SOG2_YEAST
ID SOG2_YEAST Reviewed; 791 AA.
AC Q08817; D6W348;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Leucine-rich repeat-containing protein SOG2;
GN Name=SOG2 {ECO:0000312|SGD:S000005880}; OrderedLocusNames=YOR353C;
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] {ECO:0000312|EMBL:CAA99682.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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] {ECO:0000269|PubMed:12972564}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12972564; DOI=10.1091/mbc.e03-01-0018;
RA Nelson B., Kurischko C., Horecka J., Mody M., Nair P., Pratt L.,
RA Zougman A., McBroom L.D.B., Hughes T.R., Boone C., Luca F.C.;
RT "RAM: a conserved signaling network that regulates Ace2p transcriptional
RT activity and polarized morphogenesis.";
RL Mol. Biol. Cell 14:3782-3803(2003).
RN [4] {ECO:0000269|PubMed:12972564}
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 [5] {ECO:0000269|PubMed:12972564}
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, 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).
CC -!- FUNCTION: Required for proper cell morphogenesis and cell separation
CC after mitosis. Functions in the RAM (regulation of ACE2 activity and
CC cellular morphogenesis) signaling network and is required for proper
CC ACE2 localization and CBK1 kinase activity.
CC {ECO:0000269|PubMed:12972564}.
CC -!- INTERACTION:
CC Q08817; P32464: HYM1; NbExp=3; IntAct=EBI-30849, EBI-8859;
CC Q08817; P38692: KIC1; NbExp=5; IntAct=EBI-30849, EBI-12253;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12972564,
CC ECO:0000269|PubMed:14562095}. Note=Localizes to cortical sites of
CC growth during both budding and mating pheromone response. Localized
CC prominently to incipient bud sites and small buds and weakly to the
CC cortex and bud necks of large budded cells. Also localized to the
CC growing tips of mating projections.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z75261; CAA99682.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11114.1; -; Genomic_DNA.
DR PIR; S67265; S67265.
DR RefSeq; NP_014998.3; NM_001183773.3.
DR AlphaFoldDB; Q08817; -.
DR SMR; Q08817; -.
DR BioGRID; 34738; 304.
DR DIP; DIP-1998N; -.
DR IntAct; Q08817; 41.
DR MINT; Q08817; -.
DR STRING; 4932.YOR353C; -.
DR iPTMnet; Q08817; -.
DR MaxQB; Q08817; -.
DR PaxDb; Q08817; -.
DR PRIDE; Q08817; -.
DR EnsemblFungi; YOR353C_mRNA; YOR353C; YOR353C.
DR GeneID; 854535; -.
DR KEGG; sce:YOR353C; -.
DR SGD; S000005880; SOG2.
DR VEuPathDB; FungiDB:YOR353C; -.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_335290_0_0_1; -.
DR InParanoid; Q08817; -.
DR OMA; KEEYWAI; -.
DR BioCyc; YEAST:G3O-33824-MON; -.
DR PRO; PR:Q08817; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08817; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:SGD.
DR GO; GO:0007165; P:signal transduction; IMP:SGD.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR019487; RAM_signalling_pathway_SOG2.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF10428; SOG2; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..791
FT /note="Leucine-rich repeat-containing protein SOG2"
FT /id="PRO_0000270575"
FT REPEAT 43..64
FT /note="LRR 1"
FT REPEAT 67..88
FT /note="LRR 2"
FT REPEAT 90..111
FT /note="LRR 3"
FT REPEAT 113..134
FT /note="LRR 4"
FT REPEAT 138..159
FT /note="LRR 5"
FT REPEAT 163..183
FT /note="LRR 6"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 791 AA; 87326 MW; B0EA559AA4F66199 CRC64;
MVATSSKRTL DPKEEHLPAD KTSTNSSNTI ISELATQEKS SSSGTTLKLI ALNIKSISDE
DVGYIQNVER LSLRKNHLTS LPASFKRLSR LQYLDLHNNN FKEIPYILTQ CPQLEILDLS
SNEIEALPDE ISSFWQDNIR VLSLKDNNVT SIRNLKSITK LNKLSILDLE DNKIPKEELD
QVQSYTPFHT GIPKEEYWAI AISRYLKDHP NLPTPEPKIS RAAKRMGFIN TNLSNGAMNE
NNIISLAPSA NTTISASTAM VSSNQTSATS FSGTVNAESE QSGAVNGTEL YNHTKYNDYF
KRLSILPEES MSNGHQKISH AELVVSCRKL LFSFTECQQA IRKIASFCKE KAVAVNVVSL
LYSVRSHTDN LVEVLQQTEN EDESHDQALI KLCLTIITNF KQIITLLRKN FEIFFKEDDL
CFIRMFYMTL MCAYMEMYNA WSFIKEDDQV SGSASKAPKK HSFSRHETSS SSITSGGGPA
ASTTSTHCSG NIKLLPKTRS TRTPSASALL SNSNILTGDT TAVPLLSPNL NGAHTHGPIL
GHQNAISNGS SQTNMNEVKT TSDTIPRQQL LQHNKSISDS KKESQAHEPK QHPVMTSSII
NASNSNNVSN VNITPPPMNG GGAANSSANV VETNIDIQLY QTLSTVVKMV SVVYNQLTSE
ISKIAIASTM GKQILTDSLA PKIRDLTETC RQAMDLSKQL NERLNVLIPN DSNSEKYLTS
LEKLKTWEIM NSFLKVIISI LANTKIVMSD VPNLNELRPN LANLAKITKD VTVILDLSSY
KAVSVSANSP E
