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   02-SEP-2026, entry version 154.
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; DOI=10.1038/387s078;
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   AlphaFoldDB; P40065; -.
DR   MDRepo; P40065; -.
DR   SMR; P40065; -.
DR   BioGRID; 36852; 83.
DR   ComplexPortal; CPX-1681; Monopolin complex.
DR   DIP; DIP-5402N; -.
DR   FunCoup; P40065; 161.
DR   IntAct; P40065; 3.
DR   STRING; 4932.YER106W; -.
DR   iPTMnet; P40065; -.
DR   PaxDb; 4932-YER106W; -.
DR   PeptideAtlas; P40065; -.
DR   EnsemblFungi; YER106W_mRNA; YER106W; YER106W.
DR   GeneID; 856843; -.
DR   KEGG; sce:YER106W; -.
DR   AGR; SGD:S000000908; -.
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   OrthoDB; 4070446at2759; -.
DR   BioCyc; YEAST:G3O-30271-MONOMER; -.
DR   BioGRID-ORCS; 856843; 7 hits in 10 CRISPR screens.
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:0010789; P:meiosis I sister chromatid cohesion; IMP:SGD.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR   GO; GO:0051455; P:spindle attachment to meiosis I kinetochore; IMP:SGD.
DR   Gene3D; 6.10.250.3400; -; 1.
DR   InterPro; IPR018847; Monopolin_cplx_su_Mam1.
DR   Pfam; PF10434; MAM1; 1.
DR   PDBsum; 5CYZ; -.
DR   PDBsum; 5CZO; -.
DR   PDBsum; 5KTB; -.
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        257..268
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..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           149..158
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           227..229
FT                   /evidence="ECO:0007829|PDB:5KTB"
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
//