ID   FKBP3_HUMAN             Reviewed;         224 AA.
AC   Q00688; B2R4Q9; Q14317;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-NOV-2009, entry version 97.
DE   RecName: Full=FK506-binding protein 3;
DE            EC=5.2.1.8;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            Short=Rotamase;
DE   AltName: Full=25 kDa FKBP;
DE   AltName: Full=FKBP-25;
DE   AltName: Full=Rapamycin-selective 25 kDa immunophilin;
GN   Name=FKBP3; Synonyms=FKBP25;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92287110; PubMed=1376117; DOI=10.1016/S0006-291X(05)80990-8;
RA   Wiederrecht G., Martin M., Sigal N., Siekierka J.J.;
RT   "Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin
RT   binding protein.";
RL   Biochem. Biophys. Res. Commun. 185:298-303(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92246959; PubMed=1374240; DOI=10.1016/0006-291X(92)90651-Z;
RA   Hung D.T., Schreiber S.L.;
RT   "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein.";
RL   Biochem. Biophys. Res. Commun. 184:733-738(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RX   MEDLINE=92283784; PubMed=1375932;
RA   Jin Y.-J., Burakoff S.J., Bierer B.E.;
RT   "Molecular cloning of a 25-kDa high affinity rapamycin binding
RT   protein, FKBP25.";
RL   J. Biol. Chem. 267:10942-10945(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle, and Skin;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-160 AND LYS-170, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 109-224.
RA   Liang J., Hung D.T., Schreiber S.L., Clardy J.;
RT   "Structure of the human 25 kDa FK506 binding protein complexed with
RT   rapamycin.";
RL   J. Am. Chem. Soc. 118:1231-1232(1996).
CC   -!- FUNCTION: FK506- and rapamycin-binding proteins (FKBPs) constitute
CC       a family of receptors for the two immunosuppressants which inhibit
CC       T-cell proliferation by arresting two distinct cytoplasmic signal
CC       transmission pathways. PPIases accelerate the folding of proteins.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited preferentially by rapamycin over
CC       FK506.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58474.1; Type=Frameshift; Positions=197;
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DR   EMBL; M96256; AAA58471.1; -; mRNA.
DR   EMBL; M90309; AAA58475.1; -; mRNA.
DR   EMBL; M90820; AAA58474.1; ALT_FRAME; mRNA.
DR   EMBL; BT006904; AAP35550.1; -; mRNA.
DR   EMBL; AK311915; BAG34856.1; -; mRNA.
DR   EMBL; CH471078; EAW65785.1; -; Genomic_DNA.
DR   EMBL; BC016288; AAH16288.1; -; mRNA.
DR   EMBL; BC020809; AAH20809.1; -; mRNA.
DR   IPI; IPI00024157; -.
DR   PIR; JQ1522; JQ1522.
DR   RefSeq; NP_002004.1; -.
DR   UniGene; Hs.509226; -.
DR   UniGene; Hs.509229; -.
DR   PDB; 1PBK; X-ray; 2.50 A; A=109-224.
DR   PDB; 2KFV; NMR; -; A=1-73.
DR   PDBsum; 1PBK; -.
DR   PDBsum; 2KFV; -.
DR   IntAct; Q00688; 3.
DR   STRING; Q00688; -.
DR   PhosphoSite; Q00688; -.
DR   PeptideAtlas; Q00688; -.
DR   PRIDE; Q00688; -.
DR   Ensembl; ENST00000216330; ENSP00000216330; ENSG00000100442; Homo sapiens.
DR   Ensembl; ENST00000396062; ENSP00000379374; ENSG00000100442; Homo sapiens.
DR   GeneID; 2287; -.
DR   KEGG; hsa:2287; -.
DR   UCSC; uc001wwb.1; human.
DR   CTD; 2287; -.
DR   GeneCards; GC14M044654; -.
DR   H-InvDB; HIX0011622; -.
DR   HGNC; HGNC:3719; FKBP3.
DR   HPA; CAB012232; -.
DR   HPA; CAB012520; -.
DR   HPA; HPA000864; -.
DR   MIM; 186947; gene.
DR   PharmGKB; PA28160; -.
DR   HOGENOM; Q00688; -.
DR   HOVERGEN; Q00688; -.
DR   OMA; SKIPPNA; -.
DR   BRENDA; 5.2.1.8; 247.
DR   Pathway_Interaction_DB; hdac_classi_pathway; Signaling events mediated by HDAC Class I.
DR   NextBio; 9295; -.
DR   ArrayExpress; Q00688; -.
DR   Bgee; Q00688; -.
DR   CleanEx; HS_FKBP3; -.
DR   Genevestigator; Q00688; -.
DR   GermOnline; ENSG00000100442; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005528; F:FK506 binding; TAS:ProtInc.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR001179; PPIase_FKBP.
DR   PANTHER; PTHR10516; PPIase_FKBP; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Isomerase; Nucleus;
KW   Phosphoprotein; Rotamase.
FT   CHAIN         1    224       FK506-binding protein 3.
FT                                /FTId=PRO_0000075307.
FT   DOMAIN      128    224       PPIase FKBP-type.
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     160    160       N6-acetyllysine.
FT   MOD_RES     170    170       N6-acetyllysine.
FT   CONFLICT    181    181       T -> A (in Ref. 3; AAA58474).
FT   STRAND      111    117
FT   STRAND      130    138
FT   STRAND      144    147
FT   TURN        155    157
FT   STRAND      162    165
FT   TURN        166    169
FT   HELIX       173    179
FT   STRAND      187    192
FT   HELIX       194    196
FT   TURN        197    201
FT   HELIX       204    206
SQ   SEQUENCE   224 AA;  25177 MW;  C144C5AAB7EA9522 CRC64;
     MAAAVPQRAW TVEQLRSEQL PKKDIIKFLQ EHGSDSFLAE HKLLGNIKNV AKTANKDHLV
     TAYNHLFETK RFKGTESISK VSEQVKNVKL NEDKPKETKS EETLDEGPPK YTKSVLKKGD
     KTNFPKKGDV VHCWYTGTLQ DGTVFDTNIQ TSAKKKKNAK PLSFKVGVGK VIRGWDEALL
     TMSKGEKARL EIEPEWAYGK KGQPDAKIPP NAKLTFEVEL VDID
//