FK151_ARATH
ID FK151_ARATH Reviewed; 153 AA.
AC Q38935; Q8LA41; Q9LSF4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP15-1;
DE Short=PPIase FKBP15-1;
DE EC=5.2.1.8;
DE AltName: Full=15 kDa FK506-binding protein;
DE Short=15 kDa FKBP;
DE AltName: Full=FK506-binding protein 15-1;
DE Short=AtFKBP15-1;
DE AltName: Full=FK506-binding protein 2-1;
DE AltName: Full=Immunophilin FKBP15-1;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP15-1; OrderedLocusNames=At3g25220; ORFNames=MJL12.17;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8692927; DOI=10.1073/pnas.93.14.6964;
RA Luan S., Kudla J., Gruissem W., Schreiber S.L.;
RT "Molecular characterization of a FKBP-type immunophilin from higher
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6964-6969(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 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: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC49390.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM65589.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U52046; AAC49390.1; ALT_INIT; mRNA.
DR EMBL; AB026647; BAB02081.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76994.1; -; Genomic_DNA.
DR EMBL; AY062776; AAL32854.1; -; mRNA.
DR EMBL; AY128760; AAM91160.1; -; mRNA.
DR EMBL; AY088043; AAM65589.1; ALT_INIT; mRNA.
DR PIR; S71237; S71237.
DR RefSeq; NP_566762.1; NM_113428.3.
DR AlphaFoldDB; Q38935; -.
DR SMR; Q38935; -.
DR BioGRID; 7446; 7.
DR IntAct; Q38935; 7.
DR STRING; 3702.AT3G25220.1; -.
DR PaxDb; Q38935; -.
DR PRIDE; Q38935; -.
DR ProteomicsDB; 230521; -.
DR DNASU; 822115; -.
DR EnsemblPlants; AT3G25220.1; AT3G25220.1; AT3G25220.
DR GeneID; 822115; -.
DR Gramene; AT3G25220.1; AT3G25220.1; AT3G25220.
DR KEGG; ath:AT3G25220; -.
DR Araport; AT3G25220; -.
DR TAIR; locus:2090235; AT3G25220.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; Q38935; -.
DR OMA; KCDLQAH; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q38935; -.
DR PRO; PR:Q38935; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38935; baseline and differential.
DR Genevisible; Q38935; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PTHR45779; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..153
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP15-1"
FT /id="PRO_0000025508"
FT DOMAIN 52..140
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT MOTIF 150..153
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CONFLICT 72
FT /note="S -> I (in Ref. 5; AAM65589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16355 MW; 09549E647B738CD9 CRC64;
MMSSASAMKA VGFLLLLTIL TLAYAKKSGD VTELQIGVKY KPQKCDLQAH KGDKIKVHYR
GKLTDGTVFD SSFERGDPIE FELGTGQVIP GWDQGLLGAC VGEKRKLKIP SKLGYGDNGS
PPKIPGGATL IFDTELVAVN GEPSSEAKSK NEL
