SPO20_YEAST
ID SPO20_YEAST Reviewed; 397 AA.
AC Q04359; D6VZJ1; Q6B245;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Sporulation-specific protein 20;
GN Name=SPO20; OrderedLocusNames=YMR017W; ORFNames=YM9711.05;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP DOMAIN.
RX PubMed=9096343; DOI=10.1073/pnas.94.7.3046;
RA Weimbs T., Low S.H., Chapin S.J., Mostov K.E., Bucher P., Hofmann K.;
RT "A conserved domain is present in different families of vesicular fusion
RT proteins: a new superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3046-3051(1997).
RN [5]
RP FUNCTION.
RX PubMed=9425151; DOI=10.1083/jcb.140.1.29;
RA Neiman A.M.;
RT "Prospore membrane formation defines a developmentally regulated branch of
RT the secretory pathway in yeast.";
RL J. Cell Biol. 140:29-37(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SSO1 AND SNC2.
RX PubMed=10924463; DOI=10.1093/genetics/155.4.1643;
RA Neiman A.M., Katz L., Brennwald P.J.;
RT "Identification of domains required for developmentally regulated SNARE
RT function in Saccharomyces cerevisiae.";
RL Genetics 155:1643-1655(2000).
RN [7]
RP FUNCTION, DOMAINS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-66; LEU-67;
RP LYS-68; LEU-70; ARG-71 AND LYS-73.
RX PubMed=14742704; DOI=10.1091/mbc.e03-11-0798;
RA Nakanishi H., de los Santos P., Neiman A.M.;
RT "Positive and negative regulation of a SNARE protein by control of
RT intracellular localization.";
RL Mol. Biol. Cell 15:1802-1815(2004).
CC -!- FUNCTION: Required to maintain the prospore membrane to the nucleus
CC during sporulation in order to capture the daughter nuclei and form the
CC spores. Mediates the fusion of exocytic vesicles with the plasma
CC membrane during sporulation through its interactions with the t-SNARE
CC SSO1 and v-SNARE SNC2. {ECO:0000269|PubMed:10924463,
CC ECO:0000269|PubMed:14742704, ECO:0000269|PubMed:9425151}.
CC -!- SUBUNIT: Interacts with the t-SNARE SSO1 and the v-SNARE SNC2.
CC {ECO:0000269|PubMed:10924463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Prospore membrane. Note=Membrane-
CC associated to the plasma during vegetative growth and prospore membrane
CC associated during sporulation.
CC -!- DOMAIN: The inhibitory region sequesters the protein in the nucleus.
CC -!- DOMAIN: The positive regulatory region is essential and contains an
CC amphipathic helix with hydrophobic and positive charged faces involved
CC in the localization of the protein to the membranes through its binding
CC to phospholipids.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; Z49211; CAA89119.1; -; Genomic_DNA.
DR EMBL; AY692885; AAT92904.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09915.1; -; Genomic_DNA.
DR PIR; S54018; S54018.
DR RefSeq; NP_013730.1; NM_001182513.1.
DR AlphaFoldDB; Q04359; -.
DR SMR; Q04359; -.
DR BioGRID; 35188; 54.
DR ComplexPortal; CPX-5464; Vesicular SNARE complex SSO1-SPO20-SNC1.
DR ComplexPortal; CPX-5466; Vesicular SNARE complex SSO1-SPO20-SNC2.
DR DIP; DIP-4511N; -.
DR IntAct; Q04359; 1.
DR STRING; 4932.YMR017W; -.
DR iPTMnet; Q04359; -.
DR PaxDb; Q04359; -.
DR PRIDE; Q04359; -.
DR EnsemblFungi; YMR017W_mRNA; YMR017W; YMR017W.
DR GeneID; 855031; -.
DR KEGG; sce:YMR017W; -.
DR SGD; S000004619; SPO20.
DR VEuPathDB; FungiDB:YMR017W; -.
DR eggNOG; KOG3065; Eukaryota.
DR HOGENOM; CLU_694853_0_0_1; -.
DR InParanoid; Q04359; -.
DR OMA; FRMDNCS; -.
DR BioCyc; YEAST:G3O-32723-MON; -.
DR Reactome; R-SCE-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR PRO; PR:Q04359; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04359; protein.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0005484; F:SNAP receptor activity; IPI:SGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IC:ComplexPortal.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0043934; P:sporulation; IDA:ComplexPortal.
DR GO; GO:0006906; P:vesicle fusion; IDA:ComplexPortal.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Membrane; Reference proteome; Sporulation.
FT CHAIN 1..397
FT /note="Sporulation-specific protein 20"
FT /id="PRO_0000213614"
FT DOMAIN 330..392
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..50
FT /note="Inhibitory region"
FT REGION 51..95
FT /note="Positive regulatory region"
FT COMPBIAS 8..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 66
FT /note="K->E: Strong decrease of the sporulation rate and
FT loss of lipid binding; when associated with E-68; E-71 and
FT E-73."
FT /evidence="ECO:0000269|PubMed:14742704"
FT MUTAGEN 67
FT /note="L->P,N: Strong decrease of the sporulation rate."
FT /evidence="ECO:0000269|PubMed:14742704"
FT MUTAGEN 68
FT /note="K->E: Strong decrease of the sporulation rate and
FT loss of lipid binding; when associated with E-66; E-71 and
FT E-73."
FT /evidence="ECO:0000269|PubMed:14742704"
FT MUTAGEN 70
FT /note="L->N: Strong decrease of the sporulation rate."
FT /evidence="ECO:0000269|PubMed:14742704"
FT MUTAGEN 71
FT /note="R->E: Strong decrease of the sporulation rate and
FT loss of lipid binding; when associated with E-66; E-68 and
FT E-73."
FT /evidence="ECO:0000269|PubMed:14742704"
FT MUTAGEN 73
FT /note="K->E: Strong decrease of the sporulation rate and
FT loss of lipid binding; when associated with E-66; E-68 and
FT E-71."
FT /evidence="ECO:0000269|PubMed:14742704"
FT CONFLICT 59
FT /note="R -> K (in Ref. 3; AAT92904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 46621 MW; CFE6769B82725B49 CRC64;
MGFRKILASK SHHSRHHNQH HKNLKLQNHR YVLISNITGS HETKYLSPFR MDNCSGSRRR
DRLHVKLKSL RNKIHKQLHP NCRFDDATKT SDDKCVSYEV PERDGLATIS LEEVFPKSNR
CQIPEENLGE TDSVIHRDLG NFANENDYPQ WRKVESQYNL ENVQPEEDEI VDRLRSEIRS
TKLKSVKTTS RTLEKAIEAR CTGKRVLQQL SCQSNQLTKI ESNCDMLKIQ SNVADRKIDE
LAHENRSLLA LKSPNPFRKK REREKRDQIY NLKLKHRHLQ QETMKRAQDS DKNLAINLSS
EYGRYGQGVE RQRILRDAQK YQFEADEEDN QMEIDLYGNL EQIKAVSGDL KIMAHAFGRE
FEAQNTRMFD IENNVQQADN ALQAKRYRLE KVIGKRW
