ID A0A2U3XC66_LEPWE Unreviewed; 464 AA.
AC A0A2U3XC66;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=FKBP9 {ECO:0000313|RefSeq:XP_006728938.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006728938.1};
RN [1] {ECO:0000313|RefSeq:XP_006728938.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006728938.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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DR RefSeq; XP_006728938.1; XM_006728875.2.
DR AlphaFoldDB; A0A2U3XC66; -.
DR STRING; 9713.A0A2U3XC66; -.
DR GeneID; 102726248; -.
DR KEGG; lww:102726248; -.
DR CTD; 11328; -.
DR OrthoDB; 25281at2759; -.
DR Proteomes; UP000245341; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.10.50.40; -; 3.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR46046:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP9; 1.
DR PANTHER; PTHR46046; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF00254; FKBP_C; 3.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54534; FKBP-like; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50059; FKBP_PPIASE; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|RefSeq:XP_006728938.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..464
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015768480"
FT DOMAIN 57..145
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 169..259
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 283..371
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 382..417
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 427..462
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 464 AA; 51767 MW; 25C0726134F9213D CRC64;
MAFRARGWRS PPPPPLLLLL LWVTGQAAPV AGLGLDTELQ IERRFVPDEC PRTVRSGDFV
RYHYVGTFSD GQKFDSSYDR DSTFNVFVGK GQLIAGMDQA LVGMCVNERR FVKIPPKLAY
GSEGVSGVIP PDSVLHFDVL LMDIWNSEDQ VQVHTYFTPP SCPRTIQVSD FVRYHYNGTF
LDGTLFDSSY SRNRTFDTYI GQGYVIAGMD EGLLGVCIGE KRRIVVPPHL GYGEEGRGEC
WLLPSNSVLH FDVLLMDIWN SEDQVQVHTY FTPPSCPRTI QVSDFVRYHY NGTFLDGTLF
DSRWNLGKTY NIVLGSGQVV LGMDMGLREM CVGEKRTVVI PPHLGYGEAG VDGEVPGSAV
LVFDIELLEL VAGLPEGYMF IWNGEVSPNL FEEIDKDGNG EVLLEEFSEY IHAQVASGKG
KLAPGFDAEV IVKNMFTNQD RNGDGKVTAE EFKLKDQEAK HDEL
//
