FKB43_ARATH
ID FKB43_ARATH Reviewed; 499 AA.
AC F4J9Q6; Q1G3M4; Q9C7A0; Q9C7C8; Q9LHH4;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP43;
DE Short=PPIase FKBP43;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 43;
DE Short=AtFKBP43;
DE AltName: Full=Immunophilin FKBP43;
DE AltName: Full=Rotamase;
GN Name=FKBP43; OrderedLocusNames=At3g12340;
GN ORFNames=F28J15.1, MQC3.15, T2E22.33;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] OF 122-499.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51009.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB03141.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002047; BAB03141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069472; AAG51068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069474; AAG51009.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75184.1; -; Genomic_DNA.
DR EMBL; DQ487560; ABF59229.1; -; mRNA.
DR RefSeq; NP_001326743.1; NM_001337988.1.
DR RefSeq; NP_001326744.1; NM_001337989.1.
DR RefSeq; NP_187840.7; NM_112068.9.
DR AlphaFoldDB; F4J9Q6; -.
DR SMR; F4J9Q6; -.
DR STRING; 3702.AT3G12340.1; -.
DR iPTMnet; F4J9Q6; -.
DR PaxDb; F4J9Q6; -.
DR PRIDE; F4J9Q6; -.
DR ProteomicsDB; 230031; -.
DR EnsemblPlants; AT3G12340.1; AT3G12340.1; AT3G12340.
DR GeneID; 820412; -.
DR Gramene; AT3G12340.1; AT3G12340.1; AT3G12340.
DR KEGG; ath:AT3G12340; -.
DR Araport; AT3G12340; -.
DR TAIR; locus:2092467; AT3G12340.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_1_1_1; -.
DR InParanoid; F4J9Q6; -.
DR OMA; LGVDDGM; -.
DR OrthoDB; 402681at2759; -.
DR PRO; PR:F4J9Q6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J9Q6; baseline and differential.
DR Genevisible; F4J9Q6; AT.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..499
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP43"
FT /id="PRO_0000416135"
FT DOMAIN 411..499
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 101..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55178 MW; 6EDB7C6524204B54 CRC64;
MAFWGVEVKP GKTFTLKNNE ATGIRRLHLS QATLGHGTAT NRSILQCNVG NKSPLLLCVL
TPDKVDSCQL NLEFEETDEV IFSVIGPRSV HLTGYFLGRS TGFRPNDDES ESFGEDIVDT
DMEKGSSDDY DYSDSFINDD DPAVRGSHVS STDDDEISIK EMTAKTKEKK KNGKGRRLRK
KFQVSDSDSD ETSARADESS NEDSVEVLNN GNEPKIAKVH SSESPLPSRV TRSKARKSTL
ESGEPAKCEK TFEAKINTHK TLDNREDKPL DDAKLSPVQK DCEILSKKKR NKERSKSSAI
IIDSDDGEGK NMPESLQNEN PVSDKGIKSS SDVLLSQNGD ATLSKKKKKR DRREETTDVP
ECPEKKKQAI DKNIEKEAGT KKPLETRTLS NGVIIEDIEK GKLDGKSAVK GKKVSILYTG
KLKDTGNLFD SNLGEDPLRF RLGGENVIEG LSIGVEGMRV GDKRRLIIPP ALGYSKRGLK
EKVPKSAWLV YEVEAVKIR
