CA2D1_HUMAN
ID CA2D1_HUMAN Reviewed; 1103 AA.
AC P54289; Q17R45; Q9UD80; Q9UD81; Q9UD82;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-1;
DE AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-1;
DE Contains:
DE RecName: Full=Voltage-dependent calcium channel subunit alpha-2-1;
DE Contains:
DE RecName: Full=Voltage-dependent calcium channel subunit delta-1;
DE Flags: Precursor;
GN Name=CACNA2D1; Synonyms=CACNL2A, CCHL2A, MHS3;
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 2), AND TISSUE SPECIFICITY.
RX PubMed=1309651; DOI=10.1016/0896-6273(92)90109-q;
RA Williams M.E., Feldman D.H., McCue A.F., Brenner R., Velicelebi G.,
RA Ellis S.B., Harpold M.M.;
RT "Structure and functional expression of alpha 1, alpha 2, and beta subunits
RT of a novel human neuronal calcium channel subtype.";
RL Neuron 8:71-84(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 528-648 (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC TISSUE=Neuroblastoma;
RX PubMed=8107964; DOI=10.1016/0028-3908(93)90004-m;
RA Brust P.F., Simerson S., McCue A.F., Deal C.R., Schoonmaker S.,
RA Williams M.E., Velicelebi G., Johnson E.C., Harpold M.M., Ellis S.B.;
RT "Human neuronal voltage-dependent calcium channels: studies on subunit
RT structure and role in channel assembly.";
RL Neuropharmacology 32:1089-1102(1993).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136; ASN-324 AND ASN-675.
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-475 AND ASN-824.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP INTERCHAIN DISULFIDE BOND, AND SUBUNIT.
RX PubMed=22054663; DOI=10.1016/j.ceca.2011.10.002;
RA Calderon-Rivera A., Andrade A., Hernandez-Hernandez O.,
RA Gonzalez-Ramirez R., Sandoval A., Rivera M., Gomora J.C., Felix R.;
RT "Identification of a disulfide bridge essential for structure and function
RT of the voltage-gated Ca(2+) channel alpha(2)delta-1 auxiliary subunit.";
RL Cell Calcium 51:22-30(2012).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 38-361 IN COMPLEX WITH
RP HUMAN CAV2.2/CACNA1B AND BETA-3 SUBUNIT IN PRESENCE AND ABSENCE OF THE
RP OMEGA-CONOTOXIN MVIIA, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-92;
RP ASN-184; ASN-348; ASN-468; ASN-613; ASN-781 AND ASN-895.
RX PubMed=34234349; DOI=10.1038/s41586-021-03699-6;
RA Gao S., Yao X., Yan N.;
RT "Structure of human Cav2.2 channel blocked by the painkiller ziconotide.";
RL Nature 596:143-147(2021).
CC -!- FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium
CC channels regulates calcium current density and activation/inactivation
CC kinetics of the calcium channel. Plays an important role in excitation-
CC contraction coupling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Dimer formed of alpha-2-1 and delta-1 chains; disulfide-
CC linked. Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1 (CACNA1), alpha-2 (CACNA2D), beta (CACNB) and
CC delta (CACNA2D) subunits in a 1:1:1:1 ratio (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Alpha-2a;
CC IsoId=P54289-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-2b;
CC IsoId=P54289-2; Sequence=VSP_038348, VSP_038350;
CC Name=3; Synonyms=Alpha-2c;
CC IsoId=P54289-3; Sequence=VSP_038349, VSP_038350;
CC Name=4; Synonyms=Alpha-2d;
CC IsoId=P54289-4; Sequence=VSP_038349;
CC Name=5; Synonyms=Alpha-2e;
CC IsoId=P54289-5; Sequence=VSP_038348;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle. Isoform
CC 2 is expressed in the central nervous system. Isoform 2, isoform 4 and
CC isoform 5 are expressed in neuroblastoma cells. Isoform 3, isoform 4
CC and isoform 5 are expressed in the aorta. {ECO:0000269|PubMed:1309651,
CC ECO:0000269|PubMed:8107964}.
CC -!- DOMAIN: The MIDAS-like motif in the VWFA domain binds divalent metal
CC cations and is required to promote trafficking of the alpha-1 (CACNA1)
CC subunit to the plasma membrane by an integrin-like switch.
CC {ECO:0000250}.
CC -!- PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that
CC are disulfide-linked. {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds gabapentin, an antiepileptic drug.
CC -!- SIMILARITY: Belongs to the calcium channel subunit alpha-2/delta
CC family. {ECO:0000305}.
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DR EMBL; M76559; AAA51903.1; -; mRNA.
DR EMBL; CH471091; EAW76990.1; -; Genomic_DNA.
DR EMBL; BC117468; AAI17469.1; -; mRNA.
DR EMBL; BC117470; AAI17471.1; -; mRNA.
DR CCDS; CCDS5598.1; -. [P54289-2]
DR PIR; JH0565; JH0565.
DR RefSeq; NP_000713.2; NM_000722.3. [P54289-2]
DR RefSeq; XP_005250627.1; XM_005250570.2.
DR RefSeq; XP_005250629.1; XM_005250572.2. [P54289-3]
DR RefSeq; XP_005250630.1; XM_005250573.2. [P54289-5]
DR RefSeq; XP_005250631.1; XM_005250574.2. [P54289-4]
DR PDB; 7MIX; EM; 3.00 A; D=1-1103.
DR PDB; 7MIY; EM; 3.10 A; D=1-1103.
DR PDB; 7VFS; EM; 2.80 A; B=1-1103.
DR PDB; 7VFU; EM; 3.00 A; B=1-1103.
DR PDB; 7VFV; EM; 3.00 A; B=1-1103.
DR PDB; 7VFW; EM; 3.30 A; B=1-1103.
DR PDBsum; 7MIX; -.
DR PDBsum; 7MIY; -.
DR PDBsum; 7VFS; -.
DR PDBsum; 7VFU; -.
DR PDBsum; 7VFV; -.
DR PDBsum; 7VFW; -.
DR AlphaFoldDB; P54289; -.
DR SMR; P54289; -.
DR BioGRID; 107235; 78.
DR ComplexPortal; CPX-3192; Skeletal muscle VGCC complex.
DR ComplexPortal; CPX-3195; Cardiac muscle voltage-gated calcium channel complex.
DR CORUM; P54289; -.
DR IntAct; P54289; 34.
DR STRING; 9606.ENSP00000349320; -.
DR BindingDB; P54289; -.
DR ChEMBL; CHEMBL1919; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB04838; Cyclandelate.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB01023; Felodipine.
DR DrugBank; DB00996; Gabapentin.
DR DrugBank; DB08872; Gabapentin enacarbil.
DR DrugBank; DB00308; Ibutilide.
DR DrugBank; DB00270; Isradipine.
DR DrugBank; DB00622; Nicardipine.
DR DrugBank; DB06712; Nilvadipine.
DR DrugBank; DB00401; Nisoldipine.
DR DrugBank; DB01054; Nitrendipine.
DR DrugBank; DB00230; Pregabalin.
DR DrugBank; DB00421; Spironolactone.
DR DrugCentral; P54289; -.
DR TCDB; 8.A.18.1.1; the ca(2+) channel auxiliary subunit Alpha2Delta types 1-4 (cca-Alpha2Delta) family.
DR GlyConnect; 1895; 24 N-Linked glycans (7 sites).
DR GlyGen; P54289; 17 sites, 25 N-linked glycans (7 sites).
DR iPTMnet; P54289; -.
DR PhosphoSitePlus; P54289; -.
DR SwissPalm; P54289; -.
DR BioMuta; CACNA2D1; -.
DR DMDM; 262527579; -.
DR EPD; P54289; -.
DR jPOST; P54289; -.
DR MassIVE; P54289; -.
DR MaxQB; P54289; -.
DR PaxDb; P54289; -.
DR PeptideAtlas; P54289; -.
DR PRIDE; P54289; -.
DR ProteomicsDB; 56675; -. [P54289-1]
DR ProteomicsDB; 56676; -. [P54289-2]
DR ProteomicsDB; 56677; -. [P54289-3]
DR ProteomicsDB; 56678; -. [P54289-4]
DR ProteomicsDB; 56679; -. [P54289-5]
DR Antibodypedia; 2200; 282 antibodies from 35 providers.
DR DNASU; 781; -.
DR Ensembl; ENST00000356253.9; ENSP00000348589.5; ENSG00000153956.16. [P54289-1]
DR Ensembl; ENST00000356860.8; ENSP00000349320.3; ENSG00000153956.16. [P54289-2]
DR GeneID; 781; -.
DR KEGG; hsa:781; -.
DR MANE-Select; ENST00000356860.8; ENSP00000349320.3; NM_000722.4; NP_000713.2. [P54289-2]
DR UCSC; uc003uhr.2; human. [P54289-1]
DR CTD; 781; -.
DR DisGeNET; 781; -.
DR GeneCards; CACNA2D1; -.
DR GeneReviews; CACNA2D1; -.
DR HGNC; HGNC:1399; CACNA2D1.
DR HPA; ENSG00000153956; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; CACNA2D1; -.
DR MIM; 114204; gene.
DR neXtProt; NX_P54289; -.
DR OpenTargets; ENSG00000153956; -.
DR Orphanet; 130; Brugada syndrome.
DR Orphanet; 51083; Familial short QT syndrome.
DR PharmGKB; PA86; -.
DR VEuPathDB; HostDB:ENSG00000153956; -.
DR eggNOG; KOG2353; Eukaryota.
DR GeneTree; ENSGT00940000155209; -.
DR HOGENOM; CLU_004660_0_0_1; -.
DR InParanoid; P54289; -.
DR OMA; FWMNSFM; -.
DR PhylomeDB; P54289; -.
DR TreeFam; TF315824; -.
DR PathwayCommons; P54289; -.
DR SignaLink; P54289; -.
DR BioGRID-ORCS; 781; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; CACNA2D1; human.
DR GeneWiki; CACNA2D1; -.
DR GenomeRNAi; 781; -.
DR Pharos; P54289; Tclin.
DR PRO; PR:P54289; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P54289; protein.
DR Bgee; ENSG00000153956; Expressed in biceps brachii and 184 other tissues.
DR ExpressionAtlas; P54289; baseline and differential.
DR Genevisible; P54289; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:BHF-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0061577; P:calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISS:BHF-UCL.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; IMP:BHF-UCL.
DR GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IC:ComplexPortal.
DR GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IGI:ARUK-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISS:BHF-UCL.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013680; VDCC_a2/dsu.
DR InterPro; IPR013608; VWA_N.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF08473; VGCC_alpha2; 1.
DR Pfam; PF13768; VWA_3; 1.
DR Pfam; PF08399; VWA_N; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium channel;
KW Calcium transport; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1103
FT /note="Voltage-dependent calcium channel subunit alpha-
FT 2/delta-1"
FT /id="PRO_0000304633"
FT CHAIN 25..956
FT /note="Voltage-dependent calcium channel subunit alpha-2-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005001"
FT CHAIN 957..1103
FT /note="Voltage-dependent calcium channel subunit delta-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005002"
FT TOPO_DOM 25..1073
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1074..1094
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1095..1103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 253..430
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 446..556
FT /note="Cache"
FT MOTIF 259..263
FT /note="MIDAS-like motif"
FT BINDING 259
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54290"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:34234349,
FT ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 404..1059
FT /note="Interchain (between alpha-2-1 and delta-1 chains)"
FT VAR_SEQ 531..554
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8107964"
FT /id="VSP_038349"
FT VAR_SEQ 531..549
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:1309651,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8107964"
FT /id="VSP_038348"
FT VAR_SEQ 644
FT /note="Y -> SKKGKMKD (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:1309651,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8107964"
FT /id="VSP_038350"
FT VARIANT 1019
FT /note="E -> D (in dbSNP:rs9886043)"
FT /id="VAR_053960"
FT VARIANT 1057
FT /note="D -> A (in dbSNP:rs35131433)"
FT /id="VAR_035047"
FT CONFLICT 99
FT /note="R -> S (in Ref. 1; AAA51903)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="T -> R (in Ref. 1; AAA51903)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> E (in Ref. 1; AAA51903)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="L -> I (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 30..52
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 75..109
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 187..198
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 288..303
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 312..323
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 397..404
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 432..436
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 457..467
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 483..493
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 494..498
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 570..579
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 584..593
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 600..611
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 618..624
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 628..633
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 640..646
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:7MIX"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 676..688
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 699..716
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 717..723
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 727..736
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 743..748
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 762..769
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 771..776
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 780..785
FT /evidence="ECO:0007829|PDB:7MIX"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 800..804
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 810..816
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 818..827
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 855..857
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 858..866
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 868..870
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 875..878
FT /evidence="ECO:0007829|PDB:7VFS"
FT HELIX 880..888
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 891..904
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 972..983
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 989..994
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 997..999
FT /evidence="ECO:0007829|PDB:7MIY"
FT STRAND 1001..1007
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1014..1016
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1021..1023
FT /evidence="ECO:0007829|PDB:7MIX"
FT STRAND 1036..1038
FT /evidence="ECO:0007829|PDB:7MIX"
FT HELIX 1043..1046
FT /evidence="ECO:0007829|PDB:7VFS"
FT STRAND 1047..1049
FT /evidence="ECO:0007829|PDB:7VFS"
FT TURN 1072..1074
FT /evidence="ECO:0007829|PDB:7MIX"
SQ SEQUENCE 1103 AA; 124568 MW; 0749685DE9DB0700 CRC64;
MAAGCLLALT LTLFQSLLIG PSSEEPFPSA VTIKSWVDKM QEDLVTLAKT ASGVNQLVDI
YEKYQDLYTV EPNNARQLVE IAARDIEKLL SNRSKALVRL ALEAEKVQAA HQWREDFASN
EVVYYNAKDD LDPEKNDSEP GSQRIKPVFI EDANFGRQIS YQHAAVHIPT DIYEGSTIVL
NELNWTSALD EVFKKNREED PSLLWQVFGS ATGLARYYPA SPWVDNSRTP NKIDLYDVRR
RPWYIQGAAS PKDMLILVDV SGSVSGLTLK LIRTSVSEML ETLSDDDFVN VASFNSNAQD
VSCFQHLVQA NVRNKKVLKD AVNNITAKGI TDYKKGFSFA FEQLLNYNVS RANCNKIIML
FTDGGEERAQ EIFNKYNKDK KVRVFTFSVG QHNYDRGPIQ WMACENKGYY YEIPSIGAIR
INTQEYLDVL GRPMVLAGDK AKQVQWTNVY LDALELGLVI TGTLPVFNIT GQFENKTNLK
NQLILGVMGV DVSLEDIKRL TPRFTLCPNG YYFAIDPNGY VLLHPNLQPK PIGVGIPTIN
LRKRRPNIQN PKSQEPVTLD FLDAELENDI KVEIRNKMID GESGEKTFRT LVKSQDERYI
DKGNRTYTWT PVNGTDYSLA LVLPTYSFYY IKAKLEETIT QARYSETLKP DNFEESGYTF
IAPRDYCNDL KISDNNTEFL LNFNEFIDRK TPNNPSCNAD LINRVLLDAG FTNELVQNYW
SKQKNIKGVK ARFVVTDGGI TRVYPKEAGE NWQENPETYE DSFYKRSLDN DNYVFTAPYF
NKSGPGAYES GIMVSKAVEI YIQGKLLKPA VVGIKIDVNS WIENFTKTSI RDPCAGPVCD
CKRNSDVMDC VILDDGGFLL MANHDDYTNQ IGRFFGEIDP SLMRHLVNIS VYAFNKSYDY
QSVCEPGAAP KQGAGHRSAY VPSVADILQI GWWATAAAWS ILQQFLLSLT FPRLLEAVEM
EDDDFTASLS KQSCITEQTQ YFFDNDSKSF SGVLDCGNCS RIFHGEKLMN TNLIFIMVES
KGTCPCDTRL LIQAEQTSDG PNPCDMVKQP RYRKGPDVCF DNNVLEDYTD CGGVSGLNPS
LWYIIGIQFL LLWLVSGSTH RLL
