PMT3_SCHPO
ID PMT3_SCHPO Reviewed; 117 AA.
AC O13351; O74186;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ubiquitin-like protein pmt3/smt3;
DE Flags: Precursor;
GN Name=pmt3; Synonyms=smt3, ubl2; ORFNames=SPBC365.06;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10567589; DOI=10.1128/mcb.19.12.8660;
RA Tanaka K., Nishide J., Okazaki K., Kato H., Niwa O., Nakagawa T.,
RA Matsuda H., Kawamukai M., Murakami Y.;
RT "Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for
RT multiple nuclear events, including the control of telomere length and
RT chromosome segregation.";
RL Mol. Cell. Biol. 19:8660-8672(1999).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-117.
RC STRAIN=358;
RA Pelletier M.F., Dignard D.;
RT "Ubiquitin-like protein (Schizosaccharomyces pombe).";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH RFP1.
RX PubMed=17502373; DOI=10.1074/jbc.m702652200;
RA Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.;
RT "Fission yeast Rnf4 homologs are required for DNA repair.";
RL J. Biol. Chem. 282:20388-20394(2007).
CC -!- FUNCTION: Required for chromosome segregation where it may be involved
CC in microtubule assembly. Loss of smt3 leads to an increase in telomere
CC length. {ECO:0000269|PubMed:10567589}.
CC -!- SUBUNIT: Interacts with rfp1. {ECO:0000269|PubMed:17502373}.
CC -!- INTERACTION:
CC O13351; P36592: rad22; NbExp=4; IntAct=EBI-966336, EBI-966242;
CC O13351; O13826: rfp1; NbExp=5; IntAct=EBI-966336, EBI-3647269;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567589}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB71541.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017187; BAA32595.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB44758.1; -; Genomic_DNA.
DR EMBL; AF019235; AAB71541.1; ALT_FRAME; mRNA.
DR PIR; T40313; T40313.
DR PIR; T43537; T43537.
DR RefSeq; NP_596035.1; NM_001021945.2.
DR AlphaFoldDB; O13351; -.
DR SMR; O13351; -.
DR BioGRID; 277443; 193.
DR IntAct; O13351; 10.
DR MINT; O13351; -.
DR STRING; 4896.SPBC365.06.1; -.
DR iPTMnet; O13351; -.
DR MaxQB; O13351; -.
DR PaxDb; O13351; -.
DR PRIDE; O13351; -.
DR EnsemblFungi; SPBC365.06.1; SPBC365.06.1:pep; SPBC365.06.
DR PomBase; SPBC365.06; pmt3.
DR VEuPathDB; FungiDB:SPBC365.06; -.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_0_1_1; -.
DR InParanoid; O13351; -.
DR OMA; AYCDRVG; -.
DR PhylomeDB; O13351; -.
DR Reactome; R-SPO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-SPO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-SPO-3065679; SUMO is proteolytically processed.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SPO-3108232; SUMO E3 ligases SUMOylate target proteins.
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-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SPO-4615885; SUMOylation of DNA replication 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 Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:O13351; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030998; C:linear element; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IDA:PomBase.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..111
FT /note="Ubiquitin-like protein pmt3/smt3"
FT /id="PRO_0000035961"
FT PROPEP 112..117
FT /evidence="ECO:0000255"
FT /id="PRO_0000035962"
FT DOMAIN 35..115
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
SQ SEQUENCE 117 AA; 12935 MW; 11C860EBEA172FD2 CRC64;
MSESPSANIS DADKSAITPT TGDTSQQDVK PSTEHINLKV VGQDNNEVFF KIKKTTEFSK
LMKIYCARQG KSMNSLRFLV DGERIRPDQT PAELDMEDGD QIEAVLEQLG GCTHLCL
