CA2D4_HUMAN
ID CA2D4_HUMAN Reviewed; 1137 AA.
AC Q7Z3S7; Q7Z3S8; Q86XZ5; Q8IZS9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Voltage-dependent calcium channel subunit alpha-2/delta-4;
DE AltName: Full=Voltage-gated calcium channel subunit alpha-2/delta-4;
DE Contains:
DE RecName: Full=Voltage-dependent calcium channel subunit alpha-2-4;
DE Contains:
DE RecName: Full=Voltage-dependent calcium channel subunit delta-4;
DE Flags: Precursor;
GN Name=CACNA2D4;
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 1; 4; 5 AND 6), FUNCTION, TISSUE
RP SPECIFICITY, LACK OF GABAPENTIN-BINDING, INTERACTION WITH CACNA1C AND
RP CACNB3, AND VARIANT VAL-327.
RX PubMed=12181424; DOI=10.1124/mol.62.3.485;
RA Qin N., Yagel S., Momplaisir M.-L., Codd E.E., D'Andrea M.R.;
RT "Molecular cloning and characterization of the human voltage-gated calcium
RT channel alpha(2)delta-4 subunit.";
RL Mol. Pharmacol. 62:485-496(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-327.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Blood;
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 INVOLVEMENT IN RCD4.
RX PubMed=17033974; DOI=10.1086/508944;
RA Wycisk K.A., Zeitz C., Feil S., Wittmer M., Forster U., Neidhardt J.,
RA Wissinger B., Zrenner E., Wilke R., Kohl S., Berger W.;
RT "Mutation in the auxiliary calcium-channel subunit CACNA2D4 causes
RT autosomal recessive cone dystrophy.";
RL Am. J. Hum. Genet. 79:973-977(2006).
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. {ECO:0000269|PubMed:12181424}.
CC -!- SUBUNIT: Dimer formed of alpha-2-2 and delta-2 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 (Probable). Interacts with
CC CACNA1C and CACNB3. {ECO:0000269|PubMed:12181424, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Alpha2delta-4a;
CC IsoId=Q7Z3S7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3S7-2; Sequence=VSP_028070;
CC Name=4; Synonyms=Alpha2delta-4b;
CC IsoId=Q7Z3S7-4; Sequence=VSP_028069;
CC Name=5; Synonyms=Alpha2delta-4c;
CC IsoId=Q7Z3S7-5; Sequence=VSP_028071;
CC Name=6; Synonyms=Alpha2delta-4d;
CC IsoId=Q7Z3S7-6; Sequence=VSP_028069, VSP_028071;
CC Name=7;
CC IsoId=Q7Z3S7-7; Sequence=VSP_044107, VSP_044108, VSP_044109,
CC VSP_044110;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in certain types of
CC endocrine cells. Present in the Paneth cells of the small intestine.
CC Also present in the erythroblasts in the fetal liver, in the cells of
CC the zona reticularis of the adrenal gland and in the basophils of the
CC pituitary. Present at low level in some brain regions such as the
CC cerebellum (at protein level). {ECO:0000269|PubMed:12181424}.
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: May be proteolytically processed into subunits alpha-2-4 and
CC delta-4 that are disulfide-linked. It is however unclear whether such
CC cleavage really takes place in vivo and has a functional role (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Retinal cone dystrophy 4 (RCD4) [MIM:610478]: Characterized by
CC minimal symptoms except for slowly progressive reduction in visual
CC acuity. {ECO:0000269|PubMed:17033974}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: In contrast to CACNA2D1 and CACNA2D2, it does not bind
CC gabapentin, an antiepileptic drug.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: 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 calcium channel subunit alpha-2/delta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48288.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAN06672.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF516695; AAN06672.1; ALT_INIT; mRNA.
DR EMBL; BX537436; CAD97678.1; -; mRNA.
DR EMBL; BX537437; CAD97679.1; -; mRNA.
DR EMBL; AC005342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC048288; AAH48288.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44785.1; -. [Q7Z3S7-1]
DR RefSeq; NP_758952.4; NM_172364.4. [Q7Z3S7-1]
DR AlphaFoldDB; Q7Z3S7; -.
DR SMR; Q7Z3S7; -.
DR STRING; 9606.ENSP00000372169; -.
DR ChEMBL; CHEMBL2363032; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB00421; Spironolactone.
DR TCDB; 8.A.18.3.2; the ca(2+) channel auxiliary subunit Alpha2Delta types 1-4 (cca-Alpha2Delta) family.
DR GlyGen; Q7Z3S7; 2 sites.
DR iPTMnet; Q7Z3S7; -.
DR PhosphoSitePlus; Q7Z3S7; -.
DR BioMuta; CACNA2D4; -.
DR DMDM; 296434419; -.
DR EPD; Q7Z3S7; -.
DR jPOST; Q7Z3S7; -.
DR MassIVE; Q7Z3S7; -.
DR PaxDb; Q7Z3S7; -.
DR PeptideAtlas; Q7Z3S7; -.
DR PRIDE; Q7Z3S7; -.
DR ProteomicsDB; 69073; -. [Q7Z3S7-1]
DR ProteomicsDB; 69074; -. [Q7Z3S7-2]
DR ProteomicsDB; 69076; -. [Q7Z3S7-4]
DR ProteomicsDB; 69077; -. [Q7Z3S7-5]
DR ProteomicsDB; 69078; -. [Q7Z3S7-6]
DR Antibodypedia; 22099; 213 antibodies from 24 providers.
DR DNASU; 93589; -.
DR Ensembl; ENST00000382722.10; ENSP00000372169.4; ENSG00000151062.15. [Q7Z3S7-1]
DR Ensembl; ENST00000545595.6; ENSP00000442329.2; ENSG00000151062.15. [Q7Z3S7-7]
DR Ensembl; ENST00000585708.5; ENSP00000467697.1; ENSG00000151062.15. [Q7Z3S7-6]
DR Ensembl; ENST00000586184.5; ENSP00000465060.1; ENSG00000151062.15. [Q7Z3S7-5]
DR Ensembl; ENST00000588077.5; ENSP00000468530.1; ENSG00000151062.15. [Q7Z3S7-4]
DR Ensembl; ENST00000642910.1; ENSP00000494565.1; ENSG00000284953.2. [Q7Z3S7-6]
DR Ensembl; ENST00000644981.1; ENSP00000494395.1; ENSG00000284953.2. [Q7Z3S7-5]
DR Ensembl; ENST00000645018.2; ENSP00000495256.1; ENSG00000284953.2. [Q7Z3S7-1]
DR Ensembl; ENST00000645225.1; ENSP00000493490.1; ENSG00000284953.2. [Q7Z3S7-4]
DR Ensembl; ENST00000646498.1; ENSP00000494913.1; ENSG00000284953.2. [Q7Z3S7-7]
DR GeneID; 93589; -.
DR KEGG; hsa:93589; -.
DR MANE-Select; ENST00000382722.10; ENSP00000372169.4; NM_172364.5; NP_758952.4.
DR UCSC; uc058jsm.1; human. [Q7Z3S7-1]
DR CTD; 93589; -.
DR DisGeNET; 93589; -.
DR GeneCards; CACNA2D4; -.
DR HGNC; HGNC:20202; CACNA2D4.
DR HPA; ENSG00000151062; Tissue enriched (retina).
DR MalaCards; CACNA2D4; -.
DR MIM; 608171; gene.
DR MIM; 610478; phenotype.
DR neXtProt; NX_Q7Z3S7; -.
DR OpenTargets; ENSG00000151062; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR Orphanet; 215; Congenital stationary night blindness.
DR PharmGKB; PA130546913; -.
DR VEuPathDB; HostDB:ENSG00000151062; -.
DR eggNOG; KOG2353; Eukaryota.
DR GeneTree; ENSGT00940000155997; -.
DR HOGENOM; CLU_004660_1_1_1; -.
DR InParanoid; Q7Z3S7; -.
DR OMA; MLMWIIL; -.
DR OrthoDB; 69856at2759; -.
DR PhylomeDB; Q7Z3S7; -.
DR TreeFam; TF315824; -.
DR PathwayCommons; Q7Z3S7; -.
DR BioGRID-ORCS; 93589; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; CACNA2D4; human.
DR GenomeRNAi; 93589; -.
DR Pharos; Q7Z3S7; Tbio.
DR PRO; PR:Q7Z3S7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z3S7; protein.
DR Bgee; ENSG00000151062; Expressed in monocyte and 96 other tissues.
DR ExpressionAtlas; Q7Z3S7; baseline and differential.
DR Genevisible; Q7Z3S7; HS.
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:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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 Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1137
FT /note="Voltage-dependent calcium channel subunit alpha-
FT 2/delta-4"
FT /id="PRO_0000304655"
FT CHAIN 20..991
FT /note="Voltage-dependent calcium channel subunit alpha-2-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000304656"
FT CHAIN 992..1137
FT /note="Voltage-dependent calcium channel subunit delta-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000304657"
FT TOPO_DOM 20..1115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 291..473
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 487..580
FT /note="Cache"
FT MOTIF 297..301
FT /note="MIDAS-like motif"
FT BINDING 297
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 447..1097
FT /note="Interchain (between alpha-2-4 and delta-4 chains)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..855
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044107"
FT VAR_SEQ 1..76
FT /note="MVCGCSALLPLPNPRPTMPATPNFLANPSSSSRWIPLQPMPVAWAFVQKTSA
FT LLWLLLLGTSLSPAWGQAKIPLET -> MAVALGTRRRDR (in isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12181424"
FT /id="VSP_028069"
FT VAR_SEQ 872..886
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044108"
FT VAR_SEQ 908..911
FT /note="TGRF -> SDYV (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044109"
FT VAR_SEQ 912..1137
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044110"
FT VAR_SEQ 975..1137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028070"
FT VAR_SEQ 1104..1137
FT /note="ENAQDCGGASDTSASPPLLLLPVCAWGLLPQLLR -> VRVEADRGWAGFSS
FT PNPLCLGLCPCRQEHIGMPMNTPVPVLLGGNIRVYAL (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12181424"
FT /id="VSP_028071"
FT VARIANT 327
FT /note="I -> V (in dbSNP:rs10735005)"
FT /evidence="ECO:0000269|PubMed:12181424,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_035049"
FT VARIANT 863
FT /note="R -> H (in dbSNP:rs36077411)"
FT /id="VAR_035050"
FT VARIANT 869
FT /note="T -> M (in dbSNP:rs35331095)"
FT /id="VAR_035051"
FT CONFLICT 368
FT /note="K -> N (in Ref. 2; CAD97678)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="V -> A (in Ref. 1; AAN06672)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="T -> A (in Ref. 2; CAD97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="C -> Y (in Ref. 1; AAN06672)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="G -> E (in Ref. 2; CAD97679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1137 AA; 127938 MW; BF7FD169E1AF34F7 CRC64;
MVCGCSALLP LPNPRPTMPA TPNFLANPSS SSRWIPLQPM PVAWAFVQKT SALLWLLLLG
TSLSPAWGQA KIPLETVKLW ADTFGGDLYN TVTKYSGSLL LQKKYKDVES SLKIEEVDGL
ELVRKFSEDM ENMLRRKVEA VQNLVEAAEE ADLNHEFNES LVFDYYNSVL INERDEKGNF
VELGAEFLLE SNAHFSNLPV NTSISSVQLP TNVYNKDPDI LNGVYMSEAL NAVFVENFQR
DPTLTWQYFG SATGFFRIYP GIKWTPDENG VITFDCRNRG WYIQAATSPK DIVILVDVSG
SMKGLRMTIA KHTITTILDT LGENDFINII AYNDYVHYIE PCFKGILVQA DRDNREHFKL
LVEELMVKGV GVVDQALREA FQILKQFQEA KQGSLCNQAI MLISDGAVED YEPVFEKYNW
PDCKVRVFTY LIGREVSFAD RMKWIACNNK GYYTQISTLA DTQENVMEYL HVLSRPMVIN
HDHDIIWTEA YMDSKLLSSQ AQSLTLLTTV AMPVFSKKNE TRSHGILLGV VGSDVALREL
MKLAPRYKLG VHGYAFLNTN NGYILSHPDL RPLYREGKKL KPKPNYNSVD LSEVEWEDQA
ESLRTAMINR ETGTLSMDVK VPMDKGKRVL FLTNDYFFTD ISDTPFSLGV VLSRGHGEYI
LLGNTSVEEG LHDLLHPDLA LAGDWIYCIT DIDPDHRKLS QLEAMIRFLT RKDPDLECDE
ELVREVLFDA VVTAPMEAYW TALALNMSEE SEHVVDMAFL GTRAGLLRSS LFVGSEKVSD
RKFLTPEDEA SVFTLDRFPL WYRQASEHPA GSFVFNLRWA EGPESAGEPM VVTASTAVAV
TVDKRTAIAA AAGVQMKLEF LQRKFWAATR QCSTVDGPCT QSCEDSDLDC FVIDNNGFIL
ISKRSRETGR FLGEVDGAVL TQLLSMGVFS QVTMYDYQAM CKPSSHHHSA AQPLVSPISA
FLTATRWLLQ ELVLFLLEWS VWGSWYDRGA EAKSVFHHSH KHKKQDPLQP CDTEYPVFVY
QPAIREANGI VECGPCQKVF VVQQIPNSNL LLLVTDPTCD CSIFPPVLQE ATEVKYNASV
KCDRMRSQKL RRRPDSCHAF HPEENAQDCG GASDTSASPP LLLLPVCAWG LLPQLLR
