PDS5C_ARATH
ID PDS5C_ARATH Reviewed; 873 AA.
AC Q8GUP3; Q8VZU8; Q9SZ55;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog C {ECO:0000305};
DE AltName: Full=Precocious dissociation of sisters protein 5-C {ECO:0000305};
DE Short=AtPDS5C {ECO:0000303|PubMed:26648949};
GN Name=PDS5C {ECO:0000303|PubMed:26648949};
GN OrderedLocusNames=At4g31880 {ECO:0000312|Araport:AT4G31880};
GN ORFNames=F11C18.80 {ECO:0000312|EMBL:CAB40758.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289, AND IDENTIFICATION BY
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [7]
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:0000250|UniProtKB:Q29RF7}.
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=CAB40758.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79906.1; 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; AL049607; CAB40758.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161579; CAB79906.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85972.1; -; Genomic_DNA.
DR EMBL; AY063818; AAL36174.1; -; mRNA.
DR EMBL; BT002315; AAN86148.1; -; mRNA.
DR PIR; T06310; T06310.
DR RefSeq; NP_194916.2; NM_119339.3.
DR PDB; 7DE9; X-ray; 1.71 A; A=597-662.
DR PDBsum; 7DE9; -.
DR AlphaFoldDB; Q8GUP3; -.
DR SMR; Q8GUP3; -.
DR STRING; 3702.AT4G31880.1; -.
DR PaxDb; Q8GUP3; -.
DR PRIDE; Q8GUP3; -.
DR ProteomicsDB; 180941; -.
DR EnsemblPlants; AT4G31880.1; AT4G31880.1; AT4G31880.
DR GeneID; 829318; -.
DR Gramene; AT4G31880.1; AT4G31880.1; AT4G31880.
DR Araport; AT4G31880; -.
DR TAIR; locus:2116787; AT4G31880.
DR eggNOG; KOG1525; Eukaryota.
DR InParanoid; Q8GUP3; -.
DR OMA; GGPINQS; -.
DR OrthoDB; 69768at2759; -.
DR PhylomeDB; Q8GUP3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUP3; baseline and differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; DNA damage; DNA repair; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..873
FT /note="Sister chromatid cohesion protein PDS5 homolog C"
FT /id="PRO_0000453277"
FT REPEAT 53..92
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 99..136
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 149..187
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 189..227
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REGION 266..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:7DE9"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:7DE9"
FT TURN 618..621
FT /evidence="ECO:0007829|PDB:7DE9"
FT STRAND 622..632
FT /evidence="ECO:0007829|PDB:7DE9"
FT TURN 633..636
FT /evidence="ECO:0007829|PDB:7DE9"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:7DE9"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:7DE9"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:7DE9"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:7DE9"
SQ SEQUENCE 873 AA; 94209 MW; B360D710734C9F0B CRC64;
MSDSDKELEN QIIEAGEKLI DPPSSLDELL SFLDKLFVSL AEVEQSPPDS MQNALTPLMK
GLVGGKLFKH SDVDVKVAVA ACISEITRIT APDAPYDDDQ MKEVFKLIVS SFEDLVDKSS
RSYAKRISIL ETVAKVRSCV VMLDLECDAL LIEMFQHFLK AIRDHHSGNV FSSMENIMTL
VLEESEDIPS EMLSPILHSV KKDDEISQVS RRLAEQVLSN CASKLKTYLT EAVKSSGVPL
DKYSNIVASI CEGTFSALQQ DQVVANEKED SQGHIKRETE VEKAAEISTP ERTDAPKDES
GKSGVSNGVA QQNDSSVDTD SMKKQDDTGA KDEPQQLDNP RNTDLNNTTE EKPDVEHQIE
EKENESSSVK QADLSKDSDI KEETEPAELL DSKDVLTSPP VDSSVTAATS SENEKNKSVQ
ILPSKTSGDE TANVSSPSMA EELPEQSVPK KTANQKKKES STEEVKPSAS IATEEVSEEP
NTSEPQVTKK SGKKVASSSK TKPTVPPSKK STSETKVAKQ SEKKVVGSDN AQESTKPKEE
KKKPGRGKAI DEESLHTSSG DNEKPAVSSG KLASKSKKEA KQTVEESPNS NTKRKRSLGQ
GKASGESLVG SRIKVWWPMD QAYYKGVVES YDAAKKKHLV IYDDGDQEIL YLKNQKWSPL
DESELSQDEE AADQTGQEED ASTVPLTKKA KTGKQSKMDN SSAKKGSGAG SSKAKATPAS
KSSKTSQDDK TASKSKDSKE ASREEEASSE EESEEEEPPK TVGKSGSSRS KKDISSVSKS
GKSKASSKKK EEPSKATTSS KSKSGPVKSV PAKSKTGKGK AKSGSASTPA SKAKESASES
ESEETPKEPE PATKAKSGKS QGSQSKSGKK RKR
