CDC31_YEAST
ID CDC31_YEAST Reviewed; 161 AA.
AC P06704; D6W2V8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Cell division control protein 31;
DE AltName: Full=Nuclear pore protein CDC31;
DE AltName: Full=Nucleoporin CDC31;
GN Name=CDC31; Synonyms=DSK1; OrderedLocusNames=YOR257W;
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=3526331; DOI=10.1073/pnas.83.15.5512;
RA Baum P., Furlong C., Byers B.;
RT "Yeast gene required for spindle pole body duplication: homology of its
RT product with Ca2+-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5512-5516(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7876310; DOI=10.1083/jcb.128.5.863;
RA Spang A., Courtney I., Grein K., Matzner M., Schiebel E.;
RT "The Cdc31p-binding protein Kar1p is a component of the half bridge of the
RT yeast spindle pole body.";
RL J. Cell Biol. 128:863-877(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP FUNCTION, AND KAR1-DEPENDENT RECRUITMENT TO SPB HALF-BRIDGE.
RX PubMed=8188750; DOI=10.1083/jcb.125.4.843;
RA Biggins S., Rose M.D.;
RT "Direct interaction between yeast spindle pole body components: Kar1p is
RT required for Cdc31p localization to the spindle pole body.";
RL J. Cell Biol. 125:843-852(1994).
RN [8]
RP FUNCTION.
RX PubMed=8070654; DOI=10.1093/genetics/137.2.407;
RA Vallen E.A., Ho W., Winey M., Rose M.D.;
RT "Genetic interactions between CDC31 and KAR1, two genes required for
RT duplication of the microtubule organizing center in Saccharomyces
RT cerevisiae.";
RL Genetics 137:407-422(1994).
RN [9]
RP FUNCTION, AND INTERACTION WITH KIC1.
RX PubMed=9813095; DOI=10.1083/jcb.143.3.751;
RA Sullivan D.S., Biggins S., Rose M.D.;
RT "The yeast centrin, cdc31p, and the interacting protein kinase, Kic1p, are
RT required for cell integrity.";
RL J. Cell Biol. 143:751-765(1998).
RN [10]
RP INTERACTION WITH THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [11]
RP FUNCTION, CELL MORPHOLOGY, MUTAGENESIS, AND STRUCTURE PREDICTION.
RX PubMed=11156974; DOI=10.1093/genetics/157.2.503;
RA Ivanovska I., Rose M.D.;
RT "Fine structure analysis of the yeast centrin, Cdc31p, identifies residues
RT specific for cell morphology and spindle pole body duplication.";
RL Genetics 157:503-518(2001).
RN [12]
RP FUNCTION, AND INTERACTION WITH MPS3 AT THE SPB.
RX PubMed=12486115; DOI=10.1083/jcb.200208169;
RA Jaspersen S.L., Giddings T.H. Jr., Winey M.;
RT "Mps3p is a novel component of the yeast spindle pole body that interacts
RT with the yeast centrin homologue Cdc31p.";
RL J. Cell Biol. 159:945-956(2002).
RN [13]
RP FUNCTION, AND INTERACTION WITH SFI1 AT THE SPB.
RX PubMed=14504268; DOI=10.1083/jcb.200307064;
RA Kilmartin J.V.;
RT "Sfi1p has conserved centrin-binding sites and an essential function in
RT budding yeast spindle pole body duplication.";
RL J. Cell Biol. 162:1211-1221(2003).
RN [14]
RP REVIEW.
RX PubMed=11935220; DOI=10.1007/s00294-001-0263-x;
RA Helfant A.H.;
RT "Composition of the spindle pole body of Saccharomyces cerevisiae and the
RT proteins involved in its duplication.";
RL Curr. Genet. 40:291-310(2002).
RN [15]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP FUNCTION, AND INTERACTION WITH VPS13.
RX PubMed=28122955; DOI=10.1083/jcb.201606078;
RA De M., Oleskie A.N., Ayyash M., Dutta S., Mancour L., Abazeed M.E.,
RA Brace E.J., Skiniotis G., Fuller R.S.;
RT "The Vps13p-Cdc31p complex is directly required for TGN late endosome
RT transport and TGN homotypic fusion.";
RL J. Cell Biol. 216:425-439(2017).
CC -!- FUNCTION: Functions as a component of the spindle pole body (SPB) half-
CC bridge (PubMed:10684247, PubMed:11156974, PubMed:12486115,
CC PubMed:14504268, PubMed:8070654). At the SPB, it is recruited by KAR1
CC and MPS3 to the SPB half-bridge and involved in the initial steps of
CC SPB duplication (PubMed:11156974, PubMed:12486115, PubMed:14504268,
CC PubMed:8070654). Also involved in connection with the protein kinase
CC KIC1 in the maintenance of cell morphology and integrity
CC (PubMed:9813095). May play a role in vesicle-mediated transport, in a
CC VPS13-dependent manner (PubMed:28122955). {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11156974, ECO:0000269|PubMed:12486115,
CC ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:28122955,
CC ECO:0000269|PubMed:8070654, ECO:0000269|PubMed:9813095}.
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. At the SPB half-bridge CDC31
CC interacts with KAR1, MPS3 and SFI1 (PubMed:12486115, PubMed:14504268).
CC Interacts with KIC1 (PubMed:9813095). Interacts with VPS13
CC (PubMed:28122955). Associates with nuclear pore complexes (NPCs)
CC (PubMed:10684247). {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:12486115, ECO:0000269|PubMed:14504268,
CC ECO:0000269|PubMed:28122955, ECO:0000269|PubMed:9813095}.
CC -!- INTERACTION:
CC P06704; P06704: CDC31; NbExp=2; IntAct=EBI-4259, EBI-4259;
CC P06704; P47069: MPS3; NbExp=2; IntAct=EBI-4259, EBI-25811;
CC P06704; P46674: SAC3; NbExp=10; IntAct=EBI-4259, EBI-16425;
CC P06704; Q12369: SFI1; NbExp=2; IntAct=EBI-4259, EBI-2213082;
CC P06704; Q6WNK7: SUS1; NbExp=6; IntAct=EBI-4259, EBI-1251050;
CC P06704; Q08231: THP1; NbExp=4; IntAct=EBI-4259, EBI-32097;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:10684247}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole
CC body {ECO:0000269|PubMed:8188750}. Note=Spindle pole body, SPB
CC half- bridge (PubMed:8188750). Interacts with the nuclear pore complex
CC (NPCs) at the nucleus envelope (PubMed:10684247).
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:8188750}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; M14078; AAA66893.1; -; Genomic_DNA.
DR EMBL; X74500; CAA52609.1; -; Genomic_DNA.
DR EMBL; Z75165; CAA99479.1; -; Genomic_DNA.
DR EMBL; AY558434; AAS56760.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11024.1; -; Genomic_DNA.
DR PIR; S47549; S47549.
DR RefSeq; NP_014900.3; NM_001183676.3.
DR PDB; 2DOQ; X-ray; 3.00 A; A/B/C=1-161.
DR PDB; 2GV5; X-ray; 3.00 A; A/B/D/E=1-161.
DR PDB; 3FWB; X-ray; 2.50 A; A=1-161.
DR PDB; 3FWC; X-ray; 2.70 A; A/E/I/M=1-161.
DR PDB; 4MBE; X-ray; 2.61 A; A/D=1-161.
DR PDBsum; 2DOQ; -.
DR PDBsum; 2GV5; -.
DR PDBsum; 3FWB; -.
DR PDBsum; 3FWC; -.
DR PDBsum; 4MBE; -.
DR AlphaFoldDB; P06704; -.
DR SMR; P06704; -.
DR BioGRID; 34647; 93.
DR ComplexPortal; CPX-1686; TREX-2 transcription-export complex.
DR DIP; DIP-2273N; -.
DR IntAct; P06704; 31.
DR MINT; P06704; -.
DR STRING; 4932.YOR257W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P06704; -.
DR MaxQB; P06704; -.
DR PaxDb; P06704; -.
DR PRIDE; P06704; -.
DR EnsemblFungi; YOR257W_mRNA; YOR257W; YOR257W.
DR GeneID; 854431; -.
DR KEGG; sce:YOR257W; -.
DR SGD; S000005783; CDC31.
DR VEuPathDB; FungiDB:YOR257W; -.
DR eggNOG; KOG0028; Eukaryota.
DR GeneTree; ENSGT00940000157995; -.
DR HOGENOM; CLU_061288_18_1_1; -.
DR InParanoid; P06704; -.
DR OMA; MIMKQST; -.
DR BioCyc; YEAST:G3O-33748-MON; -.
DR EvolutionaryTrace; P06704; -.
DR PRO; PR:P06704; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P06704; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005825; C:half bridge of spindle pole body; IDA:SGD.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0070390; C:transcription export complex 2; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048193; P:Golgi vesicle transport; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0043549; P:regulation of kinase activity; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
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; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Metal-binding; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..161
FT /note="Cell division control protein 31"
FT /id="PRO_0000073577"
FT DOMAIN 20..55
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 56..91
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 93..128
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 129..161
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 77
FT /note="K -> L (in Ref. 1; AAA66893)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="T -> I (in Ref. 1; AAA66893)"
FT /evidence="ECO:0000305"
FT TURN 10..16
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:3FWB"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:3FWB"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:3FWB"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3FWB"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3FWB"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3FWB"
SQ SEQUENCE 161 AA; 18751 MW; 25A546E76E1EF520 CRC64;
MSKNRSSLQS GPLNSELLEE QKQEIYEAFS LFDMNNDGFL DYHELKVAMK ALGFELPKRE
ILDLIDEYDS EGRHLMKYDD FYIVMGEKIL KRDPLDEIKR AFQLFDDDHT GKISIKNLRR
VAKELGETLT DEELRAMIEE FDLDGDGEIN ENEFIAICTD S
