PLI1_SCHPO
ID PLI1_SCHPO Reviewed; 727 AA.
AC O94451;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=E3 SUMO-protein ligase pli1;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase plil {ECO:0000305};
GN Name=pli1; ORFNames=SPAC1687.05;
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 12-107, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, INTERACTION WITH HUS5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-321; HIS-323 AND CYS-326.
RX PubMed=15359282; DOI=10.1038/sj.emboj.7600394;
RA Xhemalce B., Seeler J.-S., Thon G., Dejean A., Arcangioli B.;
RT "Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere
RT maintenance.";
RL EMBO J. 23:3844-3853(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-396, 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).
CC -!- FUNCTION: Acts as an E3 ligase mediating SUMO/Smt3 attachment to other
CC proteins. Involved in the maintenance of the centromere and in telomere
CC length. Regulates recombination, via extension sumoylation,
CC particularly within the heterochromatin repeats.
CC {ECO:0000269|PubMed:15359282}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with hus5/ubc9. {ECO:0000269|PubMed:15359282}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:15359282}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22599.1; -; Genomic_DNA.
DR EMBL; AB027790; BAA87094.1; -; Genomic_DNA.
DR PIR; T37748; T37748.
DR RefSeq; NP_593123.1; NM_001018519.2.
DR AlphaFoldDB; O94451; -.
DR SMR; O94451; -.
DR BioGRID; 278077; 96.
DR DIP; DIP-38715N; -.
DR IntAct; O94451; 3.
DR MINT; O94451; -.
DR STRING; 4896.SPAC1687.05.1; -.
DR iPTMnet; O94451; -.
DR SwissPalm; O94451; -.
DR MaxQB; O94451; -.
DR PaxDb; O94451; -.
DR PRIDE; O94451; -.
DR EnsemblFungi; SPAC1687.05.1; SPAC1687.05.1:pep; SPAC1687.05.
DR GeneID; 2541580; -.
DR KEGG; spo:SPAC1687.05; -.
DR PomBase; SPAC1687.05; pli1.
DR VEuPathDB; FungiDB:SPAC1687.05; -.
DR eggNOG; KOG2169; Eukaryota.
DR HOGENOM; CLU_020537_1_0_1; -.
DR InParanoid; O94451; -.
DR OMA; ECKVREQ; -.
DR PhylomeDB; O94451; -.
DR Reactome; R-SPO-3232118; SUMOylation of transcription factors.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR UniPathway; UPA00886; -.
DR PRO; PR:O94451; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0030999; P:linear element assembly; IMP:PomBase.
DR GO; GO:0110027; P:negative regulation of DNA strand resection involved in replication fork processing; IMP:PomBase.
DR GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; EXP:PomBase.
DR GO; GO:0000019; P:regulation of mitotic recombination; IMP:PomBase.
DR GO; GO:0010520; P:regulation of reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0032207; P:regulation of telomere maintenance via recombination; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..727
FT /note="E3 SUMO-protein ligase pli1"
FT /id="PRO_0000218986"
FT DOMAIN 18..52
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 108..261
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT ZN_FING 290..371
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 408..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 321
FT /note="C->S: Reduction in sumoylation of rad22."
FT /evidence="ECO:0000269|PubMed:15359282"
FT MUTAGEN 323
FT /note="H->A: Reduction in sumoylation of rad22."
FT /evidence="ECO:0000269|PubMed:15359282"
FT MUTAGEN 326
FT /note="C->S: Reduction in sumoylation of rad22."
FT /evidence="ECO:0000269|PubMed:15359282"
SQ SEQUENCE 727 AA; 80723 MW; 56228A04888DD235 CRC64;
MNQANFLQEL PNVLKRLETG LIIPQLKDIL RVFGLRLSGT KAELITRIKQ LIERIAIENN
TTSWEALKKA IDGDVTSAVC ILKYNTYQIY SAAAPIAPPS SASGNRSYSR PFAPVVHSRI
RFRKSPFYDI LEQFNAPFVV PACVGTRNTI SFSFHVTPPA LSKLLNDPKQ YRVYLFSTPS
ETIGFGNCLM EFPTPQMELR INNQVAHANY RRLKGKPGTT NPADITDLVS KYAGPPGNNV
VIYYMNSTKS YSVVVCFVKV YTIENLVDQI KSRKAESKEK IIERIKNDNQ DADIIATSTD
ISLKCPLSFS RISLPVRSVF CKHIQCFDAS AFLEMNKQTP SWMCPVCASH IQFSDLIIDG
FMQHILESTP SNSETITVDP EGNWKLNTFD EPVESSEDEF VPKEKVIELS DGEGISTMAN
KSNDQPTRRA STHNSGPPAK RKRESLVIDL TISDDDENVA TSTTESPSNA TKENSLSRNV
QSPNIDTAIS NRSTNVRHGH PGFKDYTVEN SPASRERSTS ESAQSSVHMG YAGEGGLLSG
ALRAPSQQNN NNSNTQHSIN LHTIVPSPYE PPLSVTPSTA ITNLSIPESN RTNSSASSKS
FTMNDLILPP LHLKNTTQTN NAHEDAQSSN LSQNHSLFYE RIPQRPSYRI EKQNKGIYED
ENEQSISAMP IPRAHPQLPK NLLSQTAGPL WDEQQDAQVD WNSELQSNNS YHNSGFEGTG
NTFQSID
