YOCC_SCHPO
ID YOCC_SCHPO Reviewed; 438 AA.
AC O74398;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=LIM domain-containing protein C4F6.12;
GN ORFNames=SPBC4F6.12;
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-96, AND
RP IDENTIFICATION BY 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).
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DR EMBL; CU329671; CAA20732.1; -; Genomic_DNA.
DR PIR; T40509; T40509.
DR RefSeq; NP_596112.1; NM_001022029.2.
DR AlphaFoldDB; O74398; -.
DR SMR; O74398; -.
DR BioGRID; 277373; 29.
DR STRING; 4896.SPBC4F6.12.1; -.
DR iPTMnet; O74398; -.
DR MaxQB; O74398; -.
DR PaxDb; O74398; -.
DR PRIDE; O74398; -.
DR EnsemblFungi; SPBC4F6.12.1; SPBC4F6.12.1:pep; SPBC4F6.12.
DR GeneID; 2540856; -.
DR KEGG; spo:SPBC4F6.12; -.
DR PomBase; SPBC4F6.12; -.
DR VEuPathDB; FungiDB:SPBC4F6.12; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_642755_0_0_1; -.
DR InParanoid; O74398; -.
DR PRO; PR:O74398; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:1990808; F:F-bar domain binding; IPI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; EXP:PomBase.
DR GO; GO:0044837; P:actomyosin contractile ring organization; IMP:PomBase.
DR GO; GO:1902405; P:mitotic actomyosin contractile ring localization; IMP:PomBase.
DR GO; GO:1904498; P:protein localization to mitotic actomyosin contractile ring; IMP:PomBase.
DR GO; GO:1903499; P:regulation of mitotic actomyosin contractile ring assembly; IGI:PomBase.
DR GO; GO:1903471; P:regulation of mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..438
FT /note="LIM domain-containing protein C4F6.12"
FT /id="PRO_0000315960"
FT DOMAIN 256..316
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 318..375
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 376..435
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 438 AA; 49030 MW; 74B415AECBBDF3E0 CRC64;
MHSPIPELPR FERRLTGPRA APSSPVSTNG SPLNNLVRSR LSDGALNFTG GRIATPLPQP
SLKTPESPLS KRNPTIKQNR VRFDLPDDEL SRSNVSSPEK TLLTSASTST FDSLKKELLP
ELPSLAYSDD DEFPSSPEEL NSHVNYPDVR NVYDCHTGLQ PLVDHDCIED RQKTFASKQL
PTLPLQKSSK LSNRRPALHS FHSAPANSLY PLPTPTSQLP SNLSSNNLFQ SDSLKPSMVS
SHTSTKPVLY RGNSEKSCHS CGGSLRAGRI ISASGKKLHP QCFKCDTCSQ NLEHVGFYYR
EGKFYCHLDY HEQFSPRCKH CKTPIEDQAV HINNDWFHEN HHFCAGCSEV FNVNIPCIYR
DDLYWCQTCY DNKYAVKCKK CRKPILGISV KGSDGEYHSQ CWTCGACNAL LGDEGYFMIE
NTPICRPCKA ISVKFNLD
