(data stored in SCRATCH zone)

SWISSPROT: FK161_ARATH

ID   FK161_ARATH             Reviewed;         207 AA.
AC   Q944B0; O65579;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 113.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP16-1, chloroplastic;
DE            Short=PPIase FKBP16-1;
DE            EC=5.2.1.8;
DE   AltName: Full=FK506-binding protein 16-1;
DE            Short=AtFKBP16-1;
DE   AltName: Full=Immunophilin FKBP16-1;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=FKBP16-1; OrderedLocusNames=At4g26555; ORFNames=M3E9.20, T15N24;
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15047905; DOI=10.1104/pp.103.031005;
RA   He Z., Li L., Luan S.;
RT   "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT   Arabidopsis.";
RL   Plant Physiol. 134:1248-1267(2004).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL022223; CAA18215.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL078465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161565; CAB79510.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85218.1; -; Genomic_DNA.
DR   EMBL; AK117832; BAC42474.1; -; mRNA.
DR   EMBL; AF439821; AAL27493.1; -; mRNA.
DR   EMBL; AY125564; AAM78074.1; -; mRNA.
DR   PIR; T05049; T05049.
DR   RefSeq; NP_567750.1; NM_118789.3.
DR   SMR; Q944B0; -.
DR   STRING; 3702.AT4G26555.1; -.
DR   PaxDb; Q944B0; -.
DR   PRIDE; Q944B0; -.
DR   EnsemblPlants; AT4G26555.1; AT4G26555.1; AT4G26555.
DR   GeneID; 828762; -.
DR   Gramene; AT4G26555.1; AT4G26555.1; AT4G26555.
DR   KEGG; ath:AT4G26555; -.
DR   Araport; AT4G26555; -.
DR   TAIR; locus:505006521; AT4G26555.
DR   eggNOG; ENOG410JRY4; Eukaryota.
DR   eggNOG; COG5102; LUCA.
DR   HOGENOM; HOG000077684; -.
DR   InParanoid; Q944B0; -.
DR   OrthoDB; 1601308at2759; -.
DR   PhylomeDB; Q944B0; -.
DR   PRO; PR:Q944B0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q944B0; baseline and differential.
DR   Genevisible; Q944B0; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q944B0.
DR   SWISS-2DPAGE; Q944B0.
KW   Chloroplast; Isomerase; Plastid; Reference proteome; Rotamase; Thylakoid;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   TRANSIT         ?..67
FT                   /note="Thylakoid"
FT                   /evidence="ECO:0000305"
FT   CHAIN           68..207
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP16-1,
FT                   chloroplastic"
FT                   /id="PRO_0000416130"
FT   DOMAIN          104..207
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   207 AA;  22693 MW;  9688DC74F638F3C9 CRC64;
     MAMAMEISLP FVGSSMALSA GKSRNSVSRI SRVGFSSVSA VHVPRRMFMQ LSGFGSVLTL
     LDFPSLAAPV PQMKEPEVIR TLKLPSGVRY QEIIEGEGRE AHEGDLVELN YVCRRANGYF
     VHSTVDQFSG ESSPVKLILD ENDVIEGLKE VLVGMKAGGK RRALIPPSVG YINETLKPIP
     EEFGPRRSLL SHANEPLVFE IQLLKVL
//

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