FKBP3_HUMAN
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-AUG-2022, entry version 200.
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; 121.
DR IntAct; Q00688; 19.
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; Q00688; -.
DR PeptideAtlas; Q00688; -.
DR PRIDE; Q00688; -.
DR ProteomicsDB; 57869; -.
DR TopDownProteomics; Q00688; -.
DR Antibodypedia; 56; 239 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 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; FKGTEPV; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; Q00688; -.
DR TreeFam; TF105293; -.
DR BRENDA; 5.2.1.8; 2681.
DR PathwayCommons; Q00688; -.
DR SignaLink; Q00688; -.
DR BioGRID-ORCS; 2287; 81 hits in 1072 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 206 other tissues.
DR ExpressionAtlas; Q00688; baseline and differential.
DR Genevisible; Q00688; HS.
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 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; PTHR46493; 1.
DR Pfam; PF18410; BTHB; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
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
