DPP3_HUMAN
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 03-AUG-2022, entry version 193.
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=8; 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; 29.
DR DIP; DIP-53793N; -.
DR IntAct; Q9NY33; 9.
DR MINT; Q9NY33; -.
DR STRING; 9606.ENSP00000353701; -.
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; Q9NY33; -.
DR PeptideAtlas; Q9NY33; -.
DR PRIDE; Q9NY33; -.
DR ProteomicsDB; 27822; -.
DR ProteomicsDB; 83159; -. [Q9NY33-1]
DR ProteomicsDB; 83160; -. [Q9NY33-2]
DR Antibodypedia; 52373; 435 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 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; 1448344at2759; -.
DR PhylomeDB; Q9NY33; -.
DR TreeFam; TF300598; -.
DR BRENDA; 3.4.14.4; 2681.
DR PathwayCommons; Q9NY33; -.
DR SignaLink; Q9NY33; -.
DR SIGNOR; Q9NY33; -.
DR BioGRID-ORCS; 10072; 30 hits in 1079 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 173 other tissues.
DR ExpressionAtlas; Q9NY33; baseline and differential.
DR Genevisible; Q9NY33; HS.
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:0008239; F:dipeptidyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR005317; Dipeptidyl-peptase3.
DR InterPro; IPR039461; Peptidase_M49.
DR PANTHER; PTHR23422; PTHR23422; 1.
DR Pfam; PF03571; Peptidase_M49; 1.
DR PIRSF; PIRSF007828; Dipeptidyl-peptidase_III; 1.
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
