SPR28_YEAST
ID SPR28_YEAST Reviewed; 423 AA.
AC Q04921; D6VSK1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Sporulation-regulated protein 28;
GN Name=SPR28; OrderedLocusNames=YDR218C; ORFNames=YD9934.03C;
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 SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH CDC11 AND
RP SPR3.
RX PubMed=8885406; DOI=10.1099/13500872-142-10-2897;
RA de Virgilio C., DeMarini D.J., Pringle J.R.;
RT "SPR28, a sixth member of the septin gene family in Saccharomyces
RT cerevisiae that is expressed specifically in sporulating cells.";
RL Microbiology 142:2897-2905(1996).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC into filaments and form a ring at the cleavage site. May act by
CC recruiting MYO1 and HOF1, a protein involved in septation, to the site
CC of cleavage. Septins are also involved in cell morphogenesis, bud site
CC selection, chitin deposition, cell cycle regulation, cell
CC compartmentalization and spore wall formation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with itself. Interacts with CDC11 and SPR3; probably
CC to form a ring at the bud neck. {ECO:0000269|PubMed:8885406}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Bud neck {ECO:0000250}. Note=Present at the bud
CC neck during cell division. Probably interacts with phosphoinosides such
CC as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate
CC (By similarity). Localizes to ring-like structures around each of the
CC four nuclear lobes at the onset and during meiosis II. Concentrated
CC initially at the leading edge of the developing prospore wall.
CC {ECO:0000250, ECO:0000269|PubMed:8885406}.
CC -!- DEVELOPMENTAL STAGE: Expressed during meiosis and ascospore formation.
CC First expressed at the beginning of meiosis I, and is highly expressed
CC prior meiosis II. {ECO:0000269|PubMed:8885406}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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; Z48612; CAA88498.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12061.1; -; Genomic_DNA.
DR PIR; S59425; S59425.
DR RefSeq; NP_010504.1; NM_001180526.1.
DR AlphaFoldDB; Q04921; -.
DR SMR; Q04921; -.
DR BioGRID; 32271; 54.
DR DIP; DIP-943N; -.
DR IntAct; Q04921; 2.
DR MINT; Q04921; -.
DR STRING; 4932.YDR218C; -.
DR PaxDb; Q04921; -.
DR PRIDE; Q04921; -.
DR EnsemblFungi; YDR218C_mRNA; YDR218C; YDR218C.
DR GeneID; 851804; -.
DR KEGG; sce:YDR218C; -.
DR SGD; S000002626; SPR28.
DR VEuPathDB; FungiDB:YDR218C; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; Q04921; -.
DR OMA; TRPHACL; -.
DR BioCyc; YEAST:G3O-29799-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:Q04921; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04921; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0072687; C:meiotic spindle; IDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031105; C:septin complex; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:SGD.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0097271; P:protein localization to bud neck; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..423
FT /note="Sporulation-regulated protein 28"
FT /id="PRO_0000173501"
FT DOMAIN 28..342
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 121..124
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 203..206
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 360..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 384..417
FT /evidence="ECO:0000255"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 204..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 48193 MW; EB8D3C0F47CD41DB CRC64;
MFPMKDHSAL EQHTLSRDEL RRRKGYKKGL QLSILLLGEK GSGKSTFLNN LCGQDISLSD
GDYDDDDDKV TNNVTPENGN AIEDIDPGYK TAHLSPGLKL VTRRVYLNDE LGVPITLDII
LFPGCGDNVD NSQSSVVIKN YLDQQFANVL KEEVRIKRNT KETDGRPHVC LYFLKSTPRG
VKKFDIELMK TICDKVNLIP IIPKADGLTE TELNLHKDIV RQEISQNNIR VFDFKSDTLG
ETLALYDMDI DSSSAKSKYD NDTKIKEISP FAIVCSKTFN KNSENRVEHI RTYEWGSLVV
EDQNTSDFIY LKAILLGSHL QELKDVTNNV LYENYRAKVL TEKKNNYDIP NYSYIDETSR
GSVSNVSTRR NSASRTLGNP DTNDENAYQI HKEIDEKNRI IEDYQRKIDL LEKMLAAPHQ
NKV
