FKBP9_RAT
ID FKBP9_RAT Reviewed; 570 AA.
AC Q66H94;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP9;
DE Short=PPIase FKBP9;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 9;
DE Short=FKBP-9;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins during protein
CC synthesis.
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 FK506. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC081961; AAH81961.1; -; mRNA.
DR RefSeq; NP_001007647.1; NM_001007646.1.
DR AlphaFoldDB; Q66H94; -.
DR SMR; Q66H94; -.
DR IntAct; Q66H94; 3.
DR STRING; 10116.ENSRNOP00000007821; -.
DR GlyGen; Q66H94; 4 sites.
DR iPTMnet; Q66H94; -.
DR PhosphoSitePlus; Q66H94; -.
DR jPOST; Q66H94; -.
DR PaxDb; Q66H94; -.
DR PRIDE; Q66H94; -.
DR Ensembl; ENSRNOT00000007821; ENSRNOP00000007821; ENSRNOG00000005478.
DR GeneID; 297123; -.
DR KEGG; rno:297123; -.
DR UCSC; RGD:1549757; rat.
DR CTD; 11328; -.
DR RGD; 1549757; Fkbp9.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157125; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; Q66H94; -.
DR OMA; HTYDTYV; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q66H94; -.
DR TreeFam; TF105296; -.
DR PRO; PR:Q66H94; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000005478; Expressed in ovary and 19 other tissues.
DR Genevisible; Q66H94; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.10.50.40; -; 4.
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 Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF00254; FKBP_C; 4.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 4.
PE 2: Evidence at transcript level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; Metal-binding;
KW Reference proteome; Repeat; Rotamase; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..570
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP9"
FT /id="PRO_0000045761"
FT DOMAIN 54..142
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 166..254
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 278..365
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 389..477
FT /note="PPIase FKBP-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 488..523
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 533..568
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 567..570
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 548
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 550
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 570 AA; 63127 MW; C4672322A367B310 CRC64;
MAFGARGWRR WSLLLLLLWV TGQAAPVLGL AVSSELQIQR SFVPDECPRT VRSGDFVRYH
YVGTFLDGQK FDSSYDRDST FSVFVGKGQL IAGMDQALVG MCVNERRFVT IPPNLAYGSE
GVSGVIPPNS VLHFDVLLVD IWNSEDQVQI QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG
TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITIPPFLAYG EEGDGKDIPG
QASLVFDVAL LDLHNPKDTI SVENKVVPES CERRSQSGDF LRYHYNGTLL DGTLFDSSYS
RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEEGRGSIP GSAVLVFDIH
VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL
GFGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVSGL
PEGYMFIWNG EVSPNLFEEI DKDGNGEVLL EEFSEYIHAQ VASGKGKLAP GFNAEMIVKN
MFTNQDRNGD GKVTAEEFKL KDQETKHDEL
