CAPS1_HUMAN
ID CAPS1_HUMAN Reviewed; 1353 AA.
AC Q9ULU8; A6NF60; Q13339; Q6GQQ6; Q8N2Z5; Q8N3M7; Q8NFR0; Q96BC2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Calcium-dependent secretion activator 1;
DE AltName: Full=Calcium-dependent activator protein for secretion 1;
DE Short=CAPS-1;
GN Name=CADPS; Synonyms=CAPS, CAPS1, KIAA1121;
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=12659812; DOI=10.1016/s0888-7543(02)00040-x;
RA Cisternas F.A., Vincent J.B., Scherer S.W., Ray P.N.;
RT "Cloning and characterization of human CADPS and CADPS2, new members of the
RT Ca2+-dependent activator for secretion protein family.";
RL Genomics 81:279-291(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-1353 (ISOFORM 3).
RC TISSUE=Amygdala;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1108-1353 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=9289490; DOI=10.1074/jbc.272.32.19637;
RA Ann K., Kowalchyk J.A., Loyet K.M., Martin T.F.J.;
RT "Novel Ca2+-binding protein (CAPS) related to UNC-31 required for Ca2+-
RT activated exocytosis.";
RL J. Biol. Chem. 272:19637-19640(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1109-1353 (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 320-1353 (ISOFORM 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1121-1353.
RC TISSUE=PNS, and Skin;
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 [8]
RP INTERACTION WITH DRD2.
RX PubMed=15857609; DOI=10.1016/j.bcp.2005.02.015;
RA Binda A.V., Kabbani N., Levenson R.;
RT "Regulation of dense core vesicle release from PC12 cells by interaction
RT between the D2 dopamine receptor and calcium-dependent activator protein
RT for secretion (CAPS).";
RL Biochem. Pharmacol. 69:1451-1461(2005).
RN [9]
RP STRUCTURE BY NMR OF 522-634.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of human calcium-dependent activator
RT protein for secretion (CAPS).";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles
CC filled with neurotransmitters and neuropeptides. Probably acts upstream
CC of fusion in the biogenesis or maintenance of mature secretory
CC vesicles. Regulates catecholamine loading of DCVs. May specifically
CC mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles
CC (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-
CC binding protein that acts at prefusion step following ATP-dependent
CC priming and participates in DCVs-membrane fusion. However, it may also
CC participate in small clear synaptic vesicles (SVs) exocytosis and it is
CC unclear whether its function is related to Ca(2+) triggering (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RASL10B (By
CC similarity). Interacts with the dopamine receptor DRD2. {ECO:0000250,
CC ECO:0000269|PubMed:15857609}.
CC -!- INTERACTION:
CC Q9ULU8-4; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-10180690, EBI-10175124;
CC Q9ULU8-4; O00560: SDCBP; NbExp=3; IntAct=EBI-10180690, EBI-727004;
CC Q9ULU8-4; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-10180690, EBI-10172590;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q62717}.
CC Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle
CC membrane {ECO:0000250|UniProtKB:Q62717}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62717}. Note=Membrane-associated to vesicles.
CC Strongly enriched in synaptic fractions. Preferentially binds to dense
CC core vesicles but not to synaptic vesicles. Binds phosphoinosides, with
CC a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably
CC localizes to different vesicles compared to CADPS2.
CC {ECO:0000250|UniProtKB:Q62717}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ULU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULU8-2; Sequence=VSP_016803, VSP_016805, VSP_016806,
CC VSP_016807;
CC Name=3;
CC IsoId=Q9ULU8-3; Sequence=VSP_016804, VSP_016806, VSP_016807;
CC Name=4;
CC IsoId=Q9ULU8-4; Sequence=VSP_016808;
CC Name=5;
CC IsoId=Q9ULU8-5; Sequence=VSP_016801, VSP_016802;
CC -!- TISSUE SPECIFICITY: Specifically expressed in neural and endocrine
CC secretory tissues. Expressed in brain and pancreas and at low level in
CC heart. Also expressed in fetal heart, cerebellum, cerebral cortex,
CC medulla, occipital pole, frontal and temporal lobes, and putamen, as
CC well as weak expression in spinal cord. {ECO:0000269|PubMed:12659812}.
CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC phospholipids and plasma membrane. It however does not mediate binding
CC to DCVs (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79701.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH15754.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA86435.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF458662; AAM61861.1; -; mRNA.
DR EMBL; AB032947; BAA86435.2; ALT_INIT; mRNA.
DR EMBL; AC104161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833895; CAD38751.1; -; mRNA.
DR EMBL; U36448; AAA79701.1; ALT_FRAME; mRNA.
DR EMBL; BC015754; AAH15754.1; ALT_INIT; mRNA.
DR EMBL; BC029460; AAH29460.1; -; mRNA.
DR EMBL; BC072684; AAH72684.1; -; mRNA.
DR CCDS; CCDS2898.1; -. [Q9ULU8-2]
DR CCDS; CCDS2899.1; -. [Q9ULU8-3]
DR CCDS; CCDS46858.1; -. [Q9ULU8-1]
DR RefSeq; NP_003707.2; NM_003716.3. [Q9ULU8-1]
DR RefSeq; NP_899630.1; NM_183393.2. [Q9ULU8-2]
DR RefSeq; NP_899631.1; NM_183394.2. [Q9ULU8-3]
DR PDB; 1WI1; NMR; -; A=522-634.
DR PDBsum; 1WI1; -.
DR AlphaFoldDB; Q9ULU8; -.
DR SMR; Q9ULU8; -.
DR BioGRID; 114174; 57.
DR IntAct; Q9ULU8; 14.
DR MINT; Q9ULU8; -.
DR STRING; 9606.ENSP00000373215; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR iPTMnet; Q9ULU8; -.
DR PhosphoSitePlus; Q9ULU8; -.
DR SwissPalm; Q9ULU8; -.
DR BioMuta; CADPS; -.
DR DMDM; 85540963; -.
DR EPD; Q9ULU8; -.
DR jPOST; Q9ULU8; -.
DR MassIVE; Q9ULU8; -.
DR MaxQB; Q9ULU8; -.
DR PaxDb; Q9ULU8; -.
DR PeptideAtlas; Q9ULU8; -.
DR PRIDE; Q9ULU8; -.
DR ProteomicsDB; 85123; -. [Q9ULU8-1]
DR ProteomicsDB; 85124; -. [Q9ULU8-2]
DR ProteomicsDB; 85125; -. [Q9ULU8-3]
DR ProteomicsDB; 85126; -. [Q9ULU8-4]
DR ProteomicsDB; 85127; -. [Q9ULU8-5]
DR Antibodypedia; 31723; 150 antibodies from 29 providers.
DR DNASU; 8618; -.
DR Ensembl; ENST00000283269.13; ENSP00000283269.9; ENSG00000163618.18. [Q9ULU8-3]
DR Ensembl; ENST00000357948.7; ENSP00000350632.3; ENSG00000163618.18. [Q9ULU8-2]
DR Ensembl; ENST00000383710.9; ENSP00000373215.4; ENSG00000163618.18. [Q9ULU8-1]
DR Ensembl; ENST00000490353.2; ENSP00000418736.2; ENSG00000163618.18. [Q9ULU8-5]
DR GeneID; 8618; -.
DR KEGG; hsa:8618; -.
DR MANE-Select; ENST00000383710.9; ENSP00000373215.4; NM_003716.4; NP_003707.2.
DR UCSC; uc003dll.3; human. [Q9ULU8-1]
DR CTD; 8618; -.
DR DisGeNET; 8618; -.
DR GeneCards; CADPS; -.
DR HGNC; HGNC:1426; CADPS.
DR HPA; ENSG00000163618; Group enriched (brain, retina).
DR MIM; 604667; gene.
DR neXtProt; NX_Q9ULU8; -.
DR OpenTargets; ENSG00000163618; -.
DR PharmGKB; PA26024; -.
DR VEuPathDB; HostDB:ENSG00000163618; -.
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00950000183306; -.
DR HOGENOM; CLU_007068_0_0_1; -.
DR InParanoid; Q9ULU8; -.
DR OMA; RWEIKGN; -.
DR OrthoDB; 138870at2759; -.
DR PhylomeDB; Q9ULU8; -.
DR TreeFam; TF312963; -.
DR PathwayCommons; Q9ULU8; -.
DR SignaLink; Q9ULU8; -.
DR SIGNOR; Q9ULU8; -.
DR BioGRID-ORCS; 8618; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; CADPS; human.
DR EvolutionaryTrace; Q9ULU8; -.
DR GeneWiki; CADPS; -.
DR GenomeRNAi; 8618; -.
DR Pharos; Q9ULU8; Tbio.
DR PRO; PR:Q9ULU8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9ULU8; protein.
DR Bgee; ENSG00000163618; Expressed in pons and 143 other tissues.
DR ExpressionAtlas; Q9ULU8; baseline and differential.
DR Genevisible; Q9ULU8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0099012; C:neuronal dense core vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0045921; P:positive regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR033227; CAPS.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12166; PTHR12166; 1.
DR Pfam; PF06292; MUN; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasmic vesicle;
KW Exocytosis; Lipid-binding; Membrane; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..1353
FT /note="Calcium-dependent secretion activator 1"
FT /id="PRO_0000053864"
FT DOMAIN 380..495
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 521..624
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 931..1111
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..1129
FT /note="Interaction with DRD2"
FT /evidence="ECO:0000269|PubMed:15857609"
FT REGION 1177..1353
FT /note="Mediates targeting and association with DCVs"
FT /evidence="ECO:0000250"
FT REGION 1329..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TJ1"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT VAR_SEQ 443..457
FT /note="WGTQGDFSTTHALPA -> VIRRNRREQLPHSAI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016801"
FT VAR_SEQ 458..1353
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016802"
FT VAR_SEQ 685..701
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12659812"
FT /id="VSP_016803"
FT VAR_SEQ 861..867
FT /note="ENQKDAE -> GKKREMYEHPVFCLASQVMDLTIQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016804"
FT VAR_SEQ 861..866
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12659812"
FT /id="VSP_016805"
FT VAR_SEQ 902..908
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12659812,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_016806"
FT VAR_SEQ 1009..1058
FT /note="KSLTSNLPNVNLPNVNLPKVPNLPVNIPLGIPQMPTFSAPSWMAAIYDAD
FT -> N (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12659812,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_016807"
FT VAR_SEQ 1159
FT /note="E -> EFAKMW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9289490"
FT /id="VSP_016808"
FT CONFLICT 62
FT /note="G -> S (in Ref. 1; AAM61861)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="S -> Y (in Ref. 6; AAA79701)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="A -> P (in Ref. 6; AAA79701)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="V -> G (in Ref. 6; AAA79701)"
FT /evidence="ECO:0000305"
FT CONFLICT 1250
FT /note="E -> G (in Ref. 1; AAM61861 and 5; CAD38751)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="M -> V (in Ref. 2; BAA86435)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310
FT /note="L -> F (in Ref. 1; AAM61861)"
FT /evidence="ECO:0000305"
FT STRAND 522..531
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 540..550
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:1WI1"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:1WI1"
FT HELIX 609..623
FT /evidence="ECO:0007829|PDB:1WI1"
SQ SEQUENCE 1353 AA; 152786 MW; 9911C50B3A507112 CRC64;
MLDPSSSEEE SDEIVEEESG KEVLGSAPSG ARLSPSRTSE GSAGSAGLGG GGAGAGAGVG
AGGGGGSGAS SGGGAGGLQP SSRAGGGRPS SPSPSVVSEK EKEELERLQK EEEERKKRLQ
LYVFVMRCIA YPFNAKQPTD MARRQQKISK QQLQTVKDRF QAFLNGETQI MADEAFMNAV
QSYYEVFLKS DRVARMVQSG GCSANDSREV FKKHIEKRVR SLPEIDGLSK ETVLSSWMAK
FDAIYRGEED PRKQQARMTA SAASELILSK EQLYEMFQNI LGIKKFEHQL LYNACQLDNP
DEQAAQIRRE LDGRLQMADQ IARERKFPKF VSKEMENMYI EELKSSVNLL MANLESMPVS
KGGEFKLQKL KRSHNASIID MGEESENQLS KSDVVLSFSL EVVIMEVQGL KSLAPNRIVY
CTMEVEGGEK LQTDQAEASK PTWGTQGDFS TTHALPAVKV KLFTESTGVL ALEDKELGRV
ILHPTPNSPK QSEWHKMTVS KNCPDQDLKI KLAVRMDKPQ NMKHSGYLWA IGKNVWKRWK
KRFFVLVQVS QYTFAMCSYR EKKAEPQELL QLDGYTVDYT DPQPGLEGGR AFFNAVKEGD
TVIFASDDEQ DRILWVQAMY RATGQSHKPV PPTQVQKLNA KGGNVPQLDA PISQFYADRA
QKHGMDEFIS SNPCNFDHAS LFEMVQRLTL DHRLNDSYSC LGWFSPGQVF VLDEYCARNG
VRGCHRHLCY LRDLLERAEN GAMIDPTLLH YSFAFCASHV HGNRPDGIGT VTVEEKERFE
EIKERLRVLL ENQITHFRYC FPFGRPEGAL KATLSLLERV LMKDIVTPVP QEEVKTVIRK
CLEQAALVNY SRLSEYAKIE ENQKDAENVG RLITPAKKLE DTIRLAELVI EVLQQNEEHH
AEPHVDKGEA FAWWSDLMVE HAETFLSLFA VDMDAALEVQ PPDTWDSFPL FQLLNDFLRT
DYNLCNGKFH KHLQDLFAPL VVRYVDLMES SIAQSIHRGF ERESWEPVKS LTSNLPNVNL
PNVNLPKVPN LPVNIPLGIP QMPTFSAPSW MAAIYDADNG SGTSEDLFWK LDALQTFIRD
LHWPEEEFGK HLEQRLKLMA SDMIESCVKR TRIAFEVKLQ KTSRSTDFRV PQSICTMFNV
MVDAKAQSTK LCSMEMGQEH QYHSKIDELI EETVKEMITL LVAKFVTILE GVLAKLSRYD
EGTLFSSFLS FTVKAASKYV DVPKPGMDVA DAYVTFVRHS QDVLRDKVNE EMYIERLFDQ
WYNSSMNVIC TWLTDRMDLQ LHIYQLKTLI RMVKKTYRDF RLQGVLDSTL NSKTYETIRN
RLTVEEATAS VSEGGGLQGI SMKDSDEEDE EDD
