SPS2_YEAST
ID SPS2_YEAST Reviewed; 502 AA.
AC P08459; D6VTE2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Sporulation-specific protein 2;
DE Flags: Precursor;
GN Name=SPS2; OrderedLocusNames=YDR522C; ORFNames=D9719.26;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-502.
RX PubMed=3023934; DOI=10.1128/mcb.6.7.2443-2451.1986;
RA Percival-Smith A., Segall J.;
RT "Characterization and mutational analysis of a cluster of three genes
RT expressed preferentially during sporulation of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 6:2443-2451(1986).
RN [4]
RP FUNCTION.
RX PubMed=3302678; DOI=10.1128/mcb.7.7.2484-2490.1987;
RA Percival-Smith A., Segall J.;
RT "Increased copy number of the 5' end of the SPS2 gene inhibits sporulation
RT of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:2484-2490(1987).
RN [5]
RP FUNCTION.
RX PubMed=7565676; DOI=10.1128/mcb.15.10.5279;
RA Sia R.A., Mitchell A.P.;
RT "Stimulation of later functions of the yeast meiotic protein kinase Ime2p
RT by the IDS2 gene product.";
RL Mol. Cell. Biol. 15:5279-5287(1995).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=15590821; DOI=10.1128/ec.3.6.1464-1475.2004;
RA Coluccio A., Bogengruber E., Conrad M.N., Dresser M.E., Briza P.,
RA Neiman A.M.;
RT "Morphogenetic pathway of spore wall assembly in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 3:1464-1475(2004).
CC -!- FUNCTION: Involved in middle stages of meiosis. Redundant with SPS22
CC for the organization of the beta-glucan layer of the spore wall.
CC {ECO:0000269|PubMed:15590821, ECO:0000269|PubMed:3302678,
CC ECO:0000269|PubMed:7565676}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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DR EMBL; U33057; AAB64962.1; -; Genomic_DNA.
DR EMBL; M13629; AAA35080.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12352.1; -; Genomic_DNA.
DR PIR; S69578; S69578.
DR RefSeq; NP_010810.1; NM_001180830.1.
DR AlphaFoldDB; P08459; -.
DR SMR; P08459; -.
DR BioGRID; 32572; 114.
DR DIP; DIP-7764N; -.
DR IntAct; P08459; 4.
DR STRING; 4932.YDR522C; -.
DR PaxDb; P08459; -.
DR PRIDE; P08459; -.
DR EnsemblFungi; YDR522C_mRNA; YDR522C; YDR522C.
DR GeneID; 852134; -.
DR KEGG; sce:YDR522C; -.
DR SGD; S000002930; SPS2.
DR VEuPathDB; FungiDB:YDR522C; -.
DR eggNOG; ENOG502QT4Q; Eukaryota.
DR GeneTree; ENSGT00940000176339; -.
DR HOGENOM; CLU_035846_2_1_1; -.
DR InParanoid; P08459; -.
DR OMA; RWVNLTT; -.
DR BioCyc; YEAST:G3O-30038-MON; -.
DR PRO; PR:P08459; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P08459; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR Gene3D; 3.80.20.20; -; 1.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Meiosis; Membrane;
KW Reference proteome; Signal; Sporulation.
FT SIGNAL 1..56
FT /evidence="ECO:0000255"
FT CHAIN 57..475
FT /note="Sporulation-specific protein 2"
FT /id="PRO_0000033195"
FT PROPEP 476..502
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000277471"
FT REGION 441..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 475
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 203
FT /note="P -> L (in Ref. 1; AAA35080)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="I -> S (in Ref. 1; AAA35080)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="V -> G (in Ref. 1; AAA35080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55939 MW; 11F9EFB11CD4D59C CRC64;
MPIWKTQTFF TSISVIQIVN KETKVSTKKE KDSMLNQLNT ILRFLFLFLQ LIKSSAAVEP
NGGPNILDHN IMLVNTNATI PKKEQTDFEV ISPTKQTQVD EDCKKGLYHI ENAGNLIELQ
AKCWKVVGNI EISSNYSGSL IDLGLIREIE GDLIIKNNKH IFRIQGYNLE SLGKLELDSL
TSFVSLDFPA LKEVETVDWR VLPILSSVVI NGNIKKIKNI IISDTALTSI DYFNNVKKVD
IFNINNNRFL ENLFASLESV TKQLTVHSNA KELELDLSNL HTVENMTIKD VSEIKLAKLS
SVNSSLEFIE NQFSSLELPL LAKVQGTLGL IDNKNLKKLN FSNATDIQGG LMIANNTELA
KIDFFPKLRQ IGGAIYFEGS FDKIDLPELK LVKGSAYIKS SSEELNCEEF TSPKAGRSII
RGGKIECTSG MKSKMLNVDE EGNVLGKQET DNDNGKKEKG KNGAKSQGSS KKMENSAPKN
IFIDAFKMSV YAVFTVLFSI IF
