82180.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z28325; CAA82180.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260883; AAP21751.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09251.1; -; Genomic_DNA.
DR PIR; S38179; S38179.
DR RefSeq; NP_013026.2; NM_001179890.1.
DR AlphaFoldDB; P36169; -.
DR BioGRID; 34231; 78.
DR DIP; DIP-4605N; -.
DR IntAct; P36169; 1.
DR MINT; P36169; -.
DR STRING; 4932.YKR100C; -.
DR iPTMnet; P36169; -.
DR MaxQB; P36169; -.
DR PaxDb; P36169; -.
DR PRIDE; P36169; -.
DR EnsemblFungi; YKR100C_mRNA; YKR100C; YKR100C.
DR GeneID; 853975; -.
DR KEGG; sce:YKR100C; -.
DR SGD; S000001808; SKG1.
DR VEuPathDB; FungiDB:YKR100C; -.
DR eggNOG; ENOG502RZI6; Eukaryota.
DR GeneTree; ENSGT00940000176519; -.
DR HOGENOM; CLU_079389_0_0_1; -.
DR InParanoid; P36169; -.
DR OMA; KYYVPAY; -.
DR BioCyc; YEAST:G3O-32062-MON; -.
DR PRO; PR:P36169; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36169; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0033101; C:cellular bud membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Membrane; Phosphoprotein;
KW Reference proteome; 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_0000203230"
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 278..304
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 COMPBIAS 289..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 355 AA; 39830 MW; D3BD732250D825FF CRC64;
MTASTSVAVG CAVGIPVGVG IIIAVCFWFN LQKRYKREEQ DDRELERAIY DESGFVSFDN
FGPLRDSKDE AALASSELKN PDHTSGSSEG SAHPEEKDGK SRDQEKPLGK KNSKYYVPAY
RRKINLLQVR NNNYGNNARQ KSVVDLPSIN NSSNVSLSSS QRHITKRQIS VYDQMVPVIS
DEGPNFFADP SSDTNTSNDQ NKASMIELKH NTRQSSNENL IRNLQNQDFG SYYPRRASSS
FLNGNISNAS FHTRNSSITS VNKRDALEDV FATPKSAAQS QLPNTFDKDN EGMDADHSVK
DSRSAITDKD KDLYKLQNNY DVGNIGEIAE EDQYENEFTN YSQSKREFIE SLRPK
