SPR3_YEAST
ID SPR3_YEAST Reviewed; 512 AA.
AC P41901; D6VUJ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sporulation-regulated protein 3;
GN Name=SPR3; OrderedLocusNames=YGR059W;
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 [GENOMIC DNA].
RX PubMed=8636217; DOI=10.1083/jcb.132.3.399;
RA Fares H., Goetsch L., Pringle J.R.;
RT "Identification of a developmentally regulated septin and involvement of
RT the septins in spore formation in Saccharomyces cerevisiae.";
RL J. Cell Biol. 132:399-411(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7590307; DOI=10.1016/0378-1119(95)00438-c;
RA Ozsarac N., Bhattacharyya M., Dawes I.W., Clancy M.J.;
RT "The SPR3 gene encodes a sporulation-specific homologue of the yeast
RT CDC3/10/11/12 family of bud neck microfilaments and is regulated by ABFI.";
RL Gene 164:157-162(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP INTERACTION WITH CDC11 AND SPR28.
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 other septin proteins such as SPR28 to form a
CC ring at the bud neck. {ECO:0000269|PubMed:8885406}.
CC -!- SUBCELLULAR LOCATION: Prospore membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Bud neck {ECO:0000250}. Note=Present at
CC the bud neck during cell division. Probably interacts with
CC phosphoinosides such as phosphatidylinositol 4-phosphate or
CC phosphatidylinositol 5-phosphate (By similarity). Localized to the
CC leading edges of the membrane sacs that form near the spindle-pole
CC bodies and gradually extend to engulf the nuclear lobes that contain
CC the haploid chromosome sets, thus forming the spores. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Sporulation-specific.
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}.
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DR EMBL; L31767; AAC37482.1; -; Genomic_DNA.
DR EMBL; U24129; AAC13870.1; -; Genomic_DNA.
DR EMBL; Z72844; CAA97061.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08155.1; -; Genomic_DNA.
DR PIR; S48524; S48524.
DR RefSeq; NP_011573.3; NM_001181188.3.
DR AlphaFoldDB; P41901; -.
DR SMR; P41901; -.
DR BioGRID; 33304; 128.
DR DIP; DIP-3011N; -.
DR IntAct; P41901; 2.
DR MINT; P41901; -.
DR STRING; 4932.YGR059W; -.
DR PaxDb; P41901; -.
DR PRIDE; P41901; -.
DR EnsemblFungi; YGR059W_mRNA; YGR059W; YGR059W.
DR GeneID; 852950; -.
DR KEGG; sce:YGR059W; -.
DR SGD; S000003291; SPR3.
DR VEuPathDB; FungiDB:YGR059W; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; P41901; -.
DR OMA; AFTWRTM; -.
DR BioCyc; YEAST:G3O-30776-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:P41901; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P41901; 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: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: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:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; 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 Coiled coil; GTP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Sporulation.
FT CHAIN 1..512
FT /note="Sporulation-regulated protein 3"
FT /id="PRO_0000173502"
FT DOMAIN 106..365
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 31..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..123
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 165..168
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 246..249
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 376..406
FT /evidence="ECO:0000255"
FT COILED 451..496
FT /evidence="ECO:0000255"
FT BINDING 116..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="E -> D (in Ref. 2; AAC13870)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> C (in Ref. 2; AAC13870)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> L (in Ref. 2; AAC13870)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="Y -> H (in Ref. 2; AAC13870)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="E -> G (in Ref. 2; AAC13870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 59845 MW; 1FC55B13E6A88F5D CRC64;
MKSKGSRLST DCPVEFPKIV SGFAEEVKIR RQSSQGQYAV DSHPPKSPEL KHRRQRSSSF
VNGKCRNRDL PLLDNKKAQE INTNSHGQDI GIKNLPRQRE LLNAKNGIDF TLMVAGQSGL
GKTTFINSLF STSLIDDDIK ENKPIIRYKS IVEGDGTHLN FNVIDTPGFG NNMDNAFTWR
TMVNYIDEEI RSYIFQEEQP DRTKMVDNRV HCCLYFLRPS NKGIDTLDVV TMKKLAKRVN
LIPVIAKSDL LTKEELKNFK TQVREIIRVQ DIPVCFFFGD EVLNATQDIF QKYPFSIIAS
NEYIFNEKGE KVKGRQYKWG AVDIENEKYC DFKILQKTIF DWNLIDLVES TEDYYEKCRS
EMLRTRLLKA RDCLTTKSVD ITEEQRKFLE EEMNFDEIEE NKLKNYKCYE IINKTVMDKV
ATEWDPEFIT RQLEAKKKFN ELSNREISKF RDWKKSLFME QENFNQEIEQ LNHKLENLQL
ECQDLEYKLL IGKSSNSHST DSATLVNVHI KR
