PIN1_ARATH
ID PIN1_ARATH Reviewed; 119 AA.
AC Q9SL42; Q42334;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase Pin1;
DE Short=PPIase Pin1;
DE EC=5.2.1.8;
DE AltName: Full=PIN1At;
DE AltName: Full=Rotamase Pin1;
GN Name=PIN1; OrderedLocusNames=At2g18040; ORFNames=T27K22.9;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10744752; DOI=10.1074/jbc.275.14.10577;
RA Landrieu I., de Veylder L., Fruchart J.-S., Odaert B., Casteels P.,
RA Portetelle D., Van Montagu M., Inze D., Lippens G.;
RT "The Arabidopsis thaliana PIN1At gene encodes a single-domain
RT phosphorylation-dependent peptidyl prolyl cis/trans isomerase.";
RL J. Biol. Chem. 275:10577-10581(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-119.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [8]
RP STRUCTURE BY NMR OF 1-18 AND 36-119.
RX PubMed=10959635; DOI=10.1023/a:1008375707703;
RA Landrieu I., Wieruszeski J.-M., Odaert B., Inze D., Grzesiek S., Lippen G.;
RT "Sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment
RT and secondary structure of the Arabidopsis thaliana PIN1At protein.";
RL J. Biomol. NMR 17:271-272(2000).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=12079389; DOI=10.1016/s0022-2836(02)00429-1;
RA Landrieu I., Wieruszeski J.-M., Wintjens R., Inze D., Lippens G.;
RT "Solution structure of the single-domain prolyl cis/trans isomerase PIN1At
RT from Arabidopsis thaliana.";
RL J. Mol. Biol. 320:321-332(2002).
CC -!- FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-Ser-
CC Pro bonds. {ECO:0000269|PubMed:10744752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- INTERACTION:
CC Q9SL42; O82794: AGL24; NbExp=4; IntAct=EBI-2618990, EBI-592083;
CC Q9SL42; O64645: SOC1; NbExp=3; IntAct=EBI-2618990, EBI-592041;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:10744752}.
CC -!- MISCELLANEOUS: Like all plant Pin1-type PPIases, do not contain the N-
CC terminal WW domain found in other eukaryotic parvulins, but contains a
CC four-amino acid insertion next to the phospho-specific recognition site
CC of the active site. These extra amino acids may be important for
CC mediating the substrate interaction of plant enzymes.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000305}.
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DR EMBL; AC006201; AAD20122.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06719.1; -; Genomic_DNA.
DR EMBL; AF360318; AAK26028.1; -; mRNA.
DR EMBL; AY057514; AAL09755.1; -; mRNA.
DR EMBL; AY056314; AAL07163.1; -; mRNA.
DR EMBL; AY085059; AAM61615.1; -; mRNA.
DR EMBL; F13919; CAA23077.1; -; mRNA.
DR PIR; E84559; E84559.
DR RefSeq; NP_179395.1; NM_127360.4.
DR PDB; 1J6Y; NMR; -; A=1-119.
DR PDBsum; 1J6Y; -.
DR AlphaFoldDB; Q9SL42; -.
DR BMRB; Q9SL42; -.
DR SMR; Q9SL42; -.
DR IntAct; Q9SL42; 2.
DR STRING; 3702.AT2G18040.1; -.
DR iPTMnet; Q9SL42; -.
DR PaxDb; Q9SL42; -.
DR PRIDE; Q9SL42; -.
DR ProteomicsDB; 235022; -.
DR EnsemblPlants; AT2G18040.1; AT2G18040.1; AT2G18040.
DR GeneID; 816316; -.
DR Gramene; AT2G18040.1; AT2G18040.1; AT2G18040.
DR KEGG; ath:AT2G18040; -.
DR Araport; AT2G18040; -.
DR TAIR; locus:2060922; AT2G18040.
DR eggNOG; KOG3259; Eukaryota.
DR HOGENOM; CLU_090028_4_0_1; -.
DR OMA; DEVQCLH; -.
DR OrthoDB; 1437969at2759; -.
DR PhylomeDB; Q9SL42; -.
DR EvolutionaryTrace; Q9SL42; -.
DR PRO; PR:Q9SL42; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL42; baseline and differential.
DR Genevisible; Q9SL42; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0032880; P:regulation of protein localization; IMP:TAIR.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR Pfam; PF00639; Rotamase; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Phosphoprotein; Reference proteome; Rotamase.
FT CHAIN 1..119
FT /note="Peptidyl-prolyl cis-trans isomerase Pin1"
FT /id="PRO_0000193440"
FT DOMAIN 4..119
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1J6Y"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:1J6Y"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1J6Y"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1J6Y"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1J6Y"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1J6Y"
SQ SEQUENCE 119 AA; 13015 MW; E926CB566E76A0A3 CRC64;
MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE DIVSGKANFE
EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG DISDIVDTDS GVHIIKRTA
