FKBP3_DICDI
ID FKBP3_DICDI Reviewed; 194 AA.
AC Q54N80;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=FK506-binding protein 3;
DE EC=5.2.1.8;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=fkbp3; Synonyms=impA; ORFNames=DDB_G0285455;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=16087752; DOI=10.1128/ec.4.8.1477-1482.2005;
RA Hirose S., Mayanagi T., Pears C., Amagai A., Loomis W.F., Maeda Y.;
RT "Transcriptional switch of the dia1 and impA promoter during the
RT growth/differentiation transition.";
RL Eukaryot. Cell 4:1477-1482(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins by catalyzing the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {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 -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in growing cells. Expression
CC levels decrease during the first few hours of development.
CC {ECO:0000269|PubMed:16087752}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64565.1; -; Genomic_DNA.
DR RefSeq; XP_638063.1; XM_632971.1.
DR AlphaFoldDB; Q54N80; -.
DR SMR; Q54N80; -.
DR STRING; 44689.DDB0232264; -.
DR PaxDb; Q54N80; -.
DR EnsemblProtists; EAL64565; EAL64565; DDB_G0285455.
DR GeneID; 8625109; -.
DR KEGG; ddi:DDB_G0285455; -.
DR dictyBase; DDB_G0285455; impA.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_1404823_0_0_1; -.
DR InParanoid; Q54N80; -.
DR OMA; GICEGET; -.
DR PhylomeDB; Q54N80; -.
DR PRO; PR:Q54N80; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0019954; P:asexual reproduction; IEP:dictyBase.
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; PS50059; FKBP_PPIASE; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Membrane; Reference proteome; Rotamase; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..194
FT /note="FK506-binding protein 3"
FT /id="PRO_0000331282"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 44..133
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 194 AA; 21190 MW; 43D7AB2A62010A9E CRC64;
MNKFLIALLV LATLAVSFSQ EIGVSILKTD TPKGECKGKT ASIGDYISLK YVGKFEDGTV
FDSSEIHGGF SFNFTIGERK VIPGLEIGTI NICEGEKRSI KIPYQLAYGE NGIENAIPPR
TDIYFDLEVV SIEGAPAQPF YYQLIPSVGT IIAFSMLAGF IVLVKFIIKR YPDESNSKKP
APGKPKKTKA AKQN
