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   09-FEB-2010, entry version 64.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase 1;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase Pin1;
DE   AltName: Full=PPIase Pin1;
DE   AltName: Full=PIN1At;
GN   Name=PIN1; OrderedLocusNames=At2g18040; ORFNames=T27K22.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=20209439; 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   MEDLINE=20083487; 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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-119.
RC   STRAIN=cv. Columbia; TISSUE=Dry seed;
RX   MEDLINE=96158348; PubMed=8580968;
RX   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.,
RA   Marbach J., Fleck J., Clement B., Philipps G., Herve C., Bardet C.,
RA   Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F.,
RA   Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H.,
RA   Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes:
RT   analysis of a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
RN   [6]
RP   STRUCTURE BY NMR OF 1-18 AND 36-119.
RX   MEDLINE=20414193; PubMed=10959635; DOI=10.1023/A:1008375707703;
RA   Landrieu I., Wieruszeski J.-M., Odaert B., Inze D., Grzesiek S.,
RA   Lippen G.;
RT   "Sequence-specific 1H, 13C and 15N chemical shift backbone NMR
RT   assignment and secondary structure of the Arabidopsis thaliana PIN1At
RT   protein.";
RL   J. Biomol. NMR 17:271-272(2000).
RN   [7]
RP   STRUCTURE BY NMR.
RX   MEDLINE=22075372; 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
RT   PIN1At from Arabidopsis thaliana.";
RL   J. Mol. Biol. 320:321-332(2002).
CC   -!- FUNCTION: Prolyl cis/trans isomerase with specificity for phospho-
CC       Ser-Pro bonds.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC   -!- MISCELLANEOUS: Like all plant Pin1-type PPIases, do not contain
CC       the N-terminal WW domain found in other eukaryotic parvulins, but
CC       contains a four-amino acid insertion next to the phospho-specific
CC       recognition site of the active site. These extra amino acids may
CC       be important for mediating the substrate interaction of plant
CC       enzymes.
CC   -!- SIMILARITY: Belongs to the ppiC/parvulin rotamase family.
CC   -!- SIMILARITY: Contains 1 PpiC domain.
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DR   EMBL; AC006201; AAD20122.1; -; 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   IPI; IPI00529445; -.
DR   PIR; E84559; E84559.
DR   RefSeq; NP_179395.1; -.
DR   UniGene; At.20592; -.
DR   PDB; 1J6Y; NMR; -; A=1-119.
DR   PDBsum; 1J6Y; -.
DR   STRING; Q9SL42; -.
DR   PRIDE; Q9SL42; -.
DR   GeneID; 816316; -.
DR   GenomeReviews; CT485783_GR; AT2G18040.
DR   KEGG; ath:AT2G18040; -.
DR   NMPDR; fig|3702.1.peg.8800; -.
DR   TAIR; At2g18040; -.
DR   HOGENOM; HBG526275; -.
DR   InParanoid; Q9SL42; -.
DR   OMA; EMQPSFE; -.
DR   PhylomeDB; Q9SL42; -.
DR   BRENDA; 5.2.1.8; 302.
DR   ArrayExpress; Q9SL42; -.
DR   Genevestigator; Q9SL42; -.
DR   GermOnline; AT2G18040; Arabidopsis thaliana.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IGI:TAIR.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:TAIR.
DR   InterPro; IPR000297; PPIase_PpiC.
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; Complete proteome; Isomerase; Rotamase.
FT   CHAIN         1    119       Peptidyl-prolyl cis-trans isomerase 1.
FT                                /FTId=PRO_0000193440.
FT   DOMAIN        4    119       PpiC.
FT   STRAND        8     10
FT   STRAND       20     24
FT   HELIX        38     53
FT   HELIX        60     65
FT   HELIX        69     73
FT   STRAND       76     80
FT   STRAND       82     86
FT   HELIX        89     96
FT   STRAND       99    101
FT   STRAND      106    108
FT   STRAND      111    113
SQ   SEQUENCE   119 AA;  13015 MW;  E926CB566E76A0A3 CRC64;
     MASRDQVKAS HILIKHQGSR RKASWKDPEG KIILTTTREA AVEQLKSIRE DIVSGKANFE
     EVATRVSDCS SAKRGGDLGS FGRGQMQKPF EEATYALKVG DISDIVDTDS GVHIIKRTA
//