ID   MIS4_SCHPO              Reviewed;        1587 AA.
AC   Q09725;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Sister chromatid cohesion protein mis4;
DE   AltName: Full=SCC2 homolog;
GN   Name=mis4; ORFNames=SPAC31A2.05c;
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].
RX   PubMed=9808627; DOI=10.1101/gad.12.21.3408;
RA   Furuya K., Takahashi K., Yanagida M.;
RT   "Faithful anaphase is ensured by Mis4, a sister chromatid cohesion molecule
RT   required in S phase and not destroyed in G1 phase.";
RL   Genes Dev. 12:3408-3418(1998).
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [4]
RP   FUNCTION.
RX   PubMed=11882285; DOI=10.1016/s0960-9822(02)00692-9;
RA   Toyoda Y., Furuya K., Goshima G., Nagao K., Takahashi K., Yanagida M.;
RT   "Requirement of chromatid cohesion proteins rad21/scc1 and mis4/scc2 for
RT   normal spindle-kinetochore interaction in fission yeast.";
RL   Curr. Biol. 12:347-358(2002).
RN   [5]
RP   INTERACTION WITH SSL3.
RX   PubMed=16682348; DOI=10.1016/j.cub.2006.03.037;
RA   Bernard P., Drogat J., Maure J.-F., Dheur S., Vaur S., Genier S.,
RA   Javerzat J.-P.;
RT   "A screen for cohesion mutants uncovers ssl3, the fission yeast counterpart
RT   of the cohesin loading factor scc4.";
RL   Curr. Biol. 16:875-881(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Plays a structural role in chromatin. Chromatid cohesion
CC       molecule required for equal sister chromatid separation in anaphase.
CC       May form a stable link between chromatids in S phase that is split
CC       rather than removed in anaphase. Also required for spindle-kinetochore
CC       interaction in early mitosis and inhibit sister chromatid separation
CC       until the cleavage of Rad21 in anaphase. {ECO:0000269|PubMed:11882285}.
CC   -!- SUBUNIT: Interacts with ssl3. {ECO:0000269|PubMed:16682348}.
CC   -!- INTERACTION:
CC       Q09725; O13816: psc3; NbExp=2; IntAct=EBI-16083239, EBI-1131314;
CC       Q09725; O42649: psm3; NbExp=3; IntAct=EBI-16083239, EBI-1151879;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with
CC       chromosomes in a punctate fashion throughout the cell cycle.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA74749.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB016866; BAA74749.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CU329670; CAA90463.2; -; Genomic_DNA.
DR   PIR; T38603; S59644.
DR   RefSeq; NP_592917.2; NM_001018318.2.
DR   PDB; 6YUF; EM; 3.94 A; D=1-1587.
DR   PDBsum; 6YUF; -.
DR   AlphaFoldDB; Q09725; -.
DR   SMR; Q09725; -.
DR   BioGRID; 279111; 107.
DR   DIP; DIP-60691N; -.
DR   IntAct; Q09725; 2.
DR   STRING; 4896.SPAC31A2.05c.1; -.
DR   iPTMnet; Q09725; -.
DR   MaxQB; Q09725; -.
DR   PaxDb; Q09725; -.
DR   PRIDE; Q09725; -.
DR   EnsemblFungi; SPAC31A2.05c.1; SPAC31A2.05c.1:pep; SPAC31A2.05c.
DR   GeneID; 2542657; -.
DR   KEGG; spo:SPAC31A2.05c; -.
DR   PomBase; SPAC31A2.05c; mis4.
DR   VEuPathDB; FungiDB:SPAC31A2.05c; -.
DR   eggNOG; KOG1020; Eukaryota.
DR   HOGENOM; CLU_243880_0_0_1; -.
DR   InParanoid; Q09725; -.
DR   OMA; YVTKCLL; -.
DR   Reactome; R-SPO-2470946; Cohesin Loading onto Chromatin.
DR   PRO; PR:Q09725; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; EXP:PomBase.
DR   GO; GO:0032116; C:SMC loading complex; IDA:PomBase.
DR   GO; GO:0001671; F:ATPase activator activity; IDA:PomBase.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0140588; P:chromatin looping; IDA:PomBase.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; IBA:GO_Central.
DR   GO; GO:0062021; P:mitotic cohesin dsDNA (leading strand) loading; IDA:PomBase.
DR   GO; GO:0061780; P:mitotic cohesin loading; IDA:PomBase.
DR   GO; GO:0062022; P:mitotic cohesin ssDNA (lagging strand) loading; IDA:PomBase.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; EXP:PomBase.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:InterPro.
DR   GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR026003; Cohesin_HEAT.
DR   InterPro; IPR024986; Nipped-B_C.
DR   InterPro; IPR033031; Scc2/Nipped-B.
DR   PANTHER; PTHR21704; PTHR21704; 1.
DR   Pfam; PF12765; Cohesin_HEAT; 1.
DR   Pfam; PF12830; Nipped-B_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Chromosome; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1587
FT                   /note="Sister chromatid cohesion protein mis4"
FT                   /id="PRO_0000218601"
FT   REPEAT          775..812
FT                   /note="HEAT 1"
FT   REPEAT          814..851
FT                   /note="HEAT 2"
FT   REPEAT          853..888
FT                   /note="HEAT 3"
FT   REPEAT          890..927
FT                   /note="HEAT 4"
FT   REPEAT          1101..1140
FT                   /note="HEAT 5"
FT   REPEAT          1183..1220
FT                   /note="HEAT 6"
FT   REGION          140..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1587 AA;  180725 MW;  215B504316EB42D0 CRC64;
     MLFEMTPETF KKVNSSNRII KGLQYTPLAS SIPLENGLQN VLYPSSKFQN EPLQLNSEES
     SIMQRYVDML NPGATFVNDS ETFNFYKNAL SAMITEPAMP AMRVNASPVL DQKVCNSDSL
     SELNDFTKSL IQPSMLMCEP KEKPDASSIN TNRSSSDNGF LTPSSSPRSP SCSRVFNAVQ
     LCSPKKSKDD ITTPKKRLME DTYSPRESPS KIQRLQDVLL KQLQDTRLLI SQVIEAENSE
     DFSSNSLFIK REDDDGKHIS SHAIEKLYMA LTKLSRLGAC DKLLEEGSII LVKQILEKEL
     KELPVACYSI INLHDSLTQF PNLDFILKTT ALVLFIIFLV PSFKKLQNEE SILHLLNILH
     SIFEYTVPEA IDNIVQSKTS DARTSEIQHL SVLLQKVANV LNILSKVAHE IPLSEAVVIR
     IVYLFPKVST LDNSFKTKLP NCNSSSFDFL KAPLFQTLQY LFRLYPYQRD FIIEESLTNF
     SHLPTARSVS RTYRLSNGKS IQYYSTLFVR LIQSCSIQNL FDSEIVQSES KSTEALHSGN
     LTEHLKTVES ILSKSRHEEY RIANHIVAYL LSRSLKQNKT ESDNSFAILT KILLEDLLNM
     LSLPEWCGTE TIIRQFAMNL VMTVTNDKQA VSSKNAALDL ISLIVNKVLA LFDLSLFEKH
     NIPAPTNFND IISFIPSITR LNELSQVSFN HFYFLCKGDI SLENILPYNY NKWFSFLLQL
     RKVCNDSEAL KIIDNCIDKN MQKSQEGFQG PSPFKADEND EDIFIISLYH SSLFLNLKFF
     VSLIIGFLDS PQASLRTKCL RIINQMKTIP SILRTHPEVL AQIISKSNDQ SAIVRDTVLD
     LLGTYIMAYR ETIPQIYGCI ISGISDPSTI VRKRAIKQLC EVYEATEDLN IRVDIASKLL
     TRSNDEEETI SELSLEVLEK LWFSPASNEL DCQKGYEQLT FLEKQKLRVQ YFPILKLCAE
     PSTERHVLLV TSLKTMLTSK EEINLSTLHT QIRLLLSCLF NQLIEVVTED QVDESTKGIL
     YEIMSTLFVF SRAFPFLFDL SYLHLLKPYL RSASTIEEQR FLYYVVAIFR QVLPFQKEIS
     ESFLRSLESV LLQRLTKAGT ATLMEIVPCL CSLFTRLNDY ERLKKIVVSC LKSLEEARHS
     ENNFQKMVRL IDLIGLFSRY GDLNRINDDW KHSLDFISPE CDDAYVILLG YFQKLLKDAK
     GQLRIHIIDN MSRICLRETS LFISPLMLST LDMIIAENNV NEVSVLFKSF LELLAADEDL
     IFEADQKLSL KGKQNVQSNK SVDRDMLKGT KDKQWIEGVS ASLMQHFLPC ILDSCFSKNL
     RYSMLGIEIL KCIIHQGLVN PRMCFSTIIA LESNAIKETR EVAILLHTEL HRRHESLIDG
     LYAQSADLIF SLQKTEEYQT FKLGEFSPFQ SAYTIVSADK SSKSRKKLIM QILKPLKLDG
     IDLPSFTEEK VSFVSFCCVC LAGIPYVSIE EPLMIISTVD SVLATIGPTI TGWMKKLDHE
     RFKILAGINL CNLIYLKRYI KYAFSISDSS RPIREKKPLT LLNRGYVDLI TSDAKPDIVS
     KLVIKLFEEE NILSGEDQVE GEQLTVV