FK152_ARATH
ID FK152_ARATH Reviewed; 163 AA.
AC Q38936; Q9FJL2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP15-2;
DE Short=PPIase FKBP15-2;
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 15-2;
DE Short=AtFKBP15-2;
DE AltName: Full=FK506-binding protein 2-2;
DE AltName: Full=Immunophilin FKBP15-2;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP15-2; OrderedLocusNames=At5g48580; ORFNames=K15N18.5;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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:0000305}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; U52047; AAC49391.1; -; mRNA.
DR EMBL; AB015468; BAB10691.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95691.1; -; Genomic_DNA.
DR EMBL; AF370159; AAK43974.1; -; mRNA.
DR EMBL; AY059146; AAL15252.1; -; mRNA.
DR EMBL; AY085294; AAM62526.1; -; mRNA.
DR PIR; S71238; S71238.
DR RefSeq; NP_199669.1; NM_124234.4.
DR AlphaFoldDB; Q38936; -.
DR SMR; Q38936; -.
DR STRING; 3702.AT5G48580.1; -.
DR PaxDb; Q38936; -.
DR PRIDE; Q38936; -.
DR ProteomicsDB; 230599; -.
DR EnsemblPlants; AT5G48580.1; AT5G48580.1; AT5G48580.
DR GeneID; 834915; -.
DR Gramene; AT5G48580.1; AT5G48580.1; AT5G48580.
DR KEGG; ath:AT5G48580; -.
DR Araport; AT5G48580; -.
DR TAIR; locus:2152506; AT5G48580.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_8_2_1; -.
DR InParanoid; Q38936; -.
DR OMA; THAVECE; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q38936; -.
DR PRO; PR:Q38936; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38936; baseline and differential.
DR Genevisible; Q38936; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IMP:TAIR.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:TAIR.
DR GO; GO:0009620; P:response to fungus; IPI:TAIR.
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; 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..163
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP15-2"
FT /id="PRO_0000025509"
FT DOMAIN 52..140
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 160..163
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT COMPBIAS 148..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3..4
FT /note="SK -> DE (in Ref. 1; AAC49391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 17658 MW; 71A7C5825759639D CRC64;
MASKMSLRYS LFLIFFSLIS LQGFAKKTGD VSELQIGVKF KPKTCEVQAH KGDTIKVHYR
GKLTDGTVFD SSFERGDPFE FKLGSGQVIK GWDQGLLGAC VGEKRKLKIP AKLGYGEQGS
PPTIPGGATL IFDTELIAVN EKPAGGEEYG GDEDDEGYGN DEL
