PDS5E_ARATH
ID PDS5E_ARATH Reviewed; 990 AA.
AC Q9S9P0; Q0WPH2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog E {ECO:0000305};
DE AltName: Full=Precocious dissociation of sisters protein 5-E {ECO:0000305};
DE Short=AtPDS5E {ECO:0000303|PubMed:26648949};
GN Name=PDS5E {ECO:0000303|PubMed:26648949};
GN OrderedLocusNames=At1g15940 {ECO:0000312|Araport:AT1G15940};
GN ORFNames=T24D18.4 {ECO:0000312|EMBL:AAF18491.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-990.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26648949; DOI=10.3389/fpls.2015.01034;
RA Pradillo M., Knoll A., Oliver C., Varas J., Corredor E., Puchta H.,
RA Santos J.L.;
RT "Involvement of the cohesin cofactor PDS5 (SPO76) during meiosis and DNA
RT repair in Arabidopsis thaliana.";
RL Front. Plant Sci. 6:1034-1034(2015).
CC -!- FUNCTION: Cohesin cofactor dispensable during the meiotic division but
CC playing an important role in DNA repair by homologous recombination
CC (HR) probably by helping SMC5/SMC6 complex (PubMed:26648949). Regulator
CC of sister chromatid cohesion in mitosis which may stabilize cohesin
CC complex association with chromatin (PubMed:26648949). May couple sister
CC chromatid cohesion during mitosis to DNA replication (By similarity).
CC Cohesion ensures that chromosome partitioning is accurate in both
CC meiotic and mitotic cells and plays an important role in DNA repair
CC (PubMed:26648949). {ECO:0000250|UniProtKB:Q29RF7,
CC ECO:0000269|PubMed:26648949}.
CC -!- SUBUNIT: Interacts with the cohesin complex.
CC {ECO:0000250|UniProtKB:Q29RF7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- DISRUPTION PHENOTYPE: Weak impact on meiosis such as formation of some
CC chromosome bridges at late anaphase I and telophase I in forming
CC pollen, but severe effects on development, fertility, somatic
CC homologous recombination (HR) and DNA repair, especially in plants
CC lacking PDS5A, PDS5B, PDS5C, PDS5D and PDS5E.
CC {ECO:0000269|PubMed:26648949}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR EMBL; AC010924; AAF18491.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29387.1; -; Genomic_DNA.
DR EMBL; AK229098; BAF00977.1; -; mRNA.
DR PIR; H86293; H86293.
DR RefSeq; NP_173046.2; NM_101462.5.
DR AlphaFoldDB; Q9S9P0; -.
DR SMR; Q9S9P0; -.
DR STRING; 3702.AT1G15940.1; -.
DR PaxDb; Q9S9P0; -.
DR PRIDE; Q9S9P0; -.
DR ProteomicsDB; 176959; -.
DR EnsemblPlants; AT1G15940.1; AT1G15940.1; AT1G15940.
DR GeneID; 838164; -.
DR Gramene; AT1G15940.1; AT1G15940.1; AT1G15940.
DR KEGG; ath:AT1G15940; -.
DR Araport; AT1G15940; -.
DR TAIR; locus:2200557; AT1G15940.
DR eggNOG; KOG1525; Eukaryota.
DR HOGENOM; CLU_008968_0_0_1; -.
DR InParanoid; Q9S9P0; -.
DR OMA; METIMIT; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; Q9S9P0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9P0; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0035825; P:homologous recombination; IMP:UniProtKB.
DR GO; GO:0009556; P:microsporogenesis; IGI:TAIR.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; DNA damage; DNA repair; Mitosis; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..990
FT /note="Sister chromatid cohesion protein PDS5 homolog E"
FT /id="PRO_0000453279"
FT REPEAT 31..57
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 58..96
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 153..190
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 191..228
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 232..269
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REGION 262..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 458..465
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 539..546
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 583..590
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 677..684
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 715..722
FT /note="Nuclear localization signal 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 266..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 990 AA; 109595 MW; 47854068D1B444FB CRC64;
MGPLVEATEF SKEQALTDAA ENLLKPHFST DATLSLLEVM ESLLATVEQD LSSSVQKALH
PPMRALVSAD LLRNPDSDVR VSVVSCLTEI MRITAPEAPY NDEQMKDIFQ VTIEAFEKLA
DASSRSYRKA EVILETVAKV RSSLVMLDLE CDDLVLEMFQ RFLKIIRPDH PQLVLVSMET
IMITVIDESE EVPMDLLEIL LTTVKKDSQD VSPAALTLVE KVLSSCTCKL QPCIMEALKS
SGTSLDMYSP VVSSICQSEF ATTQAHNDVK PKDNEADEKI SEGQVVPSDS LEDKLNLGLS
RKGTRSKRSA RGGTRRANGD EKVITANEGL SESTDAETAS GSTRKRGWKP KSLMNPEEGY
SFKTSSSKKV QEKELGDSSL GKVAAKKVPL PSKVGQTNQS VVISLSSSGR ARTGSRKRSR
TKMEETDHDV SSVATQPAKK QTVKKTNPAK EDLTKSNVKK HEDGIKTGKS SKKEKADNGL
AKTSAKKPLA ETMMVKPSGK KLVHSDAKKK NSEGASMDTP IPQSSKSKKK DSRATTPATK
KSEQAPKSHP KMKRIAGEEV ESNTNELGEE LVGKRVNVWW PLDKKFYEGV IKSYCRVKKM
HQVTYSDGDV EELNLKKERF KIIEDKSSAS EDKEDDLLES TPLSAFIQRE KSKKRKIVSK
NVEPSSSPEV RSSMQTMKKK DSVTDSIKQT KRTKGALKAV SNEPESTTGK NLKSLKKLNG
EPDKTRGRTG KKQKVTQAMH RKIEKDCDEQ EDLETKDEED SLKLGKESDA EPDRMEDHQE
LPENHNVETK TDGEEQEAAK EPTAESKTNG EEPNAEPETD GKEHKSLKEP NAEPKSDGEE
QEAAKEPNAE LKTDGENQEA AKELTAERKT DEEEHKVADE VEQKSQKETN VEPEAEGEEQ
KSVEEPNAEP KTKVEEKESA KEQTADTKLI EKEDMSKTKG EEIDKETYSS IPETGKVGNE
AEEDDQRVIK ELEEESDKAE VSTTVLEVDP
