ID   MAD1_SCHPO              Reviewed;         689 AA.
AC   P87169;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Spindle assembly checkpoint component mad1;
DE   AltName: Full=Mitotic arrest deficient protein 1;
GN   Name=mad1; ORFNames=SPBC3D6.04c;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=14592707; DOI=10.1016/s0378-1097(03)00607-4;
RA   Kim I.G., Rhee D.K., Jeong J.W., Kim S.C., Won M., Lee J., Song K.W.,
RA   Kim H.B.;
RT   "Mad1p, a component of the spindle assembly checkpoint in fission yeast,
RT   suppresses a novel septation-defective mutant, sun1, in a cell-division
RT   cycle.";
RL   FEMS Microbiol. Lett. 227:183-188(2003).
RN   [2]
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).
CC   -!- FUNCTION: Central component of the spindle assembly checkpoint. Has a
CC       role in the correct positioning of the septum. Required for anchoring
CC       mad2 to the nuclear periphery. {ECO:0000269|PubMed:14592707}.
CC   -!- INTERACTION:
CC       P87169; P24339: cut7; NbExp=3; IntAct=EBI-16079828, EBI-16168992;
CC       P87169; O14417: mad2; NbExp=4; IntAct=EBI-16079828, EBI-1269310;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MAD1 family. {ECO:0000305}.
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DR   EMBL; AF204761; AAG45711.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB09124.1; -; Genomic_DNA.
DR   PIR; T40364; T40364.
DR   RefSeq; NP_595516.1; NM_001021425.2.
DR   AlphaFoldDB; P87169; -.
DR   SMR; P87169; -.
DR   BioGRID; 276850; 97.
DR   DIP; DIP-61700N; -.
DR   IntAct; P87169; 2.
DR   STRING; 4896.SPBC3D6.04c.1; -.
DR   MaxQB; P87169; -.
DR   PaxDb; P87169; -.
DR   GeneID; 2540320; -.
DR   KEGG; spo:SPBC3D6.04c; -.
DR   PomBase; SPBC3D6.04c; mad1.
DR   eggNOG; KOG4593; Eukaryota.
DR   HOGENOM; CLU_403932_0_0_1; -.
DR   InParanoid; P87169; -.
DR   OMA; YMLLGYR; -.
DR   PhylomeDB; P87169; -.
DR   PRO; PR:P87169; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; IMP:PomBase.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR   GO; GO:0034501; P:protein localization to kinetochore; IMP:PomBase.
DR   InterPro; IPR008672; Mad1.
DR   PANTHER; PTHR23168; PTHR23168; 1.
DR   Pfam; PF05557; MAD; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Mitosis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..689
FT                   /note="Spindle assembly checkpoint component mad1"
FT                   /id="PRO_0000213796"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          50..423
FT                   /evidence="ECO:0000255"
FT   COILED          486..601
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  79890 MW;  2D2A34114F108C3A CRC64;
     MSSKLTVYQA TTSMADSPRD PFQSRSQLPR FLATSVKKPN LKKPSVNSAN ETKNPKLASL
     EFQLENLKND LKRKELEFER EQIELQRKLA EEHEQKNSLQ LRLTLVEKQL EEQSTSYQKE
     IEEVRNEKEA TQVKIHELLD AKWKEIAELK TQIEKNDQAL SEKNHEVMVS NQALQMKDTN
     LTNLEKLFAD SREQLETKCK ELAAAEQQLQ ELSVHNQQLE ESIKQVSSSI ELEKINAEQR
     LQISELEKLK AAQEERIEKL SSNNRNVEIL KEEKNDLESK LYRFEEYRDK VATLELENEK
     IQTELNSWKS LITNELPTPE AVSNKLVFLQ NTNANLGERV SSLESQLSNK PANQPLGANE
     KDAAHITELE TKLKELHEQN RRLQRQKSLA TQEIDLLREN LKSYDDEEAI LSEKNTDMKK
     LERIEGLVKL VDEYKLKLES MPVSLDVDET SDEVSLQKRR RKNEHKDAGY VTELYRKNQH
     LLFQVKEKTN IEAFLREQII TLESSIATLR QELAQVTEIN SCRVLQHRSN PTLKYERIKA
     AQLEMLNAEN SALKALLEDK KVDCLPIQSF KIAERKALDL KKEVAEREKR IQRLKEIFSV
     KSLEFREAVF SLFGYKLDFM PNGSVRVTST YSREDNTAFI FDGESSTMKL VGNPSGPEFE
     RLIRFWCDER KTIPGMLAAL TLELLDKND