CDC15_SCHPO
ID CDC15_SCHPO Reviewed; 927 AA.
AC Q09822; O14365; Q9UU50;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Cell division control protein 15;
GN Name=cdc15; ORFNames=SPAC20G8.05c;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7634333; DOI=10.1016/0092-8674(95)90432-8;
RA Fankhauser C., Reymond A., Cerutti L., Utzig S., Hofmann K., Simanis V.;
RT "The S. pombe cdc15 gene is a key element in the reorganization of F-actin
RT at mitosis.";
RL Cell 82:435-444(1995).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Fankhauser C., Reymond A., Cerutti L., Utzig S., Hofmann K., Simanis V.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 286-425.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; SER-332; THR-529;
RP SER-636; SER-639; SER-700 AND SER-774, AND IDENTIFICATION BY MASS
RP 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: After the onset of mitosis, forms a ring-like structure which
CC colocalizes with the medial actin ring. Appears to mediate cytoskeletal
CC rearrangements required for cytokinesis. Essential for viability.
CC -!- INTERACTION:
CC Q09822; O74338: blt1; NbExp=2; IntAct=EBI-1148185, EBI-1542378;
CC Q09822; Q10059: cdc12; NbExp=4; IntAct=EBI-1148185, EBI-1148281;
CC Q09822; Q9Y7Z8: myo1; NbExp=4; IntAct=EBI-1148185, EBI-1148082;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- DEVELOPMENTAL STAGE: Peaks in early mitosis before septation.
CC -!- DOMAIN: The N-terminal region is in a coiled coil structure.
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DR EMBL; X86179; CAA60115.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB08599.2; -; Genomic_DNA.
DR EMBL; AB027810; BAA87114.1; -; Genomic_DNA.
DR PIR; T38127; T38127.
DR RefSeq; NP_593322.1; NM_001018753.2.
DR PDB; 6XJ1; X-ray; 3.52 A; A/B=19-312.
DR PDBsum; 6XJ1; -.
DR AlphaFoldDB; Q09822; -.
DR SMR; Q09822; -.
DR BioGRID; 278460; 59.
DR DIP; DIP-35649N; -.
DR IntAct; Q09822; 4.
DR STRING; 4896.SPAC20G8.05c.1; -.
DR iPTMnet; Q09822; -.
DR MaxQB; Q09822; -.
DR PaxDb; Q09822; -.
DR PRIDE; Q09822; -.
DR EnsemblFungi; SPAC20G8.05c.1; SPAC20G8.05c.1:pep; SPAC20G8.05c.
DR GeneID; 2541975; -.
DR KEGG; spo:SPAC20G8.05c; -.
DR PomBase; SPAC20G8.05c; cdc15.
DR VEuPathDB; FungiDB:SPAC20G8.05c; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_003525_0_0_1; -.
DR InParanoid; Q09822; -.
DR OMA; TFESHHD; -.
DR PhylomeDB; Q09822; -.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q09822; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0032178; C:medial membrane band; 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:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IDA:PomBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:PomBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:PomBase.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IMP:PomBase.
DR GO; GO:0061171; P:establishment of bipolar cell polarity; 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:1904498; P:protein localization to mitotic actomyosin contractile ring; IMP:PomBase.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..927
FT /note="Cell division control protein 15"
FT /id="PRO_0000089443"
FT DOMAIN 20..273
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 866..927
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 321..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..207
FT /evidence="ECO:0000255"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 927 AA; 102119 MW; FDCE7E0AAA3D247D CRC64;
MEVNGVSQSE AAPYVTKSSV KFRDNFWGSE DAGMDALMSR TKSSLSVLES IDEFYAKRAS
IEREYASKLQ ELAASSADIP EVGSTLNNIL SMRTETGSMA KAHEEVSQQI NTELRNKIRE
YIDQTEQQKV VAANAIEELY QKKTALEIDL SEKKDAYEYS CNKLNSYMRQ TKKMTGRELD
KYNLKIRQAA LAVKKMDAEY RETNELLLTV TREWIDRWTE VCDAFQHIEE YRLEFLKTNM
WAYANIISTA CVKDDESCEK IRLTLENTNI DEDITQMIQN EGTGTTIPPL PEFNDYFKEN
GLNYDIDQLI SKAPSYPYSS SRPSASASLA SSPTRSAFRP KTSETVSSEV VSSPPTSPLH
SPVKPVSNEQ VEQVTEVELS IPVPSIQEAE SQKPVLTGSS MRRPSVTSPT FEVAARPLTS
MDVRSSHNAE TEVQAIPAAT DISPEVKEGK NSENAITKDN DDIILSSQLQ PTATGSRSSR
LSFSRHGHGS QTSLGSIKRK SIMERMGRPT SPFMGSSFSN MGSRSTSPTK EGFASNQHAT
GASVQSDELE DIDPRANVVL NVGPNMLSVG EAPVESTSKE EDKDVPDPIA NAMAELSSSM
RRRQSTSVDD EAPVSLSKTS SSTRLNGLGY HSRNTSIASD IDGVPKKSTL GAPPAAHTSA
QMQRMSNSFA SQTKQVFGEQ RTENSARESL RHSRSNMSRS PSPMLSRRSS TLRPSFERSA
SSLSVRQSDV VSPAPSTRAR GQSVSGQQRP SSSMSLYGEY NKSQPQLSMQ RSVSPNPLGP
NRRSSSVLQS QKSTSSNTSN RNNGGYSGSR PSSEMGHRYG SMSGRSMRQV SQRSTSRARS
PEPTNRNSVQ SKNVDPRATF TAEGEPILGY VIALYDYQAQ IPEEISFQKG DTLMVLRTQE
DGWWDGEIIN VPNSKRGLFP SNFVQTV
