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   27-MAR-2024, entry version 209.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP3;
DE            Short=PPIase FKBP3;
DE            EC=5.2.1.8;
DE   AltName: Full=25 kDa FK506-binding protein;
DE            Short=25 kDa FKBP;
DE            Short=FKBP-25;
DE   AltName: Full=FK506-binding protein 3;
DE            Short=FKBP-3;
DE   AltName: Full=Immunophilin FKBP25;
DE   AltName: Full=Rapamycin-selective 25 kDa immunophilin;
DE   AltName: Full=Rotamase;
GN   Name=FKBP3; Synonyms=FKBP25;
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 [MRNA].
RX   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 binding
RT   protein.";
RL   Biochem. Biophys. Res. Commun. 185:298-303(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   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   PubMed=1375932; DOI=10.1016/s0021-9258(19)49856-6;
RA   Jin Y.-J., Burakoff S.J., Bierer B.E.;
RT   "Molecular cloning of a 25-kDa high affinity rapamycin binding protein,
RT   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 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., 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-170, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
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).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [19]
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 a
CC       family of receptors for the two immunosuppressants which inhibit T-cell
CC       proliferation by arresting two distinct cytoplasmic signal transmission
CC       pathways. PPIases accelerate the folding of proteins.
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 preferentially by rapamycin over FK506.
CC   -!- INTERACTION:
CC       Q00688; Q00987: MDM2; NbExp=2; IntAct=EBI-1044081, EBI-389668;
CC       Q00688; Q9UGN5: PARP2; NbExp=2; IntAct=EBI-1044081, EBI-2795348;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58474.1; Type=Frameshift; Evidence={ECO:0000305};
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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   CCDS; CCDS9683.1; -.
DR   PIR; JQ1522; JQ1522.
DR   RefSeq; NP_002004.1; NM_002013.3.
DR   PDB; 1PBK; X-ray; 2.50 A; A=109-224.
DR   PDB; 2KFV; NMR; -; A=1-73.
DR   PDB; 2MPH; NMR; -; A=1-224.
DR   PDB; 5D75; X-ray; 1.83 A; A=109-224.
DR   PDB; 5GPG; X-ray; 1.67 A; A=109-224.
DR   PDBsum; 1PBK; -.
DR   PDBsum; 2KFV; -.
DR   PDBsum; 2MPH; -.
DR   PDBsum; 5D75; -.
DR   PDBsum; 5GPG; -.
DR   AlphaFoldDB; Q00688; -.
DR   BMRB; Q00688; -.
DR   SMR; Q00688; -.
DR   BioGRID; 108577; 139.
DR   IntAct; Q00688; 20.
DR   MINT; Q00688; -.
DR   STRING; 9606.ENSP00000216330; -.
DR   BindingDB; Q00688; -.
DR   ChEMBL; CHEMBL4746; -.
DR   DrugCentral; Q00688; -.
DR   GlyGen; Q00688; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q00688; -.
DR   MetOSite; Q00688; -.
DR   PhosphoSitePlus; Q00688; -.
DR   SwissPalm; Q00688; -.
DR   BioMuta; FKBP3; -.
DR   DMDM; 232096; -.
DR   EPD; Q00688; -.
DR   jPOST; Q00688; -.
DR   MassIVE; Q00688; -.
DR   MaxQB; Q00688; -.
DR   PaxDb; 9606-ENSP00000216330; -.
DR   PeptideAtlas; Q00688; -.
DR   ProteomicsDB; 57869; -.
DR   Pumba; Q00688; -.
DR   TopDownProteomics; Q00688; -.
DR   Antibodypedia; 56; 258 antibodies from 33 providers.
DR   DNASU; 2287; -.
DR   Ensembl; ENST00000216330.7; ENSP00000216330.3; ENSG00000100442.11.
DR   Ensembl; ENST00000396062.4; ENSP00000379374.3; ENSG00000100442.11.
DR   GeneID; 2287; -.
DR   KEGG; hsa:2287; -.
DR   MANE-Select; ENST00000396062.4; ENSP00000379374.3; NM_002013.4; NP_002004.1.
DR   UCSC; uc010tqf.3; human.
DR   AGR; HGNC:3719; -.
DR   CTD; 2287; -.
DR   DisGeNET; 2287; -.
DR   GeneCards; FKBP3; -.
DR   HGNC; HGNC:3719; FKBP3.
DR   HPA; ENSG00000100442; Tissue enhanced (skeletal muscle, tongue).
DR   MIM; 186947; gene.
DR   neXtProt; NX_Q00688; -.
DR   OpenTargets; ENSG00000100442; -.
DR   PharmGKB; PA28160; -.
DR   VEuPathDB; HostDB:ENSG00000100442; -.
DR   eggNOG; KOG0544; Eukaryota.
DR   GeneTree; ENSGT00940000154514; -.
DR   HOGENOM; CLU_013615_12_2_1; -.
DR   InParanoid; Q00688; -.
DR   OMA; PENKIPP; -.
DR   OrthoDB; 25281at2759; -.
DR   PhylomeDB; Q00688; -.
DR   TreeFam; TF105293; -.
DR   BRENDA; 5.2.1.8; 2681.
DR   PathwayCommons; Q00688; -.
DR   SignaLink; Q00688; -.
DR   SIGNOR; Q00688; -.
DR   BioGRID-ORCS; 2287; 81 hits in 1148 CRISPR screens.
DR   ChiTaRS; FKBP3; human.
DR   EvolutionaryTrace; Q00688; -.
DR   GeneWiki; FKBP3; -.
DR   GenomeRNAi; 2287; -.
DR   Pharos; Q00688; Tbio.
DR   PRO; PR:Q00688; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q00688; Protein.
DR   Bgee; ENSG00000100442; Expressed in skeletal muscle tissue of biceps brachii and 208 other cell types or tissues.
DR   ExpressionAtlas; Q00688; baseline and differential.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   CDD; cd21063; BTHB_FKBP25; 1.
DR   Gene3D; 1.10.720.80; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   IDEAL; IID00063; -.
DR   InterPro; IPR043368; FKBP3.
DR   InterPro; IPR041200; FKBP3_BTHB.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR46493; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP3; 1.
DR   PANTHER; PTHR46493:SF1; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP3; 1.
DR   Pfam; PF18410; BTHB; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   Genevisible; Q00688; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Isomerase; Nucleus; Phosphoprotein;
KW   Reference proteome; Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT   CHAIN           2..224
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP3"
FT                   /id="PRO_0000075307"
FT   DOMAIN          128..224
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          89..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62446"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         170
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   CONFLICT        181
FT                   /note="T -> A (in Ref. 3; AAA58474)"
FT                   /evidence="ECO:0000305"
FT   HELIX           12..16
FT                   /evidence="ECO:0007829|PDB:2KFV"
FT   HELIX           23..32
FT                   /evidence="ECO:0007829|PDB:2KFV"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:2KFV"
FT   HELIX           47..51
FT                   /evidence="ECO:0007829|PDB:2KFV"
FT   HELIX           56..69
FT                   /evidence="ECO:0007829|PDB:2KFV"
FT   STRAND          110..117
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   TURN            153..155
FT                   /evidence="ECO:0007829|PDB:2MPH"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:5D75"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   HELIX           173..178
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   STRAND          187..192
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   TURN            197..201
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:5GPG"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:5GPG"
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
//