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   27-MAR-2024, entry version 196.
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; 98.
DR   IntAct; O95302; 19.
DR   MINT; O95302; -.
DR   STRING; 9606.ENSP00000439250; -.
DR   GlyConnect; 1598; 8 N-Linked glycans (3 sites).
DR   GlyCosmos; O95302; 4 sites, 9 glycans.
DR   GlyGen; O95302; 5 sites, 12 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
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; 9606-ENSP00000439250; -.
DR   PeptideAtlas; O95302; -.
DR   ProteomicsDB; 50800; -. [O95302-1]
DR   ProteomicsDB; 6329; -.
DR   ProteomicsDB; 6778; -.
DR   Pumba; O95302; -.
DR   Antibodypedia; 2851; 89 antibodies from 24 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   AGR; HGNC:3725; -.
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; YYKPENC; -.
DR   OrthoDB; 25281at2759; -.
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 1149 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 106 other cell types or tissues.
DR   ExpressionAtlas; O95302; baseline and differential.
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   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; PF00254; FKBP_C; 4.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF54534; FKBP-like; 4.
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.
DR   Genevisible; O95302; HS.
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
//