PATH1_ARATH
ID PATH1_ARATH Reviewed; 782 AA.
AC F4J077; Q0WPV0; Q9LHJ0;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Protein PAT1 homolog 1 {ECO:0000305};
DE Short=AtPAT1H1 {ECO:0000305};
DE AltName: Full=Protein ROOT STEM CELL DEFECTIVE 2 {ECO:0000303|PubMed:26956135};
GN Name=PAT1H1 {ECO:0000303|PubMed:26956135};
GN Synonyms=RSD2 {ECO:0000303|PubMed:26956135};
GN OrderedLocusNames=At3g22270 {ECO:0000312|Araport:AT3G22270};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
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, INTERACTION WITH AFPH2/NINJA, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26956135; DOI=10.1007/s00299-016-1961-7;
RA Yu Q., Liu J., Zheng H., Jia Y., Tian H., Ding Z.;
RT "Topoisomerase II-associated protein PAT1H1 is involved in the root stem
RT cell niche maintenance in Arabidopsis thaliana.";
RL Plant Cell Rep. 35:1297-1307(2016).
CC -!- FUNCTION: Activator of mRNA decapping. Involved in mRNA decay via
CC decapping (By similarity). Involved in the regulation of root stem cell
CC niche identity. Maintains root stem cell niche stability through the
CC interaction with the negative regulator of jasmonate signaling
CC AFPH2/NINJA, and the regulation of cell division (PubMed:26956135).
CC {ECO:0000250|UniProtKB:Q0WPK4, ECO:0000269|PubMed:26956135}.
CC -!- SUBUNIT: Interacts with AFPH2/NINJA. {ECO:0000269|PubMed:26956135}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, shoot apical
CC meristem (SAM) and leaves. {ECO:0000269|PubMed:26956135}.
CC -!- DISRUPTION PHENOTYPE: Enhanced root distal stem cell differentiation
CC and increased mitotic activity in root quiescent center.
CC {ECO:0000269|PubMed:26956135}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01945.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002046; BAB01945.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76616.1; -; Genomic_DNA.
DR EMBL; AK228960; BAF00849.1; -; mRNA.
DR RefSeq; NP_188866.1; NM_113125.4.
DR AlphaFoldDB; F4J077; -.
DR ComplexPortal; CPX-1391; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1392; LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1393; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1394; LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1395; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1396; LSM1-7-PAT1 complex, variant LSM1B-LSM3A-LSM6B-PAT1H1.
DR ComplexPortal; CPX-1397; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6A-PAT1H1.
DR ComplexPortal; CPX-1398; LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1H1.
DR STRING; 3702.AT3G22270.1; -.
DR iPTMnet; F4J077; -.
DR PaxDb; F4J077; -.
DR PRIDE; F4J077; -.
DR ProteomicsDB; 236706; -.
DR EnsemblPlants; AT3G22270.1; AT3G22270.1; AT3G22270.
DR GeneID; 821797; -.
DR Gramene; AT3G22270.1; AT3G22270.1; AT3G22270.
DR KEGG; ath:AT3G22270; -.
DR Araport; AT3G22270; -.
DR TAIR; locus:2091618; AT3G22270.
DR eggNOG; ENOG502QQ60; Eukaryota.
DR HOGENOM; CLU_021130_0_0_1; -.
DR InParanoid; F4J077; -.
DR OMA; ESNVPQF; -.
DR OrthoDB; 369950at2759; -.
DR PRO; PR:F4J077; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J077; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:1990726; C:Lsm1-7-Pat1 complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033962; P:P-body assembly; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:TAIR.
DR InterPro; IPR039900; Pat1-like.
DR PANTHER; PTHR21551; PTHR21551; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; mRNA processing; Reference proteome.
FT CHAIN 1..782
FT /note="Protein PAT1 homolog 1"
FT /id="PRO_0000442789"
FT REGION 96..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 623
FT /note="T -> K (in Ref. 3; BAF00849)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 782 AA; 85646 MW; 89309922BDBCABEF CRC64;
MERSDSRDLY NFVRASSLDK NSTLFDASQY EFFGQNLDDM ELGGLDDDGV IAPVLGHADD
DEYHLFDKGE GAGLGSLSDM DDLATTFAKL NRVVTGPKHP GVIGDRGSGS FSRESSSATD
WTQDAELTSW LDEQDQEAKR WSSQPQSFAH SKPLYRTSSY PQQQPQLQHY NSEPIILPES
NFTSFPPPGN RSPQASPGNL HRAPSLPGGS QLTYSAPSPL SNSGFHLSGL SQGPHYGGNL
TRYASCGPTL GNMVQPHWVT DPGHLHGDHS GLLHNLVQQQ HQQLPPRNAI MSQHLLALQQ
RQSYAQLAAL QSQLYSSYPS PSRKVPFGVG EVREHKHKSS HRSRKNRGLS QQTSDAASQK
SETGLQFRSK HMTSEEIESI LKMQHSNSHS NDPYVNDYYH QAKLAKKSAG SKAISHFYPA
QLKDHQPRSR NSSEQHPQVH VDALGKITLP SVRRPHALLE VDSSPGFNDG SGDHKGSGKH
LEQEPLVAAR VTIEDALGVL IDIVDIDRTL QNTRPQDGGA QLKRKRQILL EGLATALQLA
DPFSKTGQKS GMTAKDDIVF LRIATLPKGR KLLTKYLQLL VPGTENARVV CMAIFRHLRF
LFGGLPSDTL AAETISNLAK AVTVCVQAMD LRALSACLAA VVCSSEQPPL RPIGSSAGDG
ASVVLISLLE RAAEVVVVPR VMHGNSNDGL WRASFDEFFN LLTKYCRSKY DTIRGQNQGS
AADVLELAIK REMPAELLRA SLRHTNDDQR NYLLNFGRKP SAISESASHA RGGQINSESV
RG
