DSC2_HUMAN
ID DSC2_HUMAN Reviewed; 901 AA.
AC Q02487;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Desmocollin-2 {ECO:0000303|PubMed:28256248};
DE AltName: Full=Cadherin family member 2;
DE AltName: Full=Desmocollin-3;
DE AltName: Full=Desmosomal glycoprotein II;
DE AltName: Full=Desmosomal glycoprotein III;
DE Flags: Precursor;
GN Name=DSC2 {ECO:0000312|HGNC:HGNC:3036}; Synonyms=CDHF2, DSC3;
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 2A AND 2B).
RC TISSUE=Keratinocyte;
RX PubMed=2037591; DOI=10.1016/s0021-9258(18)99244-6;
RA Parker A.E., Wheeler G.N., Arnemann J., Pidsley S.C., Ataliotis P.,
RA Thomas C.L., Rees D.A., Magee A.I., Buxton R.S.;
RT "Desmosomal glycoproteins II and III. Cadherin-like junctional molecules
RT generated by alternative splicing.";
RL J. Biol. Chem. 266:10438-10445(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A).
RC TISSUE=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 [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-392 AND ASN-629.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [5]
RP INVOLVEMENT IN ARVD11.
RX PubMed=17033975; DOI=10.1086/509122;
RA Syrris P., Ward D., Evans A., Asimaki A., Gandjbakhch E., Sen-Chowdhry S.,
RA McKenna W.J.;
RT "Arrhythmogenic right ventricular dysplasia/cardiomyopathy associated with
RT mutations in the desmosomal gene desmocollin-2.";
RL Am. J. Hum. Genet. 79:978-984(2006).
RN [6]
RP GLYCOSYLATION AT ASN-392.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH DSP; PKP2 AND JUP, VARIANTS ARVD11
RP CYS-203 AND MET-275, AND CHARACTERIZATION OF VARIANTS ARVD11 CYS-203 AND
RP MET-275.
RX PubMed=21062920; DOI=10.1093/cvr/cvq353;
RA Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A.,
RA Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C.,
RA Saffitz J.E., Protonotarios N., McKenna W.J.;
RT "Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy
RT caused by desmocollin-2 mutations.";
RL Cardiovasc. Res. 90:77-87(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-868 AND SER-873, AND
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 [9]
RP VARIANTS ILE-358; VAL-776 AND GLN-798.
RX PubMed=18678517; DOI=10.1016/j.ymgme.2008.06.005;
RA Posch M.G., Posch M.J., Geier C., Erdmann B., Mueller W., Richter A.,
RA Ruppert V., Pankuweit S., Maisch B., Perrot A., Buttgereit J., Dietz R.,
RA Haverkamp W., Ozcelik C.;
RT "A missense variant in desmoglein-2 predisposes to dilated
RT cardiomyopathy.";
RL Mol. Genet. Metab. 95:74-80(2008).
RN [10]
RP VARIANTS SER-11; VAL-596; HIS-638; VAL-776 AND GLN-798.
RX PubMed=20031617; DOI=10.1161/circgenetics.109.858217;
RA den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A.,
RA Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D.,
RA Bluemke D.A., Calkins H., Dalal D., Judge D.P.;
RT "Comprehensive desmosome mutation analysis in North Americans with
RT arrhythmogenic right ventricular dysplasia/cardiomyopathy.";
RL Circ. Cardiovasc. Genet. 2:428-435(2009).
RN [11]
RP VARIANTS ARVD11 THR-231 AND ALA-340, AND VARIANT GLN-798.
RX PubMed=19863551; DOI=10.1111/j.1399-0004.2009.01282.x;
RA Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L.,
RA Robb L., Talajic M., Brugada R.;
RT "Role of genetic testing in arrhythmogenic right ventricular
RT cardiomyopathy/dysplasia.";
RL Clin. Genet. 77:37-48(2010).
RN [12]
RP VARIANT ARVD11 MET-364.
RX PubMed=28256248; DOI=10.1016/j.amjcard.2017.01.011;
RA Liu J.S., Fan L.L., Li J.J., Xiang R.;
RT "Whole-Exome Sequencing Identifies a Novel Mutation of Desmocollin 2 in a
RT Chinese Family With Arrhythmogenic Right Ventricular Cardiomyopathy.";
RL Am. J. Cardiol. 119:1485-1489(2017).
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion. May contribute to epidermal cell positioning
CC (stratification) by mediating differential adhesiveness between cells
CC that express different isoforms.
CC -!- SUBUNIT: Interacts with DSP, PKP2 and JUP.
CC {ECO:0000269|PubMed:21062920}.
CC -!- INTERACTION:
CC Q02487-1; P17302: GJA1; NbExp=2; IntAct=EBI-6900677, EBI-1103439;
CC Q02487-1; Q6TYA9: GJA1; Xeno; NbExp=3; IntAct=EBI-6900677, EBI-6901331;
CC Q02487-1; F1M7L9; Xeno; NbExp=2; IntAct=EBI-6900677, EBI-6900770;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21062920};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:21062920}. Cell
CC junction, desmosome {ECO:0000269|PubMed:21062920}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2A; Synonyms=DGII;
CC IsoId=Q02487-1; Sequence=Displayed;
CC Name=2B; Synonyms=DGIII;
CC IsoId=Q02487-2; Sequence=VSP_000657, VSP_000658;
CC -!- TISSUE SPECIFICITY: Expressed in epithelia, myocardium and lymph nodes.
CC -!- DOMAIN: Calcium may be bound by the cadherin-like repeats.
CC {ECO:0000305}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC -!- DISEASE: Arrhythmogenic right ventricular dysplasia, familial, 11
CC (ARVD11) [MIM:610476]: A congenital heart disease characterized by
CC infiltration of adipose and fibrous tissue into the right ventricle and
CC loss of myocardial cells, resulting in ventricular and supraventricular
CC arrhythmias. {ECO:0000269|PubMed:17033975, ECO:0000269|PubMed:19863551,
CC ECO:0000269|PubMed:21062920, ECO:0000269|PubMed:28256248}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40141.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA40142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X56807; CAA40141.1; ALT_INIT; mRNA.
DR EMBL; X56807; CAA40142.1; ALT_INIT; mRNA.
DR EMBL; BC063291; AAH63291.1; -; mRNA.
DR CCDS; CCDS11892.1; -. [Q02487-1]
DR CCDS; CCDS11893.1; -. [Q02487-2]
DR PIR; A40390; IJHUDB.
DR PIR; B40390; IJHUDA.
DR RefSeq; NP_004940.1; NM_004949.4. [Q02487-2]
DR RefSeq; NP_077740.1; NM_024422.4. [Q02487-1]
DR PDB; 5ERP; X-ray; 2.70 A; A/B=236-680.
DR PDB; 5J5J; X-ray; 3.29 A; A=136-235.
DR PDB; 7A7D; EM; 26.00 A; a/b/c/d/e/f/g=136-679.
DR PDBsum; 5ERP; -.
DR PDBsum; 5J5J; -.
DR PDBsum; 7A7D; -.
DR AlphaFoldDB; Q02487; -.
DR SMR; Q02487; -.
DR BioGRID; 108158; 186.
DR IntAct; Q02487; 26.
DR MINT; Q02487; -.
DR STRING; 9606.ENSP00000280904; -.
DR CarbonylDB; Q02487; -.
DR GlyConnect; 1171; 41 N-Linked glycans (5 sites).
DR GlyGen; Q02487; 6 sites, 39 N-linked glycans (5 sites).
DR iPTMnet; Q02487; -.
DR PhosphoSitePlus; Q02487; -.
DR SwissPalm; Q02487; -.
DR BioMuta; DSC2; -.
DR DMDM; 461968; -.
DR EPD; Q02487; -.
DR jPOST; Q02487; -.
DR MassIVE; Q02487; -.
DR MaxQB; Q02487; -.
DR PaxDb; Q02487; -.
DR PeptideAtlas; Q02487; -.
DR PRIDE; Q02487; -.
DR ProteomicsDB; 58097; -. [Q02487-1]
DR ProteomicsDB; 58098; -. [Q02487-2]
DR ABCD; Q02487; 4 sequenced antibodies.
DR Antibodypedia; 2782; 347 antibodies from 32 providers.
DR DNASU; 1824; -.
DR Ensembl; ENST00000251081.8; ENSP00000251081.6; ENSG00000134755.18. [Q02487-2]
DR Ensembl; ENST00000280904.11; ENSP00000280904.6; ENSG00000134755.18. [Q02487-1]
DR GeneID; 1824; -.
DR KEGG; hsa:1824; -.
DR MANE-Select; ENST00000280904.11; ENSP00000280904.6; NM_024422.6; NP_077740.1.
DR UCSC; uc002kwk.5; human. [Q02487-1]
DR CTD; 1824; -.
DR DisGeNET; 1824; -.
DR GeneCards; DSC2; -.
DR GeneReviews; DSC2; -.
DR HGNC; HGNC:3036; DSC2.
DR HPA; ENSG00000134755; Tissue enhanced (esophagus, vagina).
DR MalaCards; DSC2; -.
DR MIM; 125645; gene.
DR MIM; 610476; phenotype.
DR neXtProt; NX_Q02487; -.
DR OpenTargets; ENSG00000134755; -.
DR Orphanet; 293899; Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
DR Orphanet; 293888; Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
DR Orphanet; 293910; Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
DR PharmGKB; PA27489; -.
DR VEuPathDB; HostDB:ENSG00000134755; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_2_1; -.
DR InParanoid; Q02487; -.
DR OMA; LCNCITE; -.
DR OrthoDB; 120970at2759; -.
DR PhylomeDB; Q02487; -.
DR TreeFam; TF316817; -.
DR PathwayCommons; Q02487; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q02487; -.
DR BioGRID-ORCS; 1824; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; DSC2; human.
DR GeneWiki; DSC2; -.
DR GenomeRNAi; 1824; -.
DR Pharos; Q02487; Tbio.
DR PRO; PR:Q02487; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q02487; protein.
DR Bgee; ENSG00000134755; Expressed in gingival epithelium and 173 other tissues.
DR ExpressionAtlas; Q02487; baseline and differential.
DR Genevisible; Q02487; HS.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030057; C:desmosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0086083; F:cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication; IC:BHF-UCL.
DR GO; GO:0086073; P:bundle of His cell-Purkinje myocyte adhesion involved in cell communication; IMP:BHF-UCL.
DR GO; GO:0086042; P:cardiac muscle cell-cardiac muscle cell adhesion; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cardiomyopathy; Cell adhesion;
KW Cell junction; Cell membrane; Cleavage on pair of basic residues;
KW Disease variant; Glycoprotein; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..135
FT /evidence="ECO:0000255"
FT /id="PRO_0000003869"
FT CHAIN 136..901
FT /note="Desmocollin-2"
FT /id="PRO_0000003870"
FT TOPO_DOM 136..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 136..243
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 244..355
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 356..471
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 472..579
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 580..694
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT VAR_SEQ 837..847
FT /note="KVYLCNQDENH -> ESIRGHTLIKN (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:2037591"
FT /id="VSP_000657"
FT VAR_SEQ 848..901
FT /note="Missing (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:2037591"
FT /id="VSP_000658"
FT VARIANT 11
FT /note="N -> S (in dbSNP:rs868333)"
FT /evidence="ECO:0000269|PubMed:20031617"
FT /id="VAR_029480"
FT VARIANT 203
FT /note="R -> C (in ARVD11; fails to undergo complete
FT processing into a mature form; fails to localize at the
FT desmosomes; dbSNP:rs142331975)"
FT /evidence="ECO:0000269|PubMed:21062920"
FT /id="VAR_065687"
FT VARIANT 231
FT /note="I -> T (in ARVD11; dbSNP:rs1390387214)"
FT /evidence="ECO:0000269|PubMed:19863551"
FT /id="VAR_065688"
FT VARIANT 275
FT /note="T -> M (in ARVD11; can be processed into a mature
FT form but shows a higher pro-protein to mature protein
FT ratio; only a proportion of the partly functional mutant is
FT incorporated into the desmosomes; dbSNP:rs397517404)"
FT /evidence="ECO:0000269|PubMed:21062920"
FT /id="VAR_065689"
FT VARIANT 340
FT /note="T -> A (in ARVD11; dbSNP:rs368299411)"
FT /evidence="ECO:0000269|PubMed:19863551"
FT /id="VAR_065690"
FT VARIANT 358
FT /note="T -> I (in dbSNP:rs139399951)"
FT /evidence="ECO:0000269|PubMed:18678517"
FT /id="VAR_062391"
FT VARIANT 364
FT /note="V -> M (in ARVD11)"
FT /evidence="ECO:0000269|PubMed:28256248"
FT /id="VAR_078340"
FT VARIANT 596
FT /note="A -> V (in dbSNP:rs148185335)"
FT /evidence="ECO:0000269|PubMed:20031617"
FT /id="VAR_065691"
FT VARIANT 638
FT /note="Q -> H (in dbSNP:rs147742157)"
FT /evidence="ECO:0000269|PubMed:20031617"
FT /id="VAR_065692"
FT VARIANT 776
FT /note="I -> V (in dbSNP:rs1893963)"
FT /evidence="ECO:0000269|PubMed:18678517,
FT ECO:0000269|PubMed:20031617"
FT /id="VAR_024388"
FT VARIANT 798
FT /note="R -> Q (in dbSNP:rs61731921)"
FT /evidence="ECO:0000269|PubMed:18678517,
FT ECO:0000269|PubMed:19863551, ECO:0000269|PubMed:20031617"
FT /id="VAR_062392"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5J5J"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:5J5J"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:5J5J"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5J5J"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5J5J"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5ERP"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 318..327
FT /evidence="ECO:0007829|PDB:5ERP"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 354..365
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 429..441
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 472..481
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 558..568
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 590..595
FT /evidence="ECO:0007829|PDB:5ERP"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:5ERP"
FT TURN 617..622
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 624..636
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 648..653
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:5ERP"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:5ERP"
SQ SEQUENCE 901 AA; 99962 MW; 30F7E3D33ECA67CC CRC64;
MEAARPSGSW NGALCRLLLL TLAILIFASD ACKNVTLHVP SKLDAEKLVG RVNLKECFTA
ANLIHSSDPD FQILEDGSVY TTNTILLSSE KRSFTILLSN TENQEKKKIF VFLEHQTKVL
KKRHTKEKVL RRAKRRWAPI PCSMLENSLG PFPLFLQQVQ SDTAQNYTIY YSIRGPGVDQ
EPRNLFYVER DTGNLYCTRP VDREQYESFE IIAFATTPDG YTPELPLPLI IKIEDENDNY
PIFTEETYTF TIFENCRVGT TVGQVCATDK DEPDTMHTRL KYSIIGQVPP SPTLFSMHPT
TGVITTTSSQ LDRELIDKYQ LKIKVQDMDG QYFGLQTTST CIINIDDVND HLPTFTRTSY
VTSVEENTVD VEILRVTVED KDLVNTANWR ANYTILKGNE NGNFKIVTDA KTNEGVLCVV
KPLNYEEKQQ MILQIGVVNE APFSREASPR SAMSTATVTV NVEDQDEGPE CNPPIQTVRM
KENAEVGTTS NGYKAYDPET RSSSGIRYKK LTDPTGWVTI DENTGSIKVF RSLDREAETI
KNGIYNITVL ASDQGGRTCT GTLGIILQDV NDNSPFIPKK TVIICKPTMS SAEIVAVDPD
EPIHGPPFDF SLESSTSEVQ RMWRLKAIND TAARLSYQND PPFGSYVVPI TVRDRLGMSS
VTSLDVTLCD CITENDCTHR VDPRIGGGGV QLGKWAILAI LLGIALLFCI LFTLVCGASG
TSKQPKVIPD DLAQQNLIVS NTEAPGDDKV YSANGFTTQT VGASAQGVCG TVGSGIKNGG
QETIEMVKGG HQTSESCRGA GHHHTLDSCR GGHTEVDNCR YTYSEWHSFT QPRLGEKVYL
CNQDENHKHA QDYVLTYNYE GRGSVAGSVG CCSERQEEDG LEFLDNLEPK FRTLAEACMK
R
