PDS5A_ARATH
ID PDS5A_ARATH Reviewed; 1605 AA.
AC B6EUB3; B3H5K3; Q0WNL7; Q9FIL0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 23-FEB-2022, entry version 92.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog A {ECO:0000305};
DE AltName: Full=Precocious dissociation of sisters protein 5-A {ECO:0000305};
DE Short=AtPDS5A {ECO:0000303|PubMed:26648949};
DE Short=PDS5 {ECO:0000303|PubMed:25387881};
GN Name=PDS5A {ECO:0000303|PubMed:26648949};
GN OrderedLocusNames=At5g47690 {ECO:0000312|Araport:AT5G47690};
GN ORFNames=MNJ7.28 {ECO:0000312|EMBL:BAB11316.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1584 AND THR-1588, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1274; SER-1299; SER-1524;
RP SER-1562 AND SER-1584, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
RN [10]
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 (By similarity). Interacts
CC with DEK3 (PubMed:25387881). {ECO:0000250|UniProtKB:Q29RF7,
CC ECO:0000269|PubMed:25387881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B6EUB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B6EUB3-2; Sequence=VSP_061116, VSP_061117;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016886; BAB11316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB025628; BAB11316.1; JOINED; Genomic_DNA.
DR EMBL; AB028612; BAB11316.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95551.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95553.1; -; Genomic_DNA.
DR EMBL; AK229421; BAF01282.1; -; mRNA.
DR RefSeq; NP_001119390.1; NM_001125918.2. [B6EUB3-2]
DR RefSeq; NP_199580.3; NM_124143.4. [B6EUB3-1]
DR SMR; B6EUB3; -.
DR IntAct; B6EUB3; 1.
DR STRING; 3702.AT5G47690.3; -.
DR iPTMnet; B6EUB3; -.
DR PRIDE; B6EUB3; -.
DR ProteomicsDB; 200166; -.
DR ProteomicsDB; 206170; -.
DR EnsemblPlants; AT5G47690.1; AT5G47690.1; AT5G47690. [B6EUB3-1]
DR EnsemblPlants; AT5G47690.3; AT5G47690.3; AT5G47690. [B6EUB3-2]
DR GeneID; 834820; -.
DR Gramene; AT5G47690.1; AT5G47690.1; AT5G47690. [B6EUB3-1]
DR Gramene; AT5G47690.3; AT5G47690.3; AT5G47690. [B6EUB3-2]
DR Araport; AT5G47690; -.
DR TAIR; locus:2169058; AT5G47690.
DR eggNOG; KOG1525; Eukaryota.
DR HOGENOM; CLU_002325_1_0_1; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; B6EUB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B6EUB3; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; 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 Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; DNA damage; DNA repair;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1605
FT /note="Sister chromatid cohesion protein PDS5 homolog A"
FT /id="PRO_0000453275"
FT REPEAT 50..89
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 96..136
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 146..183
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 184..221
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 261..298
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 302..339
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 341..378
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 380..416
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 552..591
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 644..681
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 723..758
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 821..860
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 961..1000
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1050..1088
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REGION 1155..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1226..1233
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1426..1433
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1167..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1538..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 1588
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 1325
FT /note="R -> RQ (in isoform 2)"
FT /id="VSP_061116"
FT VAR_SEQ 1506
FT /note="K -> IE (in isoform 2)"
FT /id="VSP_061117"
FT CONFLICT 183
FT /note="E -> G (in Ref. 4; BAF01282)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="K -> E (in Ref. 4; BAF01282)"
FT /evidence="ECO:0000305"
FT CONFLICT 1388
FT /note="K -> R (in Ref. 4; BAF01282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1605 AA; 181210 MW; 0734F636A28A560F CRC64;
MAQKPEEQLK ELGSKLDLAP VSKDSLLKLL KEAAVCLSEL EQSPPPAVLK SIQPFLDAVI
KPEILNHQDK DVKLLVASCV SEITRITAPE APYSDNIMKD IFQLIVSAFA GLNDVSGPSF
GRRVLILETV AKYRSCVVML DLECDDLVKE VFTTFLDVAR DDHPEIVFSS MQNIMIVLLE
ESEDVQEHLL LILLSKLGRN RSDVRDAARR LAMKVIEHCA PKVESDIKQF LISSMSGDSR
FSSSQIDYHE VIYDLYRCAP QALSGVAPYL TGELLADKLE TRLKVVGLVG ELFSLPGRVI
SEEFDSIFLE FLKRLTDRVV EVRMAILDHI KDCLLSDPLR AEASQIISAL CDRLLDYDEN
IRKQVVAVIC DVSVSALTSI PVDTMKLVAE RLRDKAILVK TYTMERLTEL FRVYCLRCAD
GKVDTGDFNW IPGKILRCLY DKDFRSDTIE YILCSSLFPS DFSVRDKVKH WIQIFSGFDK
VETKAFEKIL EQRQRIQQEM QRYLSIKQTQ QTADAPEIQK KILFGFRVMS RAFSDPPKTE
QNFLILDQLK DANIWKILTN LLDPNTSITQ ASRIRDDMLK ILSEKHSLYD FLSTLSIKCS
YLLFSKEYVK EILAEVSVRK SSKNTLGIQP CMDFLGLLAC FCPSLFDGAE EELISFLKDD
DEMMKEGTLK ILAKAGGTIR ENLIVLASSV DLLLERICVE GNRKQAKYAV HALASITKDD
GLKSLSVLYK RLVDMLEDKR YQPAVLQCLG CIAQIAMPVY ETRESEVVEF IRSKILKLKS
ETVDDKKLSW DDKSEICQLK IYGIKTLVKS YLPFKDAQLR AGVDDLLGIL KNILSFGEVS
EDLESSSVDK AHLRLAAAKA VLRLSRHWDD KIPIEIFHLT LKTPEIPFPT AKKIFLGKVH
QYVKDRVLEM KYACSFLFDI TGSNVLESEE DKHNLADIIQ HSYQTKVRKI SAQTDANSVT
LYPHHILPYL VHALAHHSCP DVEKCKDVKE YEMIYRQLYL IISMLLHKEE DGKTEDIDKE
REYVPTIILI FHSIKQSEDV TDATKSKNSH AICELGLSII NHLTQKEPDL QGEITPVSLP
PTLYKPSEKV EGDKSQVGEE KLWLADETVL LHFRALKLES HADASVIPQT SENEVMIDGE
SDGNEIPLGK IVERLRAQGT KTRKGKKNKS VPAEDENGKN DVDVLKMVRE INLDHLQMLD
KFESSNGHKH SPSERAEICQ RDQKGNKRNV GDATSVVSVP KRRRSSSGHS PYKFSNSGPK
VQLKASEDEL HLESDMDKNV SLDSHDENSD QEKMLESISP RKRKKSLSSK LKITESDWAL
TDVERSRSAG GGDSKLKSAS GSMKKRKNVS GLAKCSTKEN KLVNDELIGC RIEVWWPMDK
RFYEGTVKSY DSTKQRHVIL YEDGDVEVLN LKKEQWELID TGGKTAKKSR TSKGNSKKKR
SSGSKPKNPD GVQRDEDPVT TTPKGKRTPK KNLKQLHPKD TPKSLSLEHE KVESRNKKRR
SSALPKTEYS GEAGEEKSES EGKSLKEGED DEEVVNKEED LQEAKTESSG DAEGKEAEHD
DSDTEGKQEN NEMEREAEEN AETSDNETLG AWKSKVGKSI SRTAI
