ID   KMS1_SCHPO              Reviewed;         607 AA.
AC   P87245;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Karyogamy meiotic segregation protein 1;
GN   Name=kms1; ORFNames=SPAC3A11.05c;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9150257; DOI=10.1007/s004380050412;
RA   Shimanuki M., Miki F., Ding D.-Q., Chikashige Y., Hiraoka Y., Horio T.,
RA   Niwa O.;
RT   "A novel fission yeast gene, kms1+, is required for the formation of
RT   meiotic prophase-specific nuclear architecture.";
RL   Mol. Gen. Genet. 254:238-249(1997).
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).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10899136; DOI=10.1093/emboj/19.14.3831;
RA   Niwa O., Shimanuki M., Miki F.;
RT   "Telomere-led bouquet formation facilitates homologous chromosome pairing
RT   and restricts ectopic interaction in fission yeast meiosis.";
RL   EMBO J. 19:3831-3840(2000).
RN   [4]
RP   INTERACTION WITH SAD1.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [5]
RP   INTERACTION WITH MCP6.
RX   PubMed=16111942; DOI=10.1016/j.cub.2005.07.058;
RA   Tanaka K., Kohda T., Yamashita A., Nonaka N., Yamamoto M.;
RT   "Hrs1p/Mcp6p on the meiotic SPB organizes astral microtubule arrays for
RT   oscillatory nuclear movement.";
RL   Curr. Biol. 15:1479-1486(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15654021; DOI=10.1242/jcs.01629;
RA   Saito T.T., Tougan T., Okuzaki D., Kasama T., Nojima H.;
RT   "Mcp6, a meiosis-specific coiled-coil protein of Schizosaccharomyces pombe,
RT   localizes to the spindle pole body and is required for horsetail movement
RT   and recombination.";
RL   J. Cell Sci. 118:447-459(2005).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Has a role in karyogamy, recombination and segregation during
CC       meiosis. Although it has been shown to associate with the spindle pole
CC       body it is unlikely to be involved in its formation or maintenance.
CC       {ECO:0000269|PubMed:9150257}.
CC   -!- SUBUNIT: Interacts with mcp1 and sad1. {ECO:0000269|PubMed:14655046,
CC       ECO:0000269|PubMed:16111942}.
CC   -!- INTERACTION:
CC       P87245; Q10336: mcp6; NbExp=2; IntAct=EBI-1542265, EBI-1562149;
CC       P87245; Q09825: sad1; NbExp=5; IntAct=EBI-1542265, EBI-929731;
CC       P87245; O74843: sif1; NbExp=3; IntAct=EBI-1542265, EBI-1542307;
CC       P87245; O94531: ufe1; NbExp=3; IntAct=EBI-1542265, EBI-1542297;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, spindle pole body {ECO:0000269|PubMed:10899136,
CC       ECO:0000269|PubMed:15654021, ECO:0000269|PubMed:16823372}.
CC       Note=Associates with the spindle pole body (SPB).
CC   -!- DISRUPTION PHENOTYPE: Cells show a distorted structure of the meiotic
CC       prophase nucleus but are able to complete mitosis successfully.
CC       {ECO:0000269|PubMed:9150257}.
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DR   EMBL; D84439; BAA20460.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16381.1; -; Genomic_DNA.
DR   PIR; T43222; T43222.
DR   RefSeq; NP_594198.1; NM_001019622.2.
DR   AlphaFoldDB; P87245; -.
DR   SMR; P87245; -.
DR   BioGRID; 279502; 15.
DR   IntAct; P87245; 5.
DR   STRING; 4896.SPAC3A11.05c.1; -.
DR   iPTMnet; P87245; -.
DR   MaxQB; P87245; -.
DR   PaxDb; P87245; -.
DR   PRIDE; P87245; -.
DR   EnsemblFungi; SPAC3A11.05c.1; SPAC3A11.05c.1:pep; SPAC3A11.05c.
DR   GeneID; 2543069; -.
DR   KEGG; spo:SPAC3A11.05c; -.
DR   PomBase; SPAC3A11.05c; kms1.
DR   VEuPathDB; FungiDB:SPAC3A11.05c; -.
DR   HOGENOM; CLU_454281_0_0_1; -.
DR   OMA; EIGIQKW; -.
DR   PhylomeDB; P87245; -.
DR   PRO; PR:P87245; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR   GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; IPI:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0031965; C:nuclear membrane; IC:PomBase.
DR   GO; GO:1990612; C:Sad1-Kms1 LINC complex; EXP:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; EXP:PomBase.
DR   GO; GO:0045141; P:meiotic telomere clustering; IMP:PomBase.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   SUPFAM; SSF47473; SSF47473; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Meiosis;
KW   Reference proteome.
FT   CHAIN           1..607
FT                   /note="Karyogamy meiotic segregation protein 1"
FT                   /id="PRO_0000084310"
FT   REGION          83..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   607 AA;  69241 MW;  216A1D5CA93C9550 CRC64;
     MLNERDFDLI FDSYDFKHEG KVHLSNFLPI INDLQLLHPA SAPPLLSEFQ KQCTLEFVRQ
     NADLSITKDN FRDVYKKLTE NEDDSFANQA EKPSMEQQNS KNSIKEDANE HSVNSAHSKS
     SSNASPESLN PSQMMSKRLS LPPMSQFTDS DFVNILRTPF AQSTPLNRNT SSRNTEMPLV
     RKDKPDFSNG HHDLIKQITE LQDMLDKARD QARKKSRTVD ILEGKVNELT HQLNMADSKY
     NESKVANNSQ NNQIKTLKAQ NLNIHKNFQK IQSELIQTNS GLYSTKKELS ALQVRYATLL
     RKFTDQTKKI EELSLAASRS SENENTIRRL ALENHELKNS NNQLNNHIDD LTREKHLIAL
     SNNPKGDEFL SPSNLDEMVY SKEVGLSFTQ PSVCISIPAV GMRESEELRE LEFKCKQQKK
     TIEECKHISQ SLQSSLTAES SRNKELVAGF LMLSEEIGIQ KWIIQSLSKM SPTLNDFCRR
     YDSSMPTYEE SSHECTVLSS FSDDETGLMA TNTTMNNSSK DFMASQDTVN ADNPHFLATK
     GQPLLLLSVM KSNILRLFYV LFLFACFYGL DYILCAELLQ AFLRVVFTFC EHIIILLYGR
     YELVQPS