MAM1_YEAST
ID MAM1_YEAST Reviewed; 302 AA.
AC P40065; D3DM13; E9P8Y3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Monopolin complex subunit MAM1;
DE AltName: Full=Monopolar microtubule attachment during meiosis 1 protein 1;
GN Name=MAM1; OrderedLocusNames=YER106W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11163190; DOI=10.1016/s0092-8674(00)00217-8;
RA Toth A., Rabitsch K.P., Galova M., Schleiffer A., Buonomo S.B.C.,
RA Nasmyth K.;
RT "Functional genomics identifies monopolin: a kinetochore protein required
RT for segregation of homologs during meiosis I.";
RL Cell 103:1155-1168(2000).
RN [5]
RP FUNCTION.
RX PubMed=11470404; DOI=10.1016/s0960-9822(01)00274-3;
RA Rabitsch K.P., Toth A., Galova M., Schleiffer A., Schaffner G., Aigner E.,
RA Rupp C., Penkner A.M., Moreno-Borchart A.C., Primig M., Esposito R.E.,
RA Klein F., Knop M., Nasmyth K.;
RT "A screen for genes required for meiosis and spore formation based on
RT whole-genome expression.";
RL Curr. Biol. 11:1001-1009(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE MONOPOLIN
RP COMPLEX.
RX PubMed=12689592; DOI=10.1016/s1534-5807(03)00086-8;
RA Rabitsch K.P., Petronczki M., Javerzat J.-P., Genier S., Chwalla B.,
RA Schleiffer A., Tanaka T.U., Nasmyth K.;
RT "Kinetochore recruitment of two nucleolar proteins is required for homolog
RT segregation in meiosis I.";
RL Dev. Cell 4:535-548(2003).
RN [7]
RP FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12717442; DOI=10.1038/ncb977;
RA Clyne R.K., Katis V.L., Jessop L., Benjamin K.R., Herskowitz I.,
RA Lichten M., Nasmyth K.;
RT "Polo-like kinase Cdc5 promotes chiasmata formation and cosegregation of
RT sister centromeres at meiosis I.";
RL Nat. Cell Biol. 5:480-485(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12663816; DOI=10.1126/science.1081846;
RA Lee B.H., Amon A.;
RT "Role of Polo-like kinase CDC5 in programming meiosis I chromosome
RT segregation.";
RL Science 300:482-486(2003).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15620645; DOI=10.1016/j.cub.2004.12.020;
RA Katis V.L., Matos J., Mori S., Shirahige K., Zachariae W., Nasmyth K.;
RT "Spo13 facilitates monopolin recruitment to kinetochores and regulates
RT maintenance of centromeric cohesion during yeast meiosis.";
RL Curr. Biol. 14:2183-2196(2004).
RN [11]
RP FUNCTION.
RX PubMed=15226378; DOI=10.1242/jcs.01231;
RA Petronczki M., Chwalla B., Siomos M.F., Yokobayashi S., Helmhart W.,
RA Deutschbauer A.M., Davis R.W., Watanabe Y., Nasmyth K.;
RT "Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/Ctf8,
RT the helicase Chl1 and the polymerase-alpha-associated protein Ctf4 is
RT essential for chromatid disjunction during meiosis II.";
RL J. Cell Sci. 117:3547-3559(2004).
CC -!- FUNCTION: Component of the monopolin complex which promotes
CC monoorientation during meiosis I, required for chromosome segregation
CC during meiosis. {ECO:0000269|PubMed:11163190,
CC ECO:0000269|PubMed:11470404, ECO:0000269|PubMed:12586695,
CC ECO:0000269|PubMed:12663816, ECO:0000269|PubMed:12689592,
CC ECO:0000269|PubMed:12717442, ECO:0000269|PubMed:15226378,
CC ECO:0000269|PubMed:15620645}.
CC -!- SUBUNIT: Component of the monopolin complex composed of at least CSM1,
CC LRS4 and MAM1. The complex associates with the kinetochore during late
CC pachytene. {ECO:0000269|PubMed:12689592}.
CC -!- INTERACTION:
CC P40065; P25651: CSM1; NbExp=7; IntAct=EBI-22643, EBI-22001;
CC P40065; P29295: HRR25; NbExp=3; IntAct=EBI-22643, EBI-8536;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11163190,
CC ECO:0000269|PubMed:12663816, ECO:0000269|PubMed:12689592,
CC ECO:0000269|PubMed:12717442, ECO:0000269|PubMed:15620645}.
CC Note=Localizes to kinechores during late pachytene.
CC -!- PTM: Phosphorylated by CDC5. This phosphorylation is required for the
CC location to the kinetochores during late pachytene.
CC {ECO:0000269|PubMed:12663816, ECO:0000269|PubMed:12717442}.
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DR EMBL; U18839; AAB64661.1; -; Genomic_DNA.
DR EMBL; AY692881; AAT92900.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07767.1; -; Genomic_DNA.
DR PIR; S50609; S50609.
DR RefSeq; NP_011032.1; NM_001178997.1.
DR PDB; 5CYZ; X-ray; 1.84 A; C=87-191.
DR PDB; 5CZO; X-ray; 2.89 A; C/D=87-191.
DR PDB; 5KTB; X-ray; 3.05 A; C=221-290.
DR PDBsum; 5CYZ; -.
DR PDBsum; 5CZO; -.
DR PDBsum; 5KTB; -.
DR AlphaFoldDB; P40065; -.
DR SMR; P40065; -.
DR BioGRID; 36852; 81.
DR ComplexPortal; CPX-1681; Monopolin complex.
DR DIP; DIP-5402N; -.
DR IntAct; P40065; 3.
DR STRING; 4932.YER106W; -.
DR PaxDb; P40065; -.
DR PRIDE; P40065; -.
DR EnsemblFungi; YER106W_mRNA; YER106W; YER106W.
DR GeneID; 856843; -.
DR KEGG; sce:YER106W; -.
DR SGD; S000000908; MAM1.
DR VEuPathDB; FungiDB:YER106W; -.
DR eggNOG; ENOG502S889; Eukaryota.
DR HOGENOM; CLU_928146_0_0_1; -.
DR InParanoid; P40065; -.
DR OMA; SENWNEN; -.
DR BioCyc; YEAST:G3O-30271-MON; -.
DR PRO; PR:P40065; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40065; protein.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0033551; C:monopolin complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR GO; GO:0010789; P:meiotic sister chromatid cohesion involved in meiosis I; IMP:SGD.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:SGD.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:SGD.
DR InterPro; IPR018847; Monopolin_cplx_su_Mam1.
DR Pfam; PF10434; MAM1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..302
FT /note="Monopolin complex subunit MAM1"
FT /id="PRO_0000202645"
FT REGION 53..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 202
FT /note="K -> E (in Ref. 3; AAT92900)"
FT /evidence="ECO:0000305"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:5CYZ"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5CYZ"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5CZO"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5CYZ"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5KTB"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:5KTB"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5KTB"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:5KTB"
SQ SEQUENCE 302 AA; 35753 MW; 64E467A38EB831FF CRC64;
MREKRTISNK DTNYLKFPNK LQRYSRFLSR KISNTSPEKQ PKKNIKEHCL SSYHKEHSVK
PKQNSGNVAA KEDKDTQHLQ NNVANEEATE CLTRSNLKKL QEKIFDRELN DIACDHCLCS
TENRRDIKYS RLWFLFELEM SENWNENLRL SCYNKYVYSA IDESWKMENI LLKEQEKHYE
YFPIGQLLIP NNIDYTNKQK RKENIEDLTI EIDSIIETNH QKKRFLPQSV LIKREDEIAF
DDFHLDARKV LNDLSATSEN PFSSSPNTKK IKSKGKTLEV VPKKKNKKII GALERKLHID
EN
