ID DPP3_HUMAN Reviewed; 737 AA. AC Q9NY33; B2RDB5; B4DLX4; F5H8L6; O95748; Q969H2; Q9BV67; Q9HAL6; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2002, sequence version 2. DT 24-JAN-2024, entry version 201. DE RecName: Full=Dipeptidyl peptidase 3; DE EC=3.4.14.4 {ECO:0000269|PubMed:11209758, ECO:0000269|PubMed:1515063, ECO:0000269|PubMed:3233187, ECO:0000269|PubMed:9425109}; DE AltName: Full=Dipeptidyl aminopeptidase III; DE AltName: Full=Dipeptidyl arylamidase III; DE AltName: Full=Dipeptidyl peptidase III; DE Short=DPP III; DE AltName: Full=Enkephalinase B; GN Name=DPP3; 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] (ISOFORM 1), AND VARIANTS HIS-145 AND HIS-678. RA Chen J.M., Fortunato M., Barrett A.J.; RT "Cloning and sequencing of human dipeptidyl-peptidase III."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Brain, and Embryo; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-76. RC TISSUE=Colon, Kidney, and Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 244-723 (ISOFORM 1), FUNCTION, CATALYTIC RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND VARIANT RP HIS-678. RX PubMed=9425109; DOI=10.1042/bj3290275; RA Fukasawa K., Fukusawa K.M., Kanai M., Fujii S., Hirose J., Harada M.; RT "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning RT and expression."; RL Biochem. J. 329:275-282(1998). RN [6] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=3233187; DOI=10.1016/0885-4505(88)90133-8; RA Shimamori Y., Watanabe Y., Fujimoto Y.; RT "Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins RT and its stimulation by cobaltous ion."; RL Biochem. Med. Metab. Biol. 40:305-310(1988). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RX PubMed=1515063; DOI=10.1515/bchm3.1992.373.2.375; RA Abramic M., Vitale L.; RT "Basic amino acids preferring broad specificity aminopeptidase from human RT erythrocytes."; RL Biol. Chem. Hoppe-Seyler 373:375-380(1992). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RC TISSUE=Erythrocyte; RX PubMed=11209758; DOI=10.1515/bc.2000.151; RA Abramic M., Schleuder D., Dolovcak L., Schroeder W., Strupat K., Sagi D., RA Peter-Katalini J., Vitale L.; RT "Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric RT arguments for similarities and differences."; RL Biol. Chem. 381:1233-1243(2000). RN [9] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [10] 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 [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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] 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 [13] 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 [14] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-726 IN COMPLEX WITH ZINC AND RP OPIOID PEPTIDE, COFACTOR, AND ZINC-BINDING SITES. RX PubMed=22493238; DOI=10.1073/pnas.1118005109; RA Bezerra G.A., Dobrovetsky E., Viertlmayr R., Dong A., Binter A., RA Abramic M., Macheroux P., Dhe-Paganon S., Gruber K.; RT "Entropy-driven binding of opioid peptides induces a large domain motion in RT human dipeptidyl peptidase III."; RL Proc. Natl. Acad. Sci. U.S.A. 109:6525-6530(2012). CC -!- FUNCTION: Cleaves and degrades bioactive peptides, including CC angiotensin, Leu-enkephalin and Met-enkephalin (PubMed:3233187, CC PubMed:1515063). Also cleaves Arg-Arg-beta-naphthylamide (in vitro) CC (PubMed:9425109, PubMed:3233187, PubMed:11209758). CC {ECO:0000269|PubMed:11209758, ECO:0000269|PubMed:1515063, CC ECO:0000269|PubMed:3233187, ECO:0000269|PubMed:9425109}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal dipeptide from a peptide comprising CC four or more residues, with broad specificity. Also acts on CC dipeptidyl 2-naphthylamides.; EC=3.4.14.4; CC Evidence={ECO:0000269|PubMed:11209758, ECO:0000269|PubMed:1515063, CC ECO:0000269|PubMed:3233187, ECO:0000269|PubMed:9425109}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:11209758, ECO:0000269|PubMed:22493238, CC ECO:0000269|PubMed:9425109}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22493238}; CC -!- ACTIVITY REGULATION: Activated by Co(2+). Inhibited by EDTA and o- CC phenanthroline (in vitro). {ECO:0000269|PubMed:11209758, CC ECO:0000269|PubMed:1515063, ECO:0000269|PubMed:3233187, CC ECO:0000269|PubMed:9425109}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.8. {ECO:0000269|PubMed:11209758, CC ECO:0000269|PubMed:3233187, ECO:0000269|PubMed:9425109}; CC -!- INTERACTION: CC Q9NY33; Q14145: KEAP1; NbExp=10; IntAct=EBI-718333, EBI-751001; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1515063, CC ECO:0000269|PubMed:3233187}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9NY33-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NY33-2; Sequence=VSP_005510; CC Name=3; Synonyms=DPP3-BBS1; CC IsoId=Q8NFJ9-2; Sequence=External; CC Name=4; CC IsoId=Q9NY33-4; Sequence=VSP_044696; CC -!- TISSUE SPECIFICITY: Detected in placenta (at protein level) CC (PubMed:3233187). Detected in erythrocytes (at protein level) CC (PubMed:1515063). {ECO:0000269|PubMed:1515063, CC ECO:0000269|PubMed:3233187}. CC -!- MASS SPECTROMETRY: Mass=82500; Mass_error=60; Method=MALDI; CC Evidence={ECO:0000269|PubMed:11209758}; CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M49 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ271216; CAB72433.1; -; mRNA. DR EMBL; AK021449; BAB13828.1; -; mRNA. DR EMBL; AK297199; BAG59686.1; -; mRNA. DR EMBL; AK315478; BAG37862.1; -; mRNA. DR EMBL; AP002748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001446; AAH01446.1; -; mRNA. DR EMBL; BC007221; AAH07221.1; -; mRNA. DR EMBL; BC014038; AAH14038.1; -; mRNA. DR EMBL; BC024271; AAH24271.1; -; mRNA. DR EMBL; AB017970; BAA75785.1; -; mRNA. DR CCDS; CCDS58147.1; -. [Q9NY33-4] DR CCDS; CCDS8141.1; -. [Q9NY33-1] DR RefSeq; NP_001243599.1; NM_001256670.1. [Q9NY33-4] DR RefSeq; NP_005691.2; NM_005700.4. [Q9NY33-1] DR RefSeq; NP_569710.2; NM_130443.3. [Q9NY33-1] DR PDB; 3FVY; X-ray; 1.90 A; A=1-726. DR PDB; 3T6B; X-ray; 2.40 A; A/B=1-726. DR PDB; 3T6J; X-ray; 2.98 A; A=1-726. DR PDB; 5E2Q; X-ray; 2.40 A; A=1-726. DR PDB; 5E33; X-ray; 1.84 A; A=1-726. DR PDB; 5E3A; X-ray; 2.05 A; A=1-726. DR PDB; 5E3C; X-ray; 2.77 A; A=1-726. DR PDB; 5EGY; X-ray; 2.74 A; A=1-726. DR PDB; 5EHH; X-ray; 2.38 A; A=1-726. DR PDB; 7OUP; X-ray; 2.65 A; A=1-737. DR PDBsum; 3FVY; -. DR PDBsum; 3T6B; -. DR PDBsum; 3T6J; -. DR PDBsum; 5E2Q; -. DR PDBsum; 5E33; -. DR PDBsum; 5E3A; -. DR PDBsum; 5E3C; -. DR PDBsum; 5EGY; -. DR PDBsum; 5EHH; -. DR PDBsum; 7OUP; -. DR AlphaFoldDB; Q9NY33; -. DR SMR; Q9NY33; -. DR BioGRID; 115383; 34. DR DIP; DIP-53793N; -. DR IntAct; Q9NY33; 10. DR MINT; Q9NY33; -. DR STRING; 9606.ENSP00000440502; -. DR BindingDB; Q9NY33; -. DR ChEMBL; CHEMBL4520; -. DR MEROPS; M49.001; -. DR GlyGen; Q9NY33; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NY33; -. DR MetOSite; Q9NY33; -. DR PhosphoSitePlus; Q9NY33; -. DR SwissPalm; Q9NY33; -. DR BioMuta; DPP3; -. DR DMDM; 20532389; -. DR CPTAC; CPTAC-58; -. DR CPTAC; CPTAC-59; -. DR EPD; Q9NY33; -. DR jPOST; Q9NY33; -. DR MassIVE; Q9NY33; -. DR MaxQB; Q9NY33; -. DR PaxDb; 9606-ENSP00000353701; -. DR PeptideAtlas; Q9NY33; -. DR ProteomicsDB; 27822; -. DR ProteomicsDB; 83159; -. [Q9NY33-1] DR ProteomicsDB; 83160; -. [Q9NY33-2] DR Pumba; Q9NY33; -. DR Antibodypedia; 52373; 487 antibodies from 33 providers. DR DNASU; 10072; -. DR Ensembl; ENST00000530165.5; ENSP00000436941.1; ENSG00000254986.8. [Q9NY33-4] DR Ensembl; ENST00000531863.6; ENSP00000432782.2; ENSG00000254986.8. [Q9NY33-1] DR Ensembl; ENST00000541961.5; ENSP00000440502.1; ENSG00000254986.8. [Q9NY33-1] DR GeneID; 10072; -. DR KEGG; hsa:10072; -. DR MANE-Select; ENST00000531863.6; ENSP00000432782.2; NM_130443.4; NP_569710.2. DR UCSC; uc010rpe.3; human. [Q9NY33-1] DR AGR; HGNC:3008; -. DR CTD; 10072; -. DR DisGeNET; 10072; -. DR GeneCards; DPP3; -. DR HGNC; HGNC:3008; DPP3. DR HPA; ENSG00000254986; Low tissue specificity. DR MIM; 606818; gene. DR neXtProt; NX_Q9NY33; -. DR OpenTargets; ENSG00000254986; -. DR PharmGKB; PA27466; -. DR VEuPathDB; HostDB:ENSG00000254986; -. DR eggNOG; KOG3675; Eukaryota. DR GeneTree; ENSGT00390000007335; -. DR HOGENOM; CLU_011977_0_0_1; -. DR InParanoid; Q9NY33; -. DR OrthoDB; 5471561at2759; -. DR PhylomeDB; Q9NY33; -. DR TreeFam; TF300598; -. DR BRENDA; 3.4.14.4; 2681. DR PathwayCommons; Q9NY33; -. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway. DR SignaLink; Q9NY33; -. DR SIGNOR; Q9NY33; -. DR BioGRID-ORCS; 10072; 31 hits in 1154 CRISPR screens. DR ChiTaRS; DPP3; human. DR EvolutionaryTrace; Q9NY33; -. DR GeneWiki; DPP3; -. DR GenomeRNAi; 10072; -. DR Pharos; Q9NY33; Tbio. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9NY33; Protein. DR Bgee; ENSG00000254986; Expressed in mucosa of transverse colon and 175 other cell types or tissues. DR ExpressionAtlas; Q9NY33; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB. DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR Gene3D; 3.30.540.30; -; 3. DR InterPro; IPR005317; Dipeptidyl-peptase3. DR InterPro; IPR039461; Peptidase_M49. DR PANTHER; PTHR23422:SF11; DIPEPTIDYL PEPTIDASE 3; 1. DR PANTHER; PTHR23422; DIPEPTIDYL PEPTIDASE III-RELATED; 1. DR Pfam; PF03571; Peptidase_M49; 1. DR PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1. DR Genevisible; Q9NY33; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm; KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..737 FT /note="Dipeptidyl peptidase 3" FT /id="PRO_0000078238" FT ACT_SITE 451 FT /evidence="ECO:0000250|UniProtKB:O55096" FT BINDING 450 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:22493238, FT ECO:0007744|PDB:3FVY" FT BINDING 455 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:22493238, FT ECO:0007744|PDB:3FVY" FT BINDING 508 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:22493238, FT ECO:0007744|PDB:3FVY" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT VAR_SEQ 91..120 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044696" FT VAR_SEQ 182..601 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_005510" FT VARIANT 76 FT /note="R -> H (in dbSNP:rs11826683)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_033494" FT VARIANT 145 FT /note="Q -> H (in dbSNP:rs11550299)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_033495" FT VARIANT 678 FT /note="R -> H (in dbSNP:rs2305535)" FT /evidence="ECO:0000269|PubMed:9425109, ECO:0000269|Ref.1" FT /id="VAR_021850" FT VARIANT 690 FT /note="E -> K (in dbSNP:rs12421620)" FT /id="VAR_051597" FT CONFLICT 224 FT /note="P -> S (in Ref. 2; BAG59686)" FT /evidence="ECO:0000305" FT CONFLICT 417..419 FT /note="YAT -> TA (in Ref. 5; BAA75785)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="I -> Y (in Ref. 5; BAA75785)" FT /evidence="ECO:0000305" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:7OUP" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 20..25 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 28..50 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 56..69 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 72..81 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 86..102 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 120..128 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 131..135 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 137..152 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:3FVY" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 178..190 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 198..204 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:3T6J" FT STRAND 210..217 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:3T6B" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 242..250 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 252..266 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 272..287 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 290..302 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 307..316 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 318..323 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 327..335 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 337..346 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 350..353 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 354..356 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 372..384 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 388..392 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 396..401 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 405..409 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 410..416 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 421..423 FT /evidence="ECO:0007829|PDB:3FVY" FT HELIX 429..452 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 453..456 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 465..467 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 469..471 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 473..475 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 479..481 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 495..499 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 500..502 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 503..518 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 524..527 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 533..552 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 553..556 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 559..562 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 563..565 FT /evidence="ECO:0007829|PDB:3FVY" FT HELIX 567..581 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 586..593 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 597..605 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 607..609 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 610..613 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 614..630 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 634..644 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 651..653 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 655..664 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 671..673 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 676..680 FT /evidence="ECO:0007829|PDB:5E33" FT STRAND 683..687 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 693..701 FT /evidence="ECO:0007829|PDB:5E33" FT TURN 705..707 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 708..721 FT /evidence="ECO:0007829|PDB:5E33" FT HELIX 722..725 FT /evidence="ECO:0007829|PDB:5E33" SQ SEQUENCE 737 AA; 82589 MW; E2BB1923C9CAFDEC CRC64; MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAYHLSRA AWYGGLAVLL QTSPEAPYIY ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK EKLERVILGS EAAQQHPEEV RGLWQTCGEL MFSLEPRLRH LGLGKEGITT YFSGNCTMED AKLAQDFLDS QNLSAYNTRL FKEVDGEGKP YYEVRLASVL GSEPSLDSEV TSKLKSYEFR GSPFQVTRGD YAPILQKVVE QLEKAKAYAA NSHQGQMLAQ YIESFTQGSI EAHKRGSRFW IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAVVNKAMS AKFERLVASA EQLLKELPWP PTFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYATQ REKLTFLEED DKDLYILWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDQETVINPE TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL HPQVLEIFGF EGADAEDVIY VNWLNMVRAG LLALEFYTPE AFNWRQAHMQ ARFVILRVLL EAGEGLVTIT PTTGSDGRPD ARVRLDRSKI RSVGKPALER FLRRLQVLKS TGDVAGGRAL YEGYATVTDA PPECFLTLRD TVLLRKESRK LIVQPNTRLE GSDVQLLEYE ASAAGLIRSF SERFPEDGPE LEEILTQLAT ADARFWKGPS EAPSGQA //