SDS22_SCHPO
ID SDS22_SCHPO Reviewed; 332 AA.
AC P22194;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 169.
DE RecName: Full=Protein phosphatase 1 regulatory subunit SDS22;
GN Name=sds22; ORFNames=SPAC4A8.12c;
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=1846086; DOI=10.1016/0092-8674(91)90216-l;
RA Ohkura H., Yanagida M.;
RT "S. pombe gene sds22+ essential for a midmitotic transition encodes a
RT leucine-rich repeat protein that positively modulates protein phosphatase-
RT 1.";
RL Cell 64:149-157(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=15335873; DOI=10.1016/0960-9822(93)90140-j;
RA Stone E.M., Yamano H., Kinoshita N., Yanagida M.;
RT "Mitotic regulation of protein phosphatases by the fission yeast sds22
RT protein.";
RL Curr. Biol. 3:13-26(1993).
RN [3]
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: Essential for the mitotic metaphase/anaphase transition.
CC Positively modulates protein phosphatase-1, possibly by forming a
CC repeating helical rod that is capable of enhancing a PP1-dependent
CC dephosphorylation activity.
CC -!- SUBUNIT: Physically interacts with the dis2 and sds21 phosphatases.
CC -!- INTERACTION:
CC P22194; P13681: dis2; NbExp=3; IntAct=EBI-16132213, EBI-4320127;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the SDS22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35342.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M57495; AAA35342.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329670; CAB11482.1; -; Genomic_DNA.
DR PIR; S43988; S43988.
DR RefSeq; NP_593824.1; NM_001019253.2.
DR AlphaFoldDB; P22194; -.
DR SMR; P22194; -.
DR BioGRID; 280012; 6.
DR DIP; DIP-61475N; -.
DR IntAct; P22194; 1.
DR STRING; 4896.SPAC4A8.12c.1; -.
DR MEROPS; X28.001; -.
DR MaxQB; P22194; -.
DR PaxDb; P22194; -.
DR EnsemblFungi; SPAC4A8.12c.1; SPAC4A8.12c.1:pep; SPAC4A8.12c.
DR GeneID; 2543597; -.
DR KEGG; spo:SPAC4A8.12c; -.
DR PomBase; SPAC4A8.12c; sds22.
DR VEuPathDB; FungiDB:SPAC4A8.12c; -.
DR eggNOG; KOG0531; Eukaryota.
DR HOGENOM; CLU_044236_0_0_1; -.
DR InParanoid; P22194; -.
DR OMA; YDNLIAH; -.
DR PhylomeDB; P22194; -.
DR PRO; PR:P22194; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:PomBase.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IPI:PomBase.
DR GO; GO:0072542; F:protein phosphatase activator activity; IGI:PomBase.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IPI:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:PomBase.
DR GO; GO:1901970; P:positive regulation of mitotic sister chromatid separation; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 10.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Leucine-rich repeat; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..332
FT /note="Protein phosphatase 1 regulatory subunit SDS22"
FT /id="PRO_0000071446"
FT REPEAT 63..82
FT /note="LRR 1"
FT REPEAT 83..104
FT /note="LRR 2"
FT REPEAT 105..126
FT /note="LRR 3"
FT REPEAT 127..148
FT /note="LRR 4"
FT REPEAT 149..170
FT /note="LRR 5"
FT REPEAT 171..192
FT /note="LRR 6"
FT REPEAT 193..214
FT /note="LRR 7"
FT REPEAT 216..237
FT /note="LRR 8"
FT REPEAT 238..259
FT /note="LRR 9"
FT REPEAT 260..281
FT /note="LRR 10"
FT DOMAIN 295..332
FT /note="LRRCT"
SQ SEQUENCE 332 AA; 38067 MW; CF7FBAD984E2A345 CRC64;
MSNVSSEDGI APETQLIIDD PDVQQIDADE DLLDDVPDDV DCVELIQSRI QSMASLGLER
FKNLQSLCLR QNQIKKIESV PETLTELDLY DNLIVRIENL DNVKNLTYLD LSFNNIKTIR
NINHLKGLEN LFFVQNRIRR IENLEGLDRL TNLELGGNKI RVIENLDTLV NLEKLWVGKN
KITKFENFEK LQKLSLLSIQ SNRITQFENL ACLSHCLREL YVSHNGLTSF SGIEVLENLE
ILDVSNNMIK HLSYLAGLKN LVELWASNNE LSSFQEIEDE LSGLKKLETV YFEGNPLQKT
NPAVYRNKVR LCLPQLRQID ATIIPKTSKQ FP
