PDS5D_ARATH
ID PDS5D_ARATH Reviewed; 826 AA.
AC A8MRD9; A0A1P8ARR1; Q9SAI0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog D {ECO:0000305};
DE AltName: Full=Precocious dissociation of sisters protein 5-D {ECO:0000305};
DE Short=AtPDS5D {ECO:0000303|PubMed:26648949};
GN Name=PDS5D {ECO:0000303|PubMed:26648949};
GN Synonyms=SL2 {ECO:0000303|PubMed:26826387};
GN OrderedLocusNames=At1g80810 {ECO:0000312|Araport:AT1G80810};
GN ORFNames=F23A5.16 {ECO:0000312|EMBL:AAF14668.1};
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 53-782 (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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).
RN [5]
RP GENE FAMILY.
RX PubMed=26826387; DOI=10.1016/j.bbrc.2016.01.151;
RA Sadiq I., Keren I., Citovsky V.;
RT "Plant homologs of mammalian MBT-domain protein-regulated KDM1 histone
RT lysine demethylases do not interact with plant Tudor/PWWP/MBT-domain
RT proteins.";
RL Biochem. Biophys. Res. Commun. 470:913-916(2016).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8MRD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MRD9-2; Sequence=VSP_061118;
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=AAF14668.1; Type=Erroneous gene model prediction; 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; AC011713; AAF14668.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36453.2; -; Genomic_DNA.
DR EMBL; CP002684; ANM59348.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59349.1; -; Genomic_DNA.
DR EMBL; AY050954; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F96840; F96840.
DR RefSeq; NP_001319432.1; NM_001335011.1. [A8MRD9-2]
DR RefSeq; NP_001321712.1; NM_001335012.1. [A8MRD9-1]
DR RefSeq; NP_001321713.1; NM_001335013.1. [A8MRD9-2]
DR SMR; A8MRD9; -.
DR PaxDb; A8MRD9; -.
DR PRIDE; A8MRD9; -.
DR ProteomicsDB; 185687; -.
DR ProteomicsDB; 211775; -.
DR EnsemblPlants; AT1G80810.2; AT1G80810.2; AT1G80810. [A8MRD9-2]
DR EnsemblPlants; AT1G80810.3; AT1G80810.3; AT1G80810. [A8MRD9-1]
DR EnsemblPlants; AT1G80810.4; AT1G80810.4; AT1G80810. [A8MRD9-2]
DR GeneID; 844420; -.
DR Gramene; AT1G80810.2; AT1G80810.2; AT1G80810. [A8MRD9-2]
DR Gramene; AT1G80810.3; AT1G80810.3; AT1G80810. [A8MRD9-1]
DR Gramene; AT1G80810.4; AT1G80810.4; AT1G80810. [A8MRD9-2]
DR KEGG; ath:AT1G80810; -.
DR Araport; AT1G80810; -.
DR TAIR; locus:2025712; AT1G80810.
DR InParanoid; A8MRD9; -.
DR OMA; KWTETEA; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; A8MRD9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A8MRD9; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007064; P:mitotic sister chromatid cohesion; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; DNA damage;
KW DNA repair; Mitosis; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..826
FT /note="Sister chromatid cohesion protein PDS5 homolog D"
FT /id="PRO_0000453278"
FT REPEAT 18..54
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 55..94
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 151..188
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 189..226
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 230..267
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 424..461
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REGION 261..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 770..825
FT /evidence="ECO:0000255"
FT MOTIF 281..288
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 357..364
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 266..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Basic and acidic 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 529..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..723
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..799
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /id="VSP_061118"
FT CONFLICT 550
FT /note="Missing (in Ref. 3; AY050954)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="E -> EQ (in Ref. 3; AY050954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 93511 MW; B67574C63A4B96B2 CRC64;
MTAIVGFDQL SKALIDAGTN LLSPPSSTDD LLTLLDETES LLKNVEQDQP LSMQSALIPS
RNALVSVDLL SHPDSDVRVS VVSCLTEIVR ITAPETPYSD DLMKEIFRLT IEAFEKLADA
SSRSYKKAEF VLDNVAKVKS CLVMLDLECY DLILQMFRNF FKFIRSDHPQ LVFSSMELIM
IAIIDETEQV STDLLDSLLA TVKKENQNVS PMSWSLAEKV LSRCARKLKP YIIEALKSRG
TSLDMYSPVV SSICQSVFNT PKVHSPVNTK EHEEKLDLGH SRKENLSKSS SKRPARHETR
GINEKEKVRN GNKSSLLKQS LKQVRSESTD AEITGKRGRK PNSLMNPEDY DISWLSGKRD
PLKTSSNKKI QKKGSGGVSS LGKVPAKKTP LPKENSPATS SRSLTGSLKR SRVKMDESDY
DSDSLSSPRL KKLASCFRDE EPNQEDDRKI GNSSKQTRSK NGLEKSQKTA KKKPVVEAKI
VNSSGKRLSA RSVAKRRNLE RAPLDTLVPQ SSKRKKMVSQ VAARQLANES EEETPKSHPT
RRRTVRKEVE SDGFGEDLVG KRVNIWWPLD KTFYEGVIDS YCTRKKMHRV IYSDGDSEEL
NLTEERWELL EDDTSADEDK EIDLPESIPL SDIMQRQKVK KSKNVAVSVE PTSSSGVRSS
SRTLMKKDCG KRLNKQVEKT REGKNLRSLK ELNAETDRTA EEQEVSLEAE SDDRSEEQEY
EDDCSDKKEQ SQDKGVEAET KEEEKQYPNS EGESEGEDSE SEEEPKWRET DDMEDDEEEE
EEEIDHMEDE AEEEKEEVDD KEASANMSEI EKEEEEEEED EEKRKS
