CNM67_YEAST
ID CNM67_YEAST Reviewed; 581 AA.
AC P53865; D6W0W5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Chaotic nuclear migration protein 67;
GN Name=CNM67; OrderedLocusNames=YNL225C; ORFNames=N1264;
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=8896273;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1071::aid-yea4>3.0.co;2-s;
RA Pandolfo D., de Antoni A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open
RT reading frames including a novel gene encoding a globin-like domain.";
RL Yeast 12:1071-1076(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NUD1.
RX PubMed=9571234; DOI=10.1091/mbc.9.5.977;
RA Brachat A., Kilmartin J.V., Wach A., Philippsen P.;
RT "Saccharomyces cerevisiae cells with defective spindle pole body outer
RT plaques accomplish nuclear migration via half-bridge-organized
RT microtubules.";
RL Mol. Biol. Cell 9:977-991(1998).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=10899120; DOI=10.1093/emboj/19.14.3657;
RA Knop M., Strasser K.;
RT "Role of the spindle pole body of yeast in mediating assembly of the
RT prospore membrane during meiosis.";
RL EMBO J. 19:3657-3667(2000).
RN [6]
RP FUNCTION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=11514632; DOI=10.1091/mbc.12.8.2519;
RA Schaerer F., Morgan G., Winey M., Philippsen P.;
RT "Cnm67p is a spacer protein of the Saccharomyces cerevisiae spindle pole
RT body outer plaque.";
RL Mol. Biol. Cell 12:2519-2533(2001).
RN [7]
RP COMPOSITION OF A SPB COMPLEX, AND INTERACTION WITH ADY3.
RX PubMed=11742972; DOI=10.1093/emboj/20.24.6946;
RA Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A.,
RA Shevchenko A., Knop M.;
RT "Prospore membrane formation linked to the leading edge protein (LEP) coat
RT assembly.";
RL EMBO J. 20:6946-6957(2001).
RN [8]
RP INTERACTION WITH ADY3.
RX PubMed=11973299; DOI=10.1093/genetics/160.4.1439;
RA Nickas M.E., Neiman A.M.;
RT "Ady3p links spindle pole body function to spore wall synthesis in
RT Saccharomyces cerevisiae.";
RL Genetics 160:1439-1450(2002).
RN [9]
RP INTERACTION WITH ADY4.
RX PubMed=12796288; DOI=10.1128/ec.2.3.431-445.2003;
RA Nickas M.E., Schwartz C., Neiman A.M.;
RT "Ady4p and Spo74p are components of the meiotic spindle pole body that
RT promote growth of the prospore membrane in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:431-445(2003).
RN [10]
RP INTERACTION WITH YOR129C.
RX PubMed=14515169;
RA Wysocka M., Bialkowska A., Micialkiewicz A., Kurlandzka A.;
RT "YOR129c, a new element interacting with Cnm67p, a component of the spindle
RT pole body of Saccharomyces cerevisiae.";
RL Acta Biochim. Pol. 50:883-890(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20 AND SER-72, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-85; SER-89 AND
RP SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the pathway that organizes the shaping and sizing
CC of the prospore membrane (PSM) during sporulation. Required for the
CC proper formation of the spindle pole body (SPB) outer plaque. May
CC connect the outer plaque to the central plaque embedded in the nuclear
CC envelope. {ECO:0000269|PubMed:11514632, ECO:0000269|PubMed:9571234}.
CC -!- SUBUNIT: Interacts directly with ADY3 and YOR129C. Interacts with ADY4.
CC Probable component of a SPB complex composed of ADY3, SSP1, DON1,
CC MPC54, SPO21/MPC70, NUD1 and CNM67. {ECO:0000269|PubMed:11742972,
CC ECO:0000269|PubMed:11973299, ECO:0000269|PubMed:12796288,
CC ECO:0000269|PubMed:14515169, ECO:0000269|PubMed:9571234}.
CC -!- INTERACTION:
CC P53865; P36094: SPC42; NbExp=3; IntAct=EBI-29172, EBI-17777;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:9571234}. Note=Localizes
CC to the meiotic outer plaque of the SPB, at the end of the meiotic
CC spindles.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Expressed from 3 to 9 hours
CC after induction of sporulation. {ECO:0000269|PubMed:10899120}.
CC -!- DOMAIN: The length of the coiled coil are required to adjust the space
CC between outer plaque and the central plaque.
CC {ECO:0000269|PubMed:11514632}.
CC -!- PTM: Phosphorylated in its N-terminal part.
CC {ECO:0000269|PubMed:11514632}.
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DR EMBL; Z69381; CAA93373.1; -; Genomic_DNA.
DR EMBL; Z71501; CAA96128.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10331.1; -; Genomic_DNA.
DR PIR; S63183; S63183.
DR RefSeq; NP_014174.1; NM_001183063.1.
DR PDB; 3OA7; X-ray; 2.30 A; A=429-581.
DR PDBsum; 3OA7; -.
DR AlphaFoldDB; P53865; -.
DR SMR; P53865; -.
DR BioGRID; 35611; 74.
DR ComplexPortal; CPX-1420; Spindle pole body intermediate layer 2 complex.
DR DIP; DIP-2447N; -.
DR IntAct; P53865; 27.
DR MINT; P53865; -.
DR STRING; 4932.YNL225C; -.
DR iPTMnet; P53865; -.
DR MaxQB; P53865; -.
DR PaxDb; P53865; -.
DR PRIDE; P53865; -.
DR EnsemblFungi; YNL225C_mRNA; YNL225C; YNL225C.
DR GeneID; 855496; -.
DR KEGG; sce:YNL225C; -.
DR SGD; S000005169; CNM67.
DR VEuPathDB; FungiDB:YNL225C; -.
DR eggNOG; ENOG502RYJ3; Eukaryota.
DR GeneTree; ENSGT00940000176826; -.
DR HOGENOM; CLU_469465_0_0_1; -.
DR InParanoid; P53865; -.
DR OMA; DHILEKM; -.
DR BioCyc; YEAST:G3O-33228-MON; -.
DR PRO; PR:P53865; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53865; protein.
DR GO; GO:0005823; C:central plaque of spindle pole body; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:SGD.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR GO; GO:0051300; P:spindle pole body organization; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR DisProt; DP02324; -.
DR InterPro; IPR021750; Sid4-like.
DR Pfam; PF11778; SID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Meiosis; Phosphoprotein; Reference proteome; Sporulation.
FT CHAIN 1..581
FT /note="Chaotic nuclear migration protein 67"
FT /id="PRO_0000089973"
FT REGION 86..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..252
FT /evidence="ECO:0000255"
FT COILED 306..363
FT /evidence="ECO:0000255"
FT COILED 373..451
FT /evidence="ECO:0000255"
FT COMPBIAS 93..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 429..446
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 475..480
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 483..497
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 518..533
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 540..554
FT /evidence="ECO:0007829|PDB:3OA7"
FT HELIX 563..571
FT /evidence="ECO:0007829|PDB:3OA7"
SQ SEQUENCE 581 AA; 67400 MW; C4DE7631A70E695A CRC64;
MTDFDLMNFP FHERLDSPVS ENGEIKDGEP IPQNWLNENH VGKSILPLFV NPEDVINCNF
SNARDSYEEN KSPSMDQMNY ARNTSYQESP GLQERPKNEK DKSPIGTDVH KKDVPNFIHS
TPRENSSKHF TRANEQASAQ PTDEHTSPDI SIEDCNGAKI FLQNSLSKED FRMLENVILG
YQKKVIELGR DNLRQEERAN SLQKELEAAT KSNDKTLDNK KKIEEQTVLI ENLTKDLSLN
KEMLEKANDT IQTKHTALLS LTDSLRKAEL FEIPIGILFF DLYDSEENSS KLDHILQEKY
PNIKGFLCAS QQEELSRISQ RFKNAKAEAE DLRNELENKK IEIQTMREKN NTLIGTNKTL
SKQNKILCDK FDKLTIDEKE ILKGCNEEIK IKLERLNERL GSWEKSKEKY ETSLKDKEKM
LADAEKKTNT LSKELDNLRS RFGNLEGNTS ERITIKNILQ SRPDISAEEC NFLMVEQIDS
ANLTTLQNTV KEIVLAVGIP YPKLRRKIPL LAIKLKYENI MLSNFAQRLH RQVYSQEMNL
KKFTDQAYYD FMSTRRMDSI DHHLERCLDH LYDHILEKMV K
