FKBP9_MOUSE
ID FKBP9_MOUSE Reviewed; 570 AA.
AC Q9Z247; Q80ZZ6; Q8R386; Q9CVM0; Q9JHX5;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP9;
DE Short=PPIase FKBP9;
DE EC=5.2.1.8;
DE AltName: Full=63 kDa FK506-binding protein;
DE Short=63 kDa FKBP;
DE Short=FKBP-63;
DE AltName: Full=FK506-binding protein 9;
DE Short=FKBP-9;
DE AltName: Full=FKBP65RS;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=Fkbp9; Synonyms=Fkbp60, Fkbp63;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND CALCIUM-BINDING.
RX PubMed=10524204; DOI=10.1016/s0167-4781(99)00080-9;
RA Shadidy M., Caubit X., Olsen R., Seternes O.M., Moens U., Krauss S.;
RT "Biochemical analysis of mouse FKBP60, a novel member of the FKBP family.";
RL Biochim. Biophys. Acta 1446:295-307(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=11710534;
RA Jo D., Lyu M.S., Cho E.-G., Park D., Kozak C.A., Kim M.G.;
RT "Identification and genetic mapping of the mouse Fkbp9 gene encoding a new
RT member of FK506-binding protein family.";
RL Mol. Cells 12:272-275(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Fetal brain, and Mammary tumor;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-570.
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:10524204}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:10524204}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal muscle,
CC lung, liver and kidney. Lower levels found in brain, spleen and testis.
CC {ECO:0000269|PubMed:10524204, ECO:0000269|PubMed:11710534}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages.
CC {ECO:0000269|PubMed:10524204}.
CC -!- PTM: Phosphorylated.
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DR EMBL; AF090334; AAC72964.1; -; mRNA.
DR EMBL; AF279263; AAF79215.1; -; mRNA.
DR EMBL; BC026133; AAH26133.1; -; mRNA.
DR EMBL; BC043129; AAH43129.1; -; mRNA.
DR EMBL; AK007499; BAB25071.1; -; mRNA.
DR CCDS; CCDS39494.1; -.
DR RefSeq; NP_036186.2; NM_012056.2.
DR AlphaFoldDB; Q9Z247; -.
DR SMR; Q9Z247; -.
DR BioGRID; 205110; 20.
DR IntAct; Q9Z247; 2.
DR MINT; Q9Z247; -.
DR STRING; 10090.ENSMUSP00000031795; -.
DR GlyConnect; 2579; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9Z247; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q9Z247; -.
DR PhosphoSitePlus; Q9Z247; -.
DR MaxQB; Q9Z247; -.
DR PaxDb; Q9Z247; -.
DR PeptideAtlas; Q9Z247; -.
DR PRIDE; Q9Z247; -.
DR ProteomicsDB; 266852; -.
DR Antibodypedia; 2851; 81 antibodies from 23 providers.
DR DNASU; 27055; -.
DR Ensembl; ENSMUST00000031795; ENSMUSP00000031795; ENSMUSG00000029781.
DR GeneID; 27055; -.
DR KEGG; mmu:27055; -.
DR UCSC; uc009cbp.2; mouse.
DR CTD; 11328; -.
DR MGI; MGI:1350921; Fkbp9.
DR VEuPathDB; HostDB:ENSMUSG00000029781; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157125; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; Q9Z247; -.
DR OMA; HTYDTYV; -.
DR OrthoDB; 1507309at2759; -.
DR PhylomeDB; Q9Z247; -.
DR TreeFam; TF105296; -.
DR BioGRID-ORCS; 27055; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Fkbp9; mouse.
DR PRO; PR:Q9Z247; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z247; protein.
DR Bgee; ENSMUSG00000029781; Expressed in epithelium of cochlear duct and 292 other tissues.
DR Genevisible; Q9Z247; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Isomerase; Metal-binding;
KW Phosphoprotein; 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_0000025516"
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:0000269|PubMed:19349973"
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"
FT CONFLICT 40
FT /note="Q -> R (in Ref. 3; AAH26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="H -> Q (in Ref. 3; AAH26133)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..236
FT /note="DGK -> NGE (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="G -> S (in Ref. 4; BAB25071)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="G -> A (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="A -> T (in Ref. 4; BAB25071)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> F (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="F -> V (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="K -> N (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="S -> I (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="E -> D (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="N -> S (in Ref. 3; AAH43129)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="D -> N (in Ref. 2; AAF79215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 62995 MW; DFE8B8F2F6A0F1DA CRC64;
MALGARGWRR RSLLLLLLWV TGQAAPVLGL AVSSELQIQQ SFVPDECPRT VHSGDFVRYH
YVGTFLDGQK FDSSYDRDST FNVFVGKGQL IAGMDQALVG MCVNERRLVT IPPNLAYGSE
GVSGVIPPNS VLHFDVLLVD IWNSEDQVHI QTYFKPPSCP RTIQVSDFVR YHYNGTFLDG
TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITVPPFLAYG EEGDGKDIPG
QASLVFDVAL LDLHNPKDTI SIENKVVPEN CERRSQSGDF LRYHYNGTLL DGTLFDSSYS
RNHTFDTYIG QGYVIPGMDE GLLGVCIGER RRIVVPPHLG YGEKGRGSIP GSAVLVFDIH
VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL
GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVSGL
PEGYMFIWNG EVSPNLFEEI DRDGNGEVLL EEFSEYIHAQ VATGKGKLAP GFNAEMIVKN
MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL
