ID DPP6_HUMAN Reviewed; 865 AA. AC P42658; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Dipeptidyl aminopeptidase-like protein 6; DE AltName: Full=DPPX; DE AltName: Full=Dipeptidyl aminopeptidase-related protein; DE AltName: Full=Dipeptidyl peptidase 6; DE AltName: Full=Dipeptidyl peptidase IV-like protein; DE AltName: Full=Dipeptidyl peptidase VI; DE Short=DPP VI; GN Name=DPP6; 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] (ISOFORMS DPPX-L AND DPPX-S), VARIANT PRO-854, RP AND LACK OF CATALYTIC ACTIVITY. RC TISSUE=Hippocampus; RX PubMed=8103397; DOI=10.1093/hmg/2.7.1037; RA Yokotani N., Doi K., Wenthold R.J., Wada K.; RT "Non-conservation of a catalytic residue in a dipeptidyl aminopeptidase IV- RT related protein encoded by a gene on human chromosome 7."; RL Hum. Mol. Genet. 2:1037-1039(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] RP INTERACTION WITH KCND2, GLYCOSYLATION, AND FUNCTION. RX PubMed=15454437; DOI=10.1529/biophysj.104.042358; RA Jerng H.H., Qian Y., Pfaffinger P.J.; RT "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase RT 10 (DPP10)."; RL Biophys. J. 87:2380-2396(2004). RN [4] RP INTERACTION WITH KCND2, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH KCND2 AND RP KCNIP2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18364354; DOI=10.1074/jbc.m706964200; RA Soh H., Goldstein S.A.; RT "I SA channel complexes include four subunits each of DPP6 and Kv4.2."; RL J. Biol. Chem. 283:15072-15077(2008). RN [5] RP INVOLVEMENT IN SUSCEPTIBILITY TO ALS. RX PubMed=18084291; DOI=10.1038/ng.2007.52; RA van Es M.A., van Vught P.W.J., Blauw H.M., Franke L., Saris C.G.J., RA Van den Bosch L., de Jong S.W., de Jong V., Baas F., van't Slot R., RA Lemmens R., Schelhaas H.J., Birve A., Sleegers K., Van Broeckhoven C., RA Schymick J.C., Traynor B.J., Wokke J.H.J., Wijmenga C., Robberecht W., RA Andersen P.M., Veldink J.H., Ophoff R.A., van den Berg L.H.; RT "Genetic variation in DPP6 is associated with susceptibility to amyotrophic RT lateral sclerosis."; RL Nat. Genet. 40:29-31(2008). RN [6] RP DISCUSSION OF THE INVOLVEMENT IN SUSCEPTIBILITY TO ALS. RX PubMed=18174402; DOI=10.1126/science.319.5859.20; RA Garber K.; RT "Genetics. The elusive ALS genes."; RL Science 319:20-20(2008). RN [7] RP INVOLVEMENT IN VF2. RX PubMed=19285295; DOI=10.1016/j.ajhg.2009.02.009; RA Alders M., Koopmann T.T., Christiaans I., Postema P.G., Beekman L., RA Tanck M.W., Zeppenfeld K., Loh P., Koch K.T., Demolombe S., Mannens M.M., RA Bezzina C.R., Wilde A.A.; RT "Haplotype-sharing analysis implicates chromosome 7q36 harboring DPP6 in RT familial idiopathic ventricular fibrillation."; RL Am. J. Hum. Genet. 84:468-476(2009). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19441798; DOI=10.1021/bi802316m; RA Seikel E., Trimmer J.S.; RT "Convergent modulation of Kv4.2 channel alpha subunits by structurally RT distinct DPPX and KChIP auxiliary subunits."; RL Biochemistry 48:5721-5730(2009). RN [9] RP INVOLVEMENT IN MRD33, AND VARIANT MRD33 LEU-385. RX PubMed=23832105; DOI=10.1016/j.ejmg.2013.06.008; RA Liao C., Fu F., Li R., Yang W.Q., Liao H.Y., Yan J.R., Li J., Li S.Y., RA Yang X., Li D.Z.; RT "Loss-of-function variation in the DPP6 gene is associated with autosomal RT dominant microcephaly and mental retardation."; RL Eur. J. Med. Genet. 56:484-489(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 127-849, FUNCTION, DISULFIDE RP BONDS, AND GLYCOSYLATION AT ASN-173; ASN-319; ASN-404; ASN-535; ASN-566 AND RP ASN-813. RX PubMed=15476821; DOI=10.1016/j.jmb.2004.09.003; RA Strop P., Bankovich A.J., Hansen K.C., Garcia K.C., Brunger A.T.; RT "Structure of a human A-type potassium channel interacting protein DPPX, a RT member of the dipeptidyl aminopeptidase family."; RL J. Mol. Biol. 343:1055-1065(2004). CC -!- FUNCTION: Promotes cell surface expression of the potassium channel CC KCND2 (PubMed:15454437, PubMed:19441798). Modulates the activity and CC gating characteristics of the potassium channel KCND2 CC (PubMed:18364354). Has no dipeptidyl aminopeptidase activity CC (PubMed:8103397, PubMed:15476821). {ECO:0000269|PubMed:15454437, CC ECO:0000269|PubMed:18364354, ECO:0000269|PubMed:8103397, CC ECO:0000305|PubMed:15476821}. CC -!- SUBUNIT: Homodimer (in vitro) (PubMed:15476821). Interacts with KCND2 CC (PubMed:15454437, PubMed:18364354). Identified in a complex with KCND2 CC and KCNIP2 (PubMed:18364354). Forms an octameric complex composed of CC four DPP6 subunits bound to the KCND2 tetramer (PubMed:18364354). CC {ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:15476821, CC ECO:0000269|PubMed:18364354, ECO:0000269|PubMed:19441798}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18364354, CC ECO:0000269|PubMed:19441798}; Single-pass type II membrane protein CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=DPPX-L; CC IsoId=P42658-1; Sequence=Displayed; CC Name=DPPX-S; CC IsoId=P42658-2; Sequence=VSP_005365; CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15454437}. CC -!- DISEASE: Familial paroxysmal ventricular fibrillation 2 (VF2) CC [MIM:612956]: A cardiac arrhythmia marked by fibrillary contractions of CC the ventricular muscle due to rapid repetitive excitation of myocardial CC fibers without coordinated contraction of the ventricle and by absence CC of atrial activity. {ECO:0000269|PubMed:19285295}. Note=The disease is CC caused by variants affecting the gene represented in this entry. A CC genetic variation 340 bases upstream from the ATG start site of the CC DPP6 gene is the cause of familial paroxysmal ventricular fibrillation CC type 2. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 33 CC (MRD33) [MIM:616311]: A disorder characterized by significantly below CC average general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. MRD33 CC patients manifest microcephaly in addition to intellectual disability. CC {ECO:0000269|PubMed:23832105}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Genetic variation in DPP6 may influence susceptibility CC to amyotrophic lateral sclerosis (ALS). ALS is a severely disabling and CC lethal disorder caused by progressive degeneration of motor neurons in CC the brain, spinal cord and brainstem. CC -!- SIMILARITY: Belongs to the peptidase S9B 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; M96859; AAA35760.1; -; mRNA. DR EMBL; M96860; AAA35761.1; -; mRNA. DR EMBL; AC006019; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC024239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC024730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC073336; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS75683.1; -. [P42658-1] DR CCDS; CCDS75684.1; -. [P42658-2] DR PIR; I54331; I54331. DR PIR; I68600; I68600. DR RefSeq; NP_570629.2; NM_130797.3. [P42658-1] DR PDB; 1XFD; X-ray; 3.00 A; A/B/C/D=127-849. DR PDB; 7E87; EM; 3.40 A; E/F/I/J=93-120. DR PDB; 7E89; EM; 4.00 A; A/B/I/J=121-849. DR PDB; 7E8B; EM; 4.20 A; I/J/K/L=93-849. DR PDB; 7E8E; EM; 3.90 A; I/J/K/L=94-120. DR PDB; 7E8G; EM; 4.50 A; I/J/K/L=121-849. DR PDB; 7E8H; EM; 4.50 A; I/J/K/L=94-849. DR PDB; 7UKG; EM; 2.24 A; I/J/K/L=82-865. DR PDBsum; 1XFD; -. DR PDBsum; 7E87; -. DR PDBsum; 7E89; -. DR PDBsum; 7E8B; -. DR PDBsum; 7E8E; -. DR PDBsum; 7E8G; -. DR PDBsum; 7E8H; -. DR PDBsum; 7UKG; -. DR AlphaFoldDB; P42658; -. DR EMDB; EMD-31011; -. DR EMDB; EMD-31012; -. DR EMDB; EMD-31013; -. DR EMDB; EMD-31016; -. DR EMDB; EMD-31018; -. DR EMDB; EMD-31019; -. DR SMR; P42658; -. DR BioGRID; 108138; 26. DR IntAct; P42658; 4. DR STRING; 9606.ENSP00000367001; -. DR ESTHER; human-DPP6; DPP4N_Peptidase_S9. DR MEROPS; S09.973; -. DR TCDB; 8.A.51.1.1; the dipeptidyl-aminopeptidase-like protein 6 beta subunit of kv4 channels (dpp6) family. DR GlyCosmos; P42658; 8 sites, 1 glycan. DR GlyGen; P42658; 8 sites, 1 O-linked glycan (1 site). DR iPTMnet; P42658; -. DR PhosphoSitePlus; P42658; -. DR SwissPalm; P42658; -. DR BioMuta; DPP6; -. DR DMDM; 218512016; -. DR MassIVE; P42658; -. DR PaxDb; 9606-ENSP00000367001; -. DR PeptideAtlas; P42658; -. DR ProteomicsDB; 55521; -. [P42658-1] DR ProteomicsDB; 55522; -. [P42658-2] DR ABCD; P42658; 5 sequenced antibodies. DR Antibodypedia; 33071; 267 antibodies from 27 providers. DR DNASU; 1804; -. DR Ensembl; ENST00000332007.7; ENSP00000328226.3; ENSG00000130226.18. [P42658-2] DR Ensembl; ENST00000377770.8; ENSP00000367001.3; ENSG00000130226.18. [P42658-1] DR GeneID; 1804; -. DR KEGG; hsa:1804; -. DR MANE-Select; ENST00000377770.8; ENSP00000367001.3; NM_130797.4; NP_570629.2. DR UCSC; uc003wlk.4; human. [P42658-1] DR AGR; HGNC:3010; -. DR CTD; 1804; -. DR DisGeNET; 1804; -. DR GeneCards; DPP6; -. DR HGNC; HGNC:3010; DPP6. DR HPA; ENSG00000130226; Tissue enhanced (brain, endometrium). DR MalaCards; DPP6; -. DR MIM; 126141; gene. DR MIM; 612956; phenotype. DR MIM; 616311; phenotype. DR neXtProt; NX_P42658; -. DR OpenTargets; ENSG00000130226; -. DR Orphanet; 2514; Autosomal dominant primary microcephaly. DR Orphanet; 228140; Idiopathic ventricular fibrillation, non Brugada type. DR PharmGKB; PA27468; -. DR VEuPathDB; HostDB:ENSG00000130226; -. DR eggNOG; KOG2100; Eukaryota. DR GeneTree; ENSGT00940000156280; -. DR InParanoid; P42658; -. DR OMA; GERYMDT; -. DR OrthoDB; 2876738at2759; -. DR PhylomeDB; P42658; -. DR TreeFam; TF313309; -. DR PathwayCommons; P42658; -. DR SignaLink; P42658; -. DR SIGNOR; P42658; -. DR BioGRID-ORCS; 1804; 13 hits in 392 CRISPR screens. DR ChiTaRS; DPP6; human. DR EvolutionaryTrace; P42658; -. DR GeneWiki; DPP6; -. DR GenomeRNAi; 1804; -. DR Pharos; P42658; Tbio. DR PRO; PR:P42658; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P42658; Protein. DR Bgee; ENSG00000130226; Expressed in middle temporal gyrus and 162 other cell types or tissues. DR ExpressionAtlas; P42658; baseline and differential. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001375; Peptidase_S9. DR InterPro; IPR002469; Peptidase_S9B_N. DR PANTHER; PTHR11731:SF20; DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6; 1. DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1. DR Pfam; PF00930; DPPIV_N; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1. DR Genevisible; P42658; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disease variant; KW Disulfide bond; Glycoprotein; Intellectual disability; Membrane; KW Neurodegeneration; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1..865 FT /note="Dipeptidyl aminopeptidase-like protein 6" FT /id="PRO_0000122409" FT TOPO_DOM 1..95 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 117..865 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 1..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 173 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT CARBOHYD 319 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT CARBOHYD 404 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT CARBOHYD 471 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 535 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT CARBOHYD 566 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT CARBOHYD 813 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15476821" FT DISULFID 411..418 FT /evidence="ECO:0000269|PubMed:15476821" FT DISULFID 527..530 FT /evidence="ECO:0000269|PubMed:15476821" FT DISULFID 536..554 FT /evidence="ECO:0000269|PubMed:15476821" FT DISULFID 735..846 FT /evidence="ECO:0000269|PubMed:15476821" FT VAR_SEQ 1..81 FT /note="MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDGGAGAKPLGPRAQAAA FT PRERGGGGGGAGGRPRFQYQARSDGDEED -> MTTAKEPSASGKSVQQQEQ (in FT isoform DPPX-S)" FT /evidence="ECO:0000303|PubMed:8103397" FT /id="VSP_005365" FT VARIANT 385 FT /note="M -> L (in MRD33; dbSNP:rs786205143)" FT /evidence="ECO:0000269|PubMed:23832105" FT /id="VAR_073680" FT VARIANT 854 FT /note="L -> P (in dbSNP:rs3734960)" FT /evidence="ECO:0000269|PubMed:8103397" FT /id="VAR_051579" FT CONFLICT 73 FT /note="A -> G (in Ref. 1; AAA35760)" FT /evidence="ECO:0000305" FT CONFLICT 520 FT /note="V -> E (in Ref. 1; AAA35760/AAA35761)" FT /evidence="ECO:0000305" FT HELIX 96..116 FT /evidence="ECO:0007829|PDB:7UKG" FT HELIX 133..136 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 165..168 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 176..179 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 181..188 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 198..206 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 217..226 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 254..258 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 261..270 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 291..295 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 298..306 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 310..319 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 325..328 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 353..364 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 376..378 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 379..400 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 405..412 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 418..425 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 445..452 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 460..466 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 483..485 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 487..494 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 495..498 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 499..507 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 513..517 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 532..535 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 540..543 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 547..553 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 556..559 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 562..566 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 567..569 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 572..577 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 580..587 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 599..601 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 604..606 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 609..612 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 618..620 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 622..627 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 645..651 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 656..658 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 666..668 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 669..674 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 675..678 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 680..682 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 683..696 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 697..711 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 713..720 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 734..740 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 747..749 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 750..757 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 767..770 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 773..776 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 783..789 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 793..795 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 797..809 FT /evidence="ECO:0007829|PDB:1XFD" FT STRAND 815..819 FT /evidence="ECO:0007829|PDB:1XFD" FT HELIX 829..843 FT /evidence="ECO:0007829|PDB:1XFD" FT TURN 844..847 FT /evidence="ECO:0007829|PDB:1XFD" SQ SEQUENCE 865 AA; 97588 MW; D3E654013F19D951 CRC64; MASLYQRFTG KINTSRSFPA PPEASHLLGG QGPEEDGGAG AKPLGPRAQA AAPRERGGGG GGAGGRPRFQ YQARSDGDEE DELVGSNPPQ RNWKGIAIAL LVILVICSLI VTSVILLTPA EDNSLSQKKK VTVEDLFSED FKIHDPEAKW ISDTEFIYRE QKGTVRLWNV ETNTSTVLIE GKKIESLRAI RYEISPDREY ALFSYNVEPI YQHSYTGYYV LSKIPHGDPQ SLDPPEVSNA KLQYAGWGPK GQQLIFIFEN NIYYCAHVGK QAIRVVSTGK EGVIYNGLSD WLYEEEILKT HIAHWWSPDG TRLAYAAIND SRVPIMELPT YTGSIYPTVK PYHYPKAGSE NPSISLHVIG LNGPTHDLEM MPPDDPRMRE YYITMVKWAT STKVAVTWLN RAQNVSILTL CDATTGVCTK KHEDESEAWL HRQNEEPVFS KDGRKFFFIR AIPQGGRGKF YHITVSSSQP NSSNDNIQSI TSGDWDVTKI LAYDEKGNKI YFLSTEDLPR RRQLYSANTV GNFNRQCLSC DLVENCTYFS ASFSHSMDFF LLKCEGPGVP MVTVHNTTDK KKMFDLETNE HVKKAINDRQ MPKVEYRDIE IDDYNLPMQI LKPATFTDTT HYPLLLVVDG TPGSQSVAEK FEVSWETVMV SSHGAVVVKC DGRGSGFQGT KLLHEVRRRL GLLEEKDQME AVRTMLKEQY IDRTRVAVFG KDYGGYLSTY ILPAKGENQG QTFTCGSALS PITDFKLYAS AFSERYLGLH GLDNRAYEMT KVAHRVSALE EQQFLIIHPT ADEKIHFQHT AELITQLIRG KANYSLQIYP DESHYFTSSS LKQHLYRSII NFFVECFRIQ DKLLTVTAKE DEEED //