CDC12_SCHPO
ID CDC12_SCHPO Reviewed; 1841 AA.
AC Q10059; Q9UTU0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cell division control protein 12;
GN Name=cdc12; ORFNames=SPAC1F5.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9105045; DOI=10.1083/jcb.137.1.169;
RA Chang F., Drubin D., Nurse P.;
RT "cdc12p, a protein required for cytokinesis in fission yeast, is a
RT component of the cell division ring and interacts with profilin.";
RL J. Cell Biol. 137:169-182(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 517-689, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=FY436;
RX PubMed=12796476; DOI=10.1083/jcb.200211078;
RA Kovar D.R., Kuhn J.R., Tichy A.L., Pollard T.D.;
RT "The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament
RT capping protein gated by profilin.";
RL J. Cell Biol. 161:875-887(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1541 AND TYR-1544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Plays a role in the cell cycle. Involved in cytokinesis.
CC Component of the cell division ring. In the absence of profilin, caps
CC the barbed end of actin filaments, thus preventing subunit addition and
CC dissociation. In the presence of profilin, nucleates actin filaments
CC that grow rapidly from their barbed ends.
CC {ECO:0000269|PubMed:12796476}.
CC -!- SUBUNIT: Interacts with profilin and actin at the FH1 and FH2 domains
CC respectively. {ECO:0000269|PubMed:12796476}.
CC -!- INTERACTION:
CC Q10059; Q09822: cdc15; NbExp=4; IntAct=EBI-1148281, EBI-1148185;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC Note=Nuclear, and septum.
CC -!- SIMILARITY: Belongs to the formin homology family. BNI1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA92232.1; -; Genomic_DNA.
DR EMBL; AB028006; BAA87310.1; -; Genomic_DNA.
DR PIR; T38091; T38091.
DR RefSeq; NP_592869.1; NM_001018269.2.
DR AlphaFoldDB; Q10059; -.
DR SMR; Q10059; -.
DR BioGRID; 278100; 21.
DR IntAct; Q10059; 1.
DR STRING; 4896.SPAC1F5.04c.1; -.
DR iPTMnet; Q10059; -.
DR MaxQB; Q10059; -.
DR PaxDb; Q10059; -.
DR PRIDE; Q10059; -.
DR EnsemblFungi; SPAC1F5.04c.1; SPAC1F5.04c.1:pep; SPAC1F5.04c.
DR GeneID; 2541603; -.
DR KEGG; spo:SPAC1F5.04c; -.
DR PomBase; SPAC1F5.04c; cdc12.
DR VEuPathDB; FungiDB:SPAC1F5.04c; -.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_002224_0_0_1; -.
DR InParanoid; Q10059; -.
DR OMA; KALHWEK; -.
DR PhylomeDB; Q10059; -.
DR PRO; PR:Q10059; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:1990808; F:F-bar domain binding; IPI:PomBase.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:1904670; P:actin filament polymerization involved in mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; IDA:PomBase.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:PomBase.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:PomBase.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IDA:PomBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:PomBase.
DR GO; GO:1904498; P:protein localization to mitotic actomyosin contractile ring; IMP:PomBase.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1841
FT /note="Cell division control protein 12"
FT /id="PRO_0000194901"
FT DOMAIN 232..620
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 740..972
FT /note="FH1"
FT DOMAIN 980..1391
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1696..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 674..715
FT /evidence="ECO:0000255"
FT COILED 1260..1290
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1502..1521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1541
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1544
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1841 AA; 207599 MW; E1AA42731FCD37C5 CRC64;
MRNSSKGQDP NFSYDSILST PTPSARRTIG PRAPKSKTTY HKPPSSIESV STLIQPNKSQ
SVTSPYVKQF TFSSKEYNSH NKHALQNSQL PLPKTPEKST VHRPKANKVE VTDLPSSSSV
EHLHTSKHLK GPRLPKNIIK SSEDVQIAPV TPPVHSRSFD PLPKPPVPSV PVSKTKRRTK
HKLAPVVEVP EITNEVSPKF TSTNDEQVYR LRSIRAGSPN SVCSFQFEIP STRPPSLDQL
IHLFNDFLRH PVFDFDENAI EMLQSCTPDE KWCFIRSNFA GFDDPSFQIP ELAAVHRPVS
WFVIQLWNKT ISNLQLITLS SLLSTQSDRW ISLFLELQGL RALHNLLTYF NSSAVVQPQQ
AEVPRCMLTL LKKKPTLVTS NSYIFQAITV TLISPNLLPR KVAADLLTWV LSLKEPLVVS
ILETGFKEIN AEYEKEVPLF FGWIKSFKDI ILEKELARTP PSSPARNSAS SSPSNIAFLE
YCTSTMEFIN QLIVACEELE QGFDLDILDS LRESGIHEVI QLLRNFPDQQ LEKQLNIYES
EEERRTISQT THEDVDSFMS NESSILSSFN EFASNEVGRL LESTIQNILL AKGTEKQKVK
LIKVFNSLLQ RILLNSKVSN ESFEDSLQAS LNMLTERFYS DDTARNALKE AKASRAMAEK
MVIERDAMAA QVNLGAEDLI AKLNKEVEDQ KDVILSQKRT NETLKTEIDA LQKSHVTQIQ
RSEVELRELY LLINSDSFQG STNSKERIIE YLLDKLDLRK KEIAAESTLW SNDGIDDKLR
DLREQMSRQS SQPSTVSTIL QIPDKKFHRP FPRHLHRYVG RSASESLTSE KDESIKSMKG
IDDFANLEIP GKGIESNVVI KDISNQTHEI NSVENKAETV SNNSKITNFD IPNDATSLPT
IITHPTPPPP PPLPVKTSLN TFSHPDSVNI VANDTSVAGV MPAFPPPPPP PPPLVSAAGG
KFVSPAVSNN ISKDDLHKTT GLTRRPTRRL KQMHWEKLNS GLEFTFWTGP SDEANKILET
LHTSGVLDEL DESFAMKEAK TLVKKTCART DYMSSELQKL FGIHFHKLSH KNPNEIIRMI
LHCDDSMNEC VEFLSSDKVL NQPKLKADLE PYRIDWANGG DLVNSEKDAS ELSRWDYLYV
RLIVDLGGYW NQRMNALKVK NIIETNYENL VRQTKLIGRA ALELRDSKVF KGLLYLILYL
GNYMNDYVRQ AKGFAIGSLQ RLPLIKNANN TKSLLHILDI TIRKHFPQFD NFSPELSTVT
EAAKLNIEAI EQECSELIRG CQNLQIDCDS GALSDPTVFH PDDKILSVIL PWLMEGTKKM
DFLKEHLRTM NTTLNNAMRY FGEQPNDPNS KNLFFKRVDS FIIDYSKARS DNLKSEEEEA
SQHRRLNLVN NHKEHVLERA MSENNKMDNE AMDGFLDKLR NVKLESHHKP RNRSAITMGK
EHLIEAPNTS TKSSPAKNEL FVPKRSSVKS DLAKVRPRYP KGSESTDGLS DALNITPTKK
GEVSSKAKKG YNYEKRRSGR QVSDSYVLNK NSKNKSNKGR SASYTFSDPS SLEDSNRQKP
FNGEKFRRFS SKSRRGSQNR DSKKTGKARK DKGINNNQTS PQNKPSKESL KSDTISNEKK
VFPQKASKVN LLTPTISNGT RASKHANEKE NTFPRGVENN LVAPMIPNNT ELNEDTSAVS
RNLENATNDL KETFPTTTTI STARAKPGNN DINTILRRNN SRGRRRMLQQ MSPLKSNKFS
GTNDLNFQQA TKPDGSNKSS YMERLEKLKQ NSERHLQSVG GKKVYSSEET PVNKILVSPS
VSILDHNRIL SQSTPIKSPQ RAQEMLAGLL SGKLAPKENE K
