DPP6_HUMAN
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 03-AUG-2022, entry version 187.
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}.
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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 PDBsum; 1XFD; -.
DR PDBsum; 7E87; -.
DR PDBsum; 7E89; -.
DR PDBsum; 7E8B; -.
DR PDBsum; 7E8E; -.
DR PDBsum; 7E8G; -.
DR PDBsum; 7E8H; -.
DR AlphaFoldDB; P42658; -.
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 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; P42658; -.
DR PeptideAtlas; P42658; -.
DR PRIDE; P42658; -.
DR ProteomicsDB; 55521; -. [P42658-1]
DR ProteomicsDB; 55522; -. [P42658-2]
DR ABCD; P42658; 5 sequenced antibodies.
DR Antibodypedia; 33071; 241 antibodies from 27 providers.
DR DNASU; 1804; -.
DR Ensembl; ENST00000332007.7; ENSP00000328226.3; ENSG00000130226.17. [P42658-2]
DR Ensembl; ENST00000377770.8; ENSP00000367001.3; ENSG00000130226.17. [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 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; MYGERYM; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; P42658; -.
DR TreeFam; TF313309; -.
DR PathwayCommons; P42658; -.
DR SignaLink; P42658; -.
DR BioGRID-ORCS; 1804; 13 hits in 318 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 161 other tissues.
DR ExpressionAtlas; P42658; baseline and differential.
DR Genevisible; P42658; HS.
DR GO; GO:0016021; C:integral component of 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
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 95..117
FT /evidence="ECO:0007829|PDB:7E87"
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
