CAPS_DROME
ID CAPS_DROME Reviewed; 1447 AA.
AC Q9NHE5; H9XVQ4; H9XVQ5; Q4AB01; Q5LJP1; Q8IM88; Q8IM89; Q8MT21; Q9Y135;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Calcium-dependent secretion activator;
DE AltName: Full=Calcium-activated protein for secretion;
GN Name=Cadps {ECO:0000312|FlyBase:FBgn0053653};
GN Synonyms=Caps {ECO:0000312|FlyBase:FBgn0053653};
GN ORFNames=CG33653 {ECO:0000312|FlyBase:FBgn0053653};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11516399; DOI=10.1016/s0896-6273(01)00382-8;
RA Renden R., Berwin B., Davis W., Ann K., Chin C.-T., Kreber R., Ganetzky B.,
RA Martin T.F.J., Broadie K.;
RT "Drosophila CAPS is an essential gene that regulates dense-core vesicle
RT release and synaptic vesicle fusion.";
RL Neuron 31:421-437(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 464-1447 (ISOFORM 3).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1447 (ISOFORM 2).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles
CC filled with neurotransmitters and neuropeptides. May specifically
CC mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles
CC (DCVs) and other dense-core vesicles. However, it probably also
CC participates in small clear synaptic vesicles (SVs) exocytosis and it
CC is unclear whether its function is related to Ca(2+) triggering.
CC {ECO:0000269|PubMed:11516399}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11516399}. Synapse {ECO:0000269|PubMed:11516399}.
CC Note=Membrane-associated to vesicles. Restricted to all classes of
CC presynaptic termini independent of the ratio of vesicular content
CC (dense core vesicles versus synaptic vesicles). Found in all identified
CC classes of peripheral and central synapses. In the CNS, it is highly
CC enriched in the synapse-dense neuropil, which lacks cell bodies.
CC Present in all synapses in the neuropil where it precisely colocalizes
CC with other pansynaptic markers. Similarly abundant in all classes of
CC neuromuscular junction (NMJ) termini, including type I, II, and III
CC NMJs, where it localizes to all 3 bouton types. Expressed at similar
CC levels in boutons which contain primarily small clear glutamatergic
CC vesicles, as well as boutons very highly enriched in large DCVs. It
CC appears that neither bouton class contains a pure population of either
CC SVs or DCVs, but only differs dramatically in the relative abundance of
CC the vesicular classes. Thus, the level of expression does not correlate
CC with the abundance of DCVs. Clearly present presynaptically and
CC colocalizes exclusively with presynaptic markers.
CC {ECO:0000269|PubMed:11516399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q9NHE5-1; Sequence=Displayed;
CC Name=2; Synonyms=D;
CC IsoId=Q9NHE5-2; Sequence=VSP_047915, VSP_047917;
CC Name=3; Synonyms=C;
CC IsoId=Q9NHE5-3; Sequence=VSP_047912, VSP_047915, VSP_047917,
CC VSP_047918, VSP_047920;
CC Name=4; Synonyms=B;
CC IsoId=Q9NHE5-4; Sequence=VSP_047914;
CC Name=5; Synonyms=A;
CC IsoId=Q9NHE5-5; Sequence=VSP_047913, VSP_047915, VSP_047917;
CC Name=6; Synonyms=E;
CC IsoId=Q9NHE5-6; Sequence=VSP_047915, VSP_047916, VSP_047917,
CC VSP_047919;
CC Name=7; Synonyms=F;
CC IsoId=Q9NHE5-7; Sequence=VSP_047915, VSP_047919;
CC -!- TISSUE SPECIFICITY: Restricted to the nervous system at all stages of
CC development and highly localized at synapses (at protein level).
CC {ECO:0000269|PubMed:11516399}.
CC -!- DEVELOPMENTAL STAGE: Not detected in early embryos through stage 8.
CC Strongly expressed in neural-specific cells at the onset of early
CC stages of neuronal differentiation beginning at stage 9-10. Accumulates
CC from stage 12 through the rest of embryogenesis in all neuronal cells
CC within the brain and ventral nerve cord (VNC). Remains restricted to
CC the central nervous system and not detected in other tissues at any
CC stage of development. {ECO:0000269|PubMed:11516399}.
CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds
CC phospholipids. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Flies display locomotory deficits and complete
CC embryonic lethality. The mutant NMJ reveals a 50% loss in evoked
CC glutamatergic transmission, and an accumulation of synaptic vesicles at
CC active zones. They also display a 3-fold accumulation of DCVs in
CC synaptic terminals. {ECO:0000269|PubMed:11516399}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38612.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=AAF34697.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM48456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF223578; AAF34697.1; ALT_FRAME; mRNA.
DR EMBL; AE014135; AAN06590.4; -; Genomic_DNA.
DR EMBL; AE014135; AAN06591.4; -; Genomic_DNA.
DR EMBL; AE014135; AAZ52485.2; -; Genomic_DNA.
DR EMBL; AE014135; AFH06799.1; -; Genomic_DNA.
DR EMBL; AE014135; AFH06800.1; -; Genomic_DNA.
DR EMBL; AY118427; AAM48456.1; ALT_INIT; mRNA.
DR EMBL; AF145637; AAD38612.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001027029.2; NM_001031858.2. [Q9NHE5-7]
DR RefSeq; NP_001027030.1; NM_001031859.2. [Q9NHE5-4]
DR RefSeq; NP_001027031.1; NM_001031860.2. [Q9NHE5-5]
DR RefSeq; NP_001245439.1; NM_001258510.2. [Q9NHE5-2]
DR RefSeq; NP_001245440.1; NM_001258511.2. [Q9NHE5-6]
DR AlphaFoldDB; Q9NHE5; -.
DR SMR; Q9NHE5; -.
DR BioGRID; 72491; 1.
DR STRING; 7227.FBpp0298334; -.
DR PaxDb; Q9NHE5; -.
DR PRIDE; Q9NHE5; -.
DR EnsemblMetazoa; FBtr0091630; FBpp0088329; FBgn0053653. [Q9NHE5-5]
DR EnsemblMetazoa; FBtr0091631; FBpp0088330; FBgn0053653. [Q9NHE5-4]
DR EnsemblMetazoa; FBtr0307333; FBpp0298334; FBgn0053653. [Q9NHE5-2]
DR EnsemblMetazoa; FBtr0307334; FBpp0298335; FBgn0053653. [Q9NHE5-6]
DR EnsemblMetazoa; FBtr0333702; FBpp0305855; FBgn0053653. [Q9NHE5-7]
DR GeneID; 49968; -.
DR KEGG; dme:Dmel_CG33653; -.
DR CTD; 8618; -.
DR FlyBase; FBgn0053653; Cadps.
DR VEuPathDB; VectorBase:FBgn0053653; -.
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00590000083094; -.
DR InParanoid; Q9NHE5; -.
DR OMA; RWEIKGN; -.
DR BioGRID-ORCS; 49968; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Cadps; fly.
DR GenomeRNAi; 49968; -.
DR PRO; PR:Q9NHE5; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0053653; Expressed in brain and 27 other tissues.
DR ExpressionAtlas; Q9NHE5; baseline and differential.
DR Genevisible; Q9NHE5; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; NAS:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:FlyBase.
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 Alternative splicing; Calcium; Cytoplasmic vesicle; Exocytosis;
KW Lipid-binding; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..1447
FT /note="Calcium-dependent secretion activator"
FT /id="PRO_0000053872"
FT DOMAIN 417..547
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 573..683
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 970..1157
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1386..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..463
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_047912"
FT VAR_SEQ 430..435
FT /note="STPSFL -> R (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047913"
FT VAR_SEQ 477..478
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047914"
FT VAR_SEQ 477
FT /note="V -> VKGLKSLAPNRIVYCTMEV (in isoform 2, isoform 3,
FT isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10731138,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_047915"
FT VAR_SEQ 705
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_047916"
FT VAR_SEQ 948
FT /note="E -> ELRKHDKMDKKKLLKEDEDVSGGHNESEVDLIDSTGLISASELATAA
FT STDGSSFRYCMPTHAVYTPPVPT (in isoform 2, isoform 3, isoform 5
FT and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10731138,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_047917"
FT VAR_SEQ 1001..1053
FT /note="DNLRNGRFHQHLRDTFAPLVVRYVDLMESSIAQSIHKGFEKERWESKGINAA
FT L -> APTQAPLSATTTGAIPTARSTSGWVRVHQGTAPLTPSKTNPEVLFSKPTRIAP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_047918"
FT VAR_SEQ 1049..1104
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_047919"
FT VAR_SEQ 1054..1447
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_047920"
FT CONFLICT 33
FT /note="S -> N (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> Q (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="R -> S (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..171
FT /note="IQLY -> NSTL (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="T -> K (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="I -> N (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="M -> V (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
FT CONFLICT 1354..1358
FT /note="AYQAV -> DIRQ (in Ref. 1; AAF34697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1447 AA; 163110 MW; 406B95DC0ECEE996 CRC64;
MIDPSSSEEE GEDDAVPNVS SKGRLTNTTK GTSAVSIIGG SAGSVVGSNI PVSGSNTDLI
GNQRQSNISS ICNRNDVGNI SVAALGSTSN KIEQICGNRA DTGNLEVPSN GIPSGISQET
LNQSVGSSRA NSLPRPLSPS PSLTSEKHET AEPHGKHERE EEERKRRIQL YVFISRCISY
PFNAKQPTDM TKRQTKISKQ QLEIITQRFQ AFLKGETQIM ADEAFQNAVQ SYHDVFLKSE
RVLKMVQSGA SSQHDFREVF RNNIEKRVRS LPEIDGLSKE TVLTSWMAKF DIILKGTGEE
DSKRPSRMQQ SLNSELILSK EQLYDMFQQI LLVKKFEHQI LFNALMLDSA DEQAAAIRRE
LDGRMQRVGE MEKNRKLMPK FVLKEMESLY VEELKSSINL LMANLESLPV SKGNMDSKYG
LQKLKRYNHS TPSFLKLILR SHGSLSKLEG DSEDGSTQLT KLDVVLTFQL EVIVMEVENG
EKLQTDQAEA SKPMWDTQGD FTTTHPLPVV KVKLYTENPG MLALEDKELG KVTLKPTPLS
SKSPEWHRMI VPKNLPDQDI RIKIACRLDK PLNMKHCGYL YAIGKSVWKK WKRRYFVLVQ
VSQYTFAMCS YKEKKSEPSE MMQLDGYTVD YIEAASANLM FGIDLNGGRY FFNAVREGDS
ISFACDDENE CSLWVMAMYR ATGQSHKPTP PITQDKNSAM SKIQGDADKA RKHGMEDFIS
TDPCTFDHAT LFKTLQNLTL EYRLNDPYAS LGWFSPGQVF VLDEYCARYG VRGCYRHLCY
LSDLLDRAEK QHMIDPTLIH YSFAFCASHV HGNRPDGVGS ITHEEKEKFS EIKERLRQLL
EFQITNFRYC FPFGRPEGAL KATLSLLERV LMKDIVTPVP PEEVRQMIKK SLETAALVNY
TRLSNKAKID EDLRGDVIVP APKKLEDLIH LAELCVDLLQ QNEEHYGEAF AWFSDLLVEH
AEIFWSLFAV DMDRVLSEQA PDTWDSFPLF QILNDYLRTD DNLRNGRFHQ HLRDTFAPLV
VRYVDLMESS IAQSIHKGFE KERWESKGIN AALNPAALNN AAQALNTAAL NPSMILCGKK
DQVNFYVPKL PKQSNSTAAN DEMRNGCATS EDLFWKLDAL QSFIRDLHWP DAEFRQHLEQ
RLKMMAVDMI EQCIQRTDSS FQSWLKKNIA FISTDYILPS EMCAMVNVIL DAKNQSFKLT
TIDGIDLYKF HAKIDDQIDK ANVAMTQGLS GKLMSVLEST LSKLARYDEG SLIGSILSFT
NVSSSGKDLG QGYVNFFRNN MDQVRGKIAD DLWTLHFFEQ WYSQQINMLC NWLSERVDHA
LHYAQVASIS HIIKKIYSDF ELQGVLEDKL NSKAYQAVAQ RMATEEATCA LTMPDACEDE
PCDEIREGEE EDNGDESTSN IPRGLPKPKV AAAQAAAVTN VVAGRVGNLL GKGIGGLSSK
LGSGSWF
