FKBP9_HUMAN
ID FKBP9_HUMAN Reviewed; 570 AA.
AC O95302; B3KY35; B7Z1G9; B7Z6H3; Q2M2A1; Q3MIR7; Q6IN76; Q6P2N1; Q96EX5;
AC Q96IJ9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
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=Rotamase;
DE Flags: Precursor;
GN Name=FKBP9; Synonyms=FKBP60, FKBP63;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Liver, Lung, and PNS;
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 [MRNA] OF 54-570 (ISOFORM 1).
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 [5]
RP GLYCOSYLATION AT ASN-174; ASN-286 AND ASN-397.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95302-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95302-2; Sequence=VSP_054825;
CC Name=3;
CC IsoId=O95302-3; Sequence=VSP_054826;
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; AK128597; BAG54697.1; -; mRNA.
DR EMBL; AK293440; BAH11505.1; -; mRNA.
DR EMBL; AK300328; BAH13259.1; -; mRNA.
DR EMBL; AC083863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007443; AAH07443.2; -; mRNA.
DR EMBL; BC064418; AAH64418.1; -; mRNA.
DR EMBL; BC072422; AAH72422.1; -; mRNA.
DR EMBL; BC101723; AAI01724.1; -; mRNA.
DR EMBL; BC112053; AAI12054.1; -; mRNA.
DR EMBL; AF089745; AAC78853.1; -; mRNA.
DR CCDS; CCDS5439.1; -. [O95302-1]
DR CCDS; CCDS64622.1; -. [O95302-3]
DR CCDS; CCDS64623.1; -. [O95302-2]
DR RefSeq; NP_001271270.1; NM_001284341.1. [O95302-3]
DR RefSeq; NP_001271272.1; NM_001284343.1. [O95302-2]
DR RefSeq; NP_009201.2; NM_007270.4. [O95302-1]
DR AlphaFoldDB; O95302; -.
DR SMR; O95302; -.
DR BioGRID; 116456; 90.
DR IntAct; O95302; 19.
DR MINT; O95302; -.
DR STRING; 9606.ENSP00000439250; -.
DR GlyConnect; 1598; 8 N-Linked glycans (3 sites).
DR GlyGen; O95302; 4 sites, 12 N-linked glycans (3 sites).
DR iPTMnet; O95302; -.
DR MetOSite; O95302; -.
DR PhosphoSitePlus; O95302; -.
DR BioMuta; FKBP9; -.
DR EPD; O95302; -.
DR jPOST; O95302; -.
DR MassIVE; O95302; -.
DR MaxQB; O95302; -.
DR PaxDb; O95302; -.
DR PeptideAtlas; O95302; -.
DR PRIDE; O95302; -.
DR ProteomicsDB; 50800; -. [O95302-1]
DR ProteomicsDB; 6329; -.
DR ProteomicsDB; 6778; -.
DR Antibodypedia; 2851; 81 antibodies from 23 providers.
DR DNASU; 11328; -.
DR Ensembl; ENST00000242209.9; ENSP00000242209.4; ENSG00000122642.11. [O95302-1]
DR Ensembl; ENST00000490776.3; ENSP00000441317.1; ENSG00000122642.11. [O95302-2]
DR Ensembl; ENST00000538336.5; ENSP00000439250.1; ENSG00000122642.11. [O95302-3]
DR GeneID; 11328; -.
DR KEGG; hsa:11328; -.
DR MANE-Select; ENST00000242209.9; ENSP00000242209.4; NM_007270.5; NP_009201.2.
DR UCSC; uc003tdh.5; human. [O95302-1]
DR CTD; 11328; -.
DR DisGeNET; 11328; -.
DR GeneCards; FKBP9; -.
DR HGNC; HGNC:3725; FKBP9.
DR HPA; ENSG00000122642; Low tissue specificity.
DR MIM; 616257; gene.
DR neXtProt; NX_O95302; -.
DR OpenTargets; ENSG00000122642; -.
DR PharmGKB; PA28166; -.
DR VEuPathDB; HostDB:ENSG00000122642; -.
DR eggNOG; KOG0549; Eukaryota.
DR GeneTree; ENSGT00940000157125; -.
DR HOGENOM; CLU_034907_0_0_1; -.
DR InParanoid; O95302; -.
DR OMA; HTYDTYV; -.
DR PhylomeDB; O95302; -.
DR TreeFam; TF105296; -.
DR PathwayCommons; O95302; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR SignaLink; O95302; -.
DR BioGRID-ORCS; 11328; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; FKBP9; human.
DR GeneWiki; FKBP9; -.
DR GenomeRNAi; 11328; -.
DR Pharos; O95302; Tbio.
DR PRO; PR:O95302; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O95302; protein.
DR Bgee; ENSG00000122642; Expressed in stromal cell of endometrium and 105 other tissues.
DR ExpressionAtlas; O95302; baseline and differential.
DR Genevisible; O95302; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; ISS: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; 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 Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Isomerase; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW 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_0000045760"
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:12754519"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
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:0000269|PubMed:12754519"
FT VAR_SEQ 1..234
FT /note="MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVR
FT SGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKI
FT PPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVR
FT YHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAY
FT GEDGD -> MA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054825"
FT VAR_SEQ 73
FT /note="S -> SRYWDTAEDKADKSPCPQVRVGVNTSPSCRLKQKGVGIYWKDLQFLV
FT RVQNHGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054826"
SQ SEQUENCE 570 AA; 63084 MW; E1F44A2FA6E112F8 CRC64;
MAFRGWRPPP PPLLLLLLWV TGQAAPVAGL GSDAELQIER RFVPDECPRT VRSGDFVRYH
YVGTFPDGQK FDSSYDRDST FNVFVGKGQL ITGMDQALVG MCVNERRFVK IPPKLAYGNE
GVSGVIPPNS VLHFDVLLMD IWNSEDQVQI HTYFKPPSCP RTIQVSDFVR YHYNGTFLDG
TLFDSSHNRM KTYDTYVGIG WLIPGMDKGL LGMCVGEKRI ITIPPFLAYG EDGDGKDIPG
QASLVFDVAL LDLHNPKDSI SIENKVVPEN CERISQSGDF LRYHYNGTLL DGTLFDSSYS
RNRTFDTYIG QGYVIPGMDE GLLGVCIGEK RRIVVPPHLG YGEEGRGNIP GSAVLVFDIH
VIDFHNPSDS ISITSHYKPP DCSVLSKKGD YLKYHYNASL LDGTLLDSTW NLGKTYNIVL
GSGQVVLGMD MGLREMCVGE KRTVIIPPHL GYGEAGVDGE VPGSAVLVFD IELLELVAGL
PEGYMFIWNG EVSPNLFEEI DKDGNGEVLL EEFSEYIHAQ VASGKGKLAP GFDAELIVKN
MFTNQDRNGD GKVTAEEFKL KDQEAKHDEL
