ID A9PH03_POPTR Unreviewed; 153 AA.
AC A9PH03;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:ABK95656.1};
RN [1] {ECO:0000313|EMBL:ABK95656.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young and mature leaves {ECO:0000313|EMBL:ABK95656.1};
RX PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT clones and their utility for the discovery of genes responding to insect
RT feeding.";
RL BMC Genomics 9:57-57(2008).
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 Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC ProRule:PRU00277};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF147647; ABK95656.1; -; mRNA.
DR RefSeq; XP_002301808.1; XM_002301772.2.
DR AlphaFoldDB; A9PH03; -.
DR GeneID; 7459501; -.
DR KEGG; pop:7459501; -.
DR eggNOG; KOG0549; Eukaryota.
DR HOGENOM; CLU_013615_8_2_1; -.
DR OrthoDB; 25281at2759; -.
DR ExpressionAtlas; A9PH03; baseline and differential.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; 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; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR45779:SF6; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 2: Evidence at transcript level;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..153
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030165083"
FT DOMAIN 51..139
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 153 AA; 16046 MW; C4AE2209BBC73898 CRC64;
MGFNCASKAT AIFLLLSVSA LVSAKKSGDV KELQIGVKYK PETCEVQAHK GDSIKVHYRG
KLTDGTVFDS SFERGDPIGF ELGSGQVIKG WDQGLLGACV GEKRKLKIPA KLGYGEQGSP
PTIPGGATLI FDTELVEVNG KTSSGGGARD SEL
//
