SSP1_YEAST
ID SSP1_YEAST Reviewed; 571 AA.
AC P38871; D3DLD2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sporulation-specific protein 1;
GN Name=SSP1; OrderedLocusNames=YHR184W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9372934; DOI=10.1128/mcb.17.12.7029;
RA Nag D.K., Koonce M.P., Axelrod J.;
RT "SSP1, a gene necessary for proper completion of meiotic divisions and
RT spore formation in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:7029-7039(1997).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, COMPOSITION OF A SPB
RP COMPLEX, AND INTERACTION WITH ADY3.
RX PubMed=11742972; DOI=10.1093/emboj/20.24.6946;
RA Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A.,
RA Shevchenko A., Knop M.;
RT "Prospore membrane formation linked to the leading edge protein (LEP) coat
RT assembly.";
RL EMBO J. 20:6946-6957(2001).
CC -!- FUNCTION: Involved in the pathway that organizes the shaping and sizing
CC of the prospore membrane (PSM) during sporulation. May be required for
CC the formation of ADY3 and DON1-containing protein coats at the leading
CC edge of the PSMs during meiosis II. {ECO:0000269|PubMed:11742972,
CC ECO:0000269|PubMed:9372934}.
CC -!- SUBUNIT: Interacts directly with ADY3. Probable component of a spindle
CC pole body (SPB) complex composed of ADY3, SSP1, DON1, MPC54,
CC SPO21/MPC70, NUD1 and CNM67. {ECO:0000269|PubMed:11742972}.
CC -!- INTERACTION:
CC P38871; Q07732: ADY3; NbExp=3; IntAct=EBI-24852, EBI-33406;
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000269|PubMed:11742972}.
CC Note=Localizes to precursors of the PSM and to the leading edge, which
CC cover the ring-shape opening of the PSMs during meiosis II. Some
CC fraction colocalizes with DON1.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Expressed from 3 to 9 hours
CC after induction of sporulation. Not expressed during mitosis.
CC {ECO:0000269|PubMed:9372934}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11742972}.
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DR EMBL; U00028; AAB68456.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06876.1; -; Genomic_DNA.
DR PIR; S46675; S46675.
DR RefSeq; NP_012054.1; NM_001179315.1.
DR AlphaFoldDB; P38871; -.
DR SMR; P38871; -.
DR BioGRID; 36617; 83.
DR DIP; DIP-1674N; -.
DR IntAct; P38871; 5.
DR MINT; P38871; -.
DR STRING; 4932.YHR184W; -.
DR MaxQB; P38871; -.
DR PaxDb; P38871; -.
DR PRIDE; P38871; -.
DR EnsemblFungi; YHR184W_mRNA; YHR184W; YHR184W.
DR GeneID; 856590; -.
DR KEGG; sce:YHR184W; -.
DR SGD; S000001227; SSP1.
DR VEuPathDB; FungiDB:YHR184W; -.
DR eggNOG; ENOG502RZY5; Eukaryota.
DR HOGENOM; CLU_478292_0_0_1; -.
DR InParanoid; P38871; -.
DR OMA; RIDCISA; -.
DR BioCyc; YEAST:G3O-31214-MON; -.
DR PRO; PR:P38871; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38871; protein.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0070056; C:prospore membrane leading edge; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Meiosis; Membrane; Phosphoprotein;
KW Reference proteome; Sporulation.
FT CHAIN 1..571
FT /note="Sporulation-specific protein 1"
FT /id="PRO_0000072216"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..486
FT /evidence="ECO:0000255"
FT COILED 542..566
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 571 AA; 65815 MW; A199EB4159771A03 CRC64;
MRSSGTYEND PSGEITSTSP KQSKQKKPTK FRERMRRWLQ NGKNNNHQGE EDVPEIFNKN
FYPQTGMTAF NNNDNGEVQD VTNNFFLPSE DESGPVQSSV KTFLTGNNDE DSNFQQNQNP
KQKSELPKSP YRQKPTQEIA LLKDLFVTNK YDDPYLNSST RFGNITSTFP SSLSLRTVTL
QTIKKRIDCI SAKKKEVWKT EEKFLKDILM WLQSSNFEDP DTISLIHEIE KIFEEDIHFE
QNVSDCLKEI SNNFEYICMR ETQLINEGNI LKNDLKKYAK AREHKGEKHE DTEVLREKVI
SSQKSFDVTK RHYKHAISIT TRQLFMNLAF EYYENCSDMK DISRKYLQES LSTLQTIDTL
SFSEELEKIR KRRFDKFWAK TNPDPTNNIQ KFVNMRTGVA GFNDSLMNHL YGKLSFGVAP
VEEELQNSQP EHTDVPENVW NEVLSDYNSM DGNPITSNKF LSAKELEPDQ LVELLAQEKE
EKEAKNISSS TAEVPSISQP EIKKENLESN DSLILRSTKR NVNVNAASLR NLSIKKTQVK
PESASEESKV LAAALNDAKQ NLDENVWRTP I
