RAN1_SCHPO
ID RAN1_SCHPO Reviewed; 470 AA.
AC P08092; Q9UUD5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Negative regulator of sexual conjugation and meiosis;
DE EC=2.7.11.1;
GN Name=ran1; Synonyms=pat1; ORFNames=SPBC19C2.05;
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=3830131; DOI=10.1002/j.1460-2075.1986.tb04697.x;
RA McLeod M., Beach D.;
RT "Homology between the ran1+ gene of fission yeast and protein kinases.";
RL EMBO J. 5:3665-3671(1986).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, 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: This protein is a negative regulator of both sexual
CC conjugation and meiosis. It phosphorylates mei2. It blocks the onset of
CC meiosis until conjugation takes place.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X04728; CAA28437.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB52032.1; -; Genomic_DNA.
DR PIR; A25685; A25685.
DR PIR; T39796; T39796.
DR RefSeq; NP_595690.1; NM_001021587.2.
DR AlphaFoldDB; P08092; -.
DR SMR; P08092; -.
DR BioGRID; 277106; 75.
DR DIP; DIP-10N; -.
DR IntAct; P08092; 4.
DR STRING; 4896.SPBC19C2.05.1; -.
DR iPTMnet; P08092; -.
DR PaxDb; P08092; -.
DR PRIDE; P08092; -.
DR EnsemblFungi; SPBC19C2.05.1; SPBC19C2.05.1:pep; SPBC19C2.05.
DR GeneID; 2540580; -.
DR KEGG; spo:SPBC19C2.05; -.
DR PomBase; SPBC19C2.05; ran1.
DR VEuPathDB; FungiDB:SPBC19C2.05; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_172_3_1; -.
DR InParanoid; P08092; -.
DR OMA; ICCNACR; -.
DR PhylomeDB; P08092; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P08092; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0044843; P:cell cycle G1/S phase transition; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0110045; P:negative regulation of cell cycle switching, mitotic to meiotic cell cycle; IGI:PomBase.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; EXP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Conjugation; Kinase; Meiosis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..470
FT /note="Negative regulator of sexual conjugation and
FT meiosis"
FT /id="PRO_0000086602"
FT DOMAIN 18..295
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 155
FT /note="V -> G (in Ref. 1; CAA28437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52212 MW; D42143353ACC7828 CRC64;
MMRENPELLL GQVLGDSLRF VSIIGAGAYG VVYKAEDIYD GTLYAVKALC KDGLNEKQKK
LQARELALHA RVSSHPYIIT LHRVLETEDA IYVVLQYCPN GDLFTYITEK KVYQGNSHLI
KTVFLQLISA VEHCHSVGIY HRDLKPENIM VGNDVNTVYL ADFGLATTEP YSSDFGCGSL
FYMSPECQRE VKKLSSLSDM LPVTPEPIES QSSSFATAPN DVWALGIILI NLCCKRNPWK
RACSQTDGTY RSYVHNPSTL LSILPISREL NSLLNRIFDR NPKTRITLPE LSTLVSNCKN
LTRRLRPAPL VSSRYLAYQQ QQQQQQMNLQ QGIQGYPHQG YMPTQNIGFP WPPTPQFVSN
WNHCATPTIP VSLQVLTPNS SLKVDPTTPL TAPIHATESF WPSAAAAAAA VHNNANSYMP
ITPTPYPNNA KIFGYPNQPP LTPIPFTGFV LHPAPVGRAA DAVDPSRKSL
