CDC12_YEAST
ID CDC12_YEAST Reviewed; 407 AA.
AC P32468; D3DL57;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Cell division control protein 12;
DE AltName: Full=Septin;
GN Name=CDC12; Synonyms=CLA10, PSL7; OrderedLocusNames=YHR107C;
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].
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=8791410; DOI=10.1016/s0955-0674(96)80054-8;
RA Longtine M.S., DeMarini D.J., Valencik M.L., Al-Awar O.S., Fares H.,
RA De Virgilio C., Pringle J.R.;
RT "The septins: roles in cytokinesis and other processes.";
RL Curr. Opin. Cell Biol. 8:106-119(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1107;
RX PubMed=7649470; DOI=10.1101/gad.9.15.1817;
RA Cvrckova F., de Virgilio C., Manser E., Pringle J.R., Nasmyth K.;
RT "Ste20-like protein kinases are required for normal localization of cell
RT growth and for cytokinesis in budding yeast.";
RL Genes Dev. 9:1817-1830(1995).
RN [3]
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 [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 IDENTIFICATION IN THE SEPTIN COMPLEX.
RX PubMed=9813094; DOI=10.1083/jcb.143.3.737;
RA Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M.,
RA Mitchison T.J., Field C.;
RT "Polymerization of purified yeast septins: evidence that organized filament
RT arrays may not be required for septin function.";
RL J. Cell Biol. 143:737-749(1998).
RN [6]
RP IDENTIFICATION IN THE GIN4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, AND INTERACTION WITH CDC11.
RX PubMed=12665577; DOI=10.1128/mcb.23.8.2762-2777.2003;
RA Casamayor A., Snyder M.;
RT "Molecular dissection of a yeast septin: distinct domains are required for
RT septin interaction, localization, and function.";
RL Mol. Cell. Biol. 23:2762-2777(2003).
RN [9]
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 [10]
RP SELF-ASSOCIATION, AND ASSEMBLY OF THE SEPTIN FILAMENTS.
RX PubMed=15282341; DOI=10.1091/mbc.e04-04-0330;
RA Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S.,
RA Chen R.E., Barth P., Alber T., Thorner J.;
RT "Protein-protein interactions governing septin heteropentamer assembly and
RT septin filament organization in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:4568-4583(2004).
RN [11]
RP INTERACTION WITH SYP1.
RX PubMed=18791237; DOI=10.1534/genetics.108.091900;
RA Qiu W., Neo S.P., Yu X., Cai M.;
RT "A novel septin-associated protein, Syp1p, is required for normal cell
RT cycle-dependent septin cytoskeleton dynamics in yeast.";
RL Genetics 180:1445-1457(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC early in the cell cycle as a patch at the incipient bud site and form a
CC ring approximate 15 minutes before bud emergence, which transforms into
CC an hour-glass shaped collar of cortical filaments that spans both sides
CC of the mother-bud neck. This collar persists until just before
CC cytokinesis, when it splits into two rings that occupy opposite sides
CC of the neck. The septins at the bud neck serve as a structural scaffold
CC that recruits different components involved in diverse processes at
CC specific stages during the cell cycle. Many proteins bind
CC asymmetrically to the septin collar. The septin assembly is regulated
CC by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and
CC HOF1, a protein involved in septation, to the site of cleavage. Septins
CC are also involved in cell morphogenesis, bud site selection, chitin
CC deposition, cell cycle regulation, cell compartmentalization and spore
CC wall formation.
CC -!- SUBUNIT: Component of the septin complex which consists of CDC3, CDC10,
CC CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of
CC highly ordered filaments at the mother-bud-neck. A complex formed by
CC CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in
CC vitro and the components seem to be present in a 2:2:2:2 arrangement in
CC vivo. The filaments are proposed to be formed by the end-to-end
CC polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a
CC bridge to bundle the polymers into paired filaments. Component of the
CC GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12,
CC GIN4, NAP1 and SHS1. Self-associates. Interacts with SYP1.
CC {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:12665577,
CC ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:9813094}.
CC -!- INTERACTION:
CC P32468; P32458: CDC11; NbExp=11; IntAct=EBI-4182, EBI-4178;
CC P32468; P38785: GIC1; NbExp=5; IntAct=EBI-4182, EBI-7575;
CC P32468; Q06648: GIC2; NbExp=5; IntAct=EBI-4182, EBI-7585;
CC P32468; Q07657: SHS1; NbExp=4; IntAct=EBI-4182, EBI-22083;
CC P32468; Q04477: SPC24; NbExp=3; IntAct=EBI-4182, EBI-27228;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14562095};
CC Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}. Note=Present at the bud neck during cell
CC division. Probably interacts with phosphoinosides such as
CC phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; L16551; AAB50036.1; -; Genomic_DNA.
DR EMBL; X82498; CAA57878.1; -; Genomic_DNA.
DR EMBL; U00059; AAB68863.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06801.1; -; Genomic_DNA.
DR PIR; S50870; S50870.
DR RefSeq; NP_011975.1; NM_001179237.1.
DR AlphaFoldDB; P32468; -.
DR SMR; P32468; -.
DR BioGRID; 36540; 809.
DR ComplexPortal; CPX-1675; Septin complex.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-853N; -.
DR IntAct; P32468; 49.
DR MINT; P32468; -.
DR STRING; 4932.YHR107C; -.
DR iPTMnet; P32468; -.
DR MaxQB; P32468; -.
DR PaxDb; P32468; -.
DR PRIDE; P32468; -.
DR EnsemblFungi; YHR107C_mRNA; YHR107C; YHR107C.
DR GeneID; 856507; -.
DR KEGG; sce:YHR107C; -.
DR SGD; S000001149; CDC12.
DR VEuPathDB; FungiDB:YHR107C; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; P32468; -.
DR OMA; EASHAEI; -.
DR BioCyc; YEAST:G3O-31150-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:P32468; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P32468; protein.
DR GO; GO:0005619; C:ascospore wall; IC:ComplexPortal.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0005937; C:mating projection; IDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0031105; C:septin complex; IDA:SGD.
DR GO; GO:0032160; C:septin filament array; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IC:ComplexPortal.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:SGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IDA:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
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 Acetylation; Cell cycle; Cell division; Coiled coil; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..407
FT /note="Cell division control protein 12"
FT /id="PRO_0000173500"
FT DOMAIN 31..314
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 41..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 98..101
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 179..182
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COILED 344..406
FT /evidence="ECO:0000255"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 407 AA; 46668 MW; A72DC393A6DBF924 CRC64;
MSAATATAAP VPPPVGISNL PNQRYKIVNE EGGTFTVMLC GESGLGKTTF INTLFQTVLK
RADGQQHRQE PIRKTVEIDI TRALLEEKHF ELRVNVIDTP GFGDNVNNNK AWQPLVDFID
DQHDSYMRQE QQPYRTKKFD LRVHAVLYFI RPTGHGLKPI DIETMKRLST RANLIPVIAK
ADTLTAQELQ QFKSRIRQVI EAQEIRIFTP PLDADSKEDA KSGSNPDSAA VEHARQLIEA
MPFAIVGSEK KFDNGQGTQV VARKYPWGLV EIENDSHCDF RKLRALLLRT YLLDLISTTQ
EMHYETYRRL RLEGHENTGE GNEDFTLPAI APARKLSHNP RYKEEENALK KYFTDQVKAE
EQRFRQWEQN IVNERIRLNG DLEEIQGKVK KLEEQVKSLQ VKKSHLK
