CDC31_SCHPO
ID CDC31_SCHPO Reviewed; 176 AA.
AC O74435;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cell division control protein 31;
GN Name=cdc31; ORFNames=SPCC1682.04;
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 [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 [2]
RP FUNCTION, INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=12857865; DOI=10.1091/mbc.e02-10-0661;
RA Paoletti A., Bordes N., Haddad R., Schwartz C.L., Chang F., Bornens M.;
RT "Fission yeast cdc31p is a component of the half-bridge and controls SPB
RT duplication.";
RL Mol. Biol. Cell 14:2793-2808(2003).
CC -!- FUNCTION: Required for the proper coordination between exit from
CC mitosis and the initiation of septation. Has a role in bipolar spindle
CC formation during spindle pole body (SPB) duplication. Required for the
CC localization of sad1 to the SPB (PubMed:12857865).
CC {ECO:0000269|PubMed:12857865}.
CC -!- SUBUNIT: Component of the spindle pole body (SPB), acting as the
CC connector of microtubule arrays in the cytoplasm and the nucleoplasm,
CC is involved in nuclear positioning before chromosome segregation, SPB
CC separation, spindle formation, chromosome segregation, nuclear
CC migration into the bud, nuclear reorientation after cytokinesis and
CC nuclear fusion during conjugation. The SPB half-bridge, which is
CC tightly associated with the cytoplasmic side of the nuclear envelope
CC and the SPB, is playing a key role as the starting structure for and in
CC the initiation of SPB duplication in G1 (PubMed:12857865). Within the
CC complex, interacts with sad1 (PubMed:12857865).
CC {ECO:0000269|PubMed:12857865}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12857865}.
CC Note=Associates with the half-bridge structure of the SPB.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20670.1; -; Genomic_DNA.
DR PIR; T41061; T41061.
DR RefSeq; NP_587797.1; NM_001022790.2.
DR AlphaFoldDB; O74435; -.
DR SMR; O74435; -.
DR BioGRID; 275831; 5.
DR STRING; 4896.SPCC1682.04.1; -.
DR iPTMnet; O74435; -.
DR MaxQB; O74435; -.
DR PaxDb; O74435; -.
DR PRIDE; O74435; -.
DR EnsemblFungi; SPCC1682.04.1; SPCC1682.04.1:pep; SPCC1682.04.
DR GeneID; 2539261; -.
DR KEGG; spo:SPCC1682.04; -.
DR PomBase; SPCC1682.04; cdc31.
DR VEuPathDB; FungiDB:SPCC1682.04; -.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_061288_18_1_1; -.
DR InParanoid; O74435; -.
DR OMA; MIMKQST; -.
DR PhylomeDB; O74435; -.
DR PRO; PR:O74435; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0061496; C:half bridge of mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005825; C:half bridge of spindle pole body; IBA:GO_Central.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1903087; P:mitotic spindle pole body duplication; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR GO; GO:1902441; P:protein localization to meiotic spindle pole body; IMP:PomBase.
DR GO; GO:0030474; P:spindle pole body duplication; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cell cycle; Cell division; Metal-binding; Mitosis; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..176
FT /note="Cell division control protein 31"
FT /id="PRO_0000073576"
FT DOMAIN 34..69
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 70..105
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 107..142
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 143..176
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 176 AA; 20470 MW; 01FB8B2AE160A5A2 CRC64;
MFANARAKRR SRASSPTPAR LGGYAPLRVE ITEEQRQDIN EAFKLFDSDK DNAIDYHELR
AAMRALGFNA EKSEVLKILR DFDKTGKGYL QMEDFVRVMT EKIVERDPLE EIKRAFELFD
DDETGKISLR NLRRVAKELN ENIDDQELEA MIEEFDLDQD GEINEQEFIA IMMDEA
