CAPS1_MOUSE
ID CAPS1_MOUSE Reviewed; 1355 AA.
AC Q80TJ1; E9QN90; Q3TSP2; Q61374; Q6AXB4; Q6PGF0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 149.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Namikawa K., Su Q.N., Toki H., Kiyama H.;
RT "Down-regulation of CAPS (Ca(2+)-dependent activator for secretion) during
RT nerve regeneration.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 693-1355.
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1355 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14530279; DOI=10.1074/jbc.m304727200;
RA Speidel D., Varoqueaux F., Enk C., Nojiri M., Grishanin R.N.,
RA Martin T.F.J., Hofmann K., Brose N., Reim K.;
RT "A family of Ca2+-dependent activator proteins for secretion: comparative
RT analysis of structure, expression, localization, and function.";
RL J. Biol. Chem. 278:52802-52809(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15820695; DOI=10.1016/j.neuron.2005.02.019;
RA Speidel D., Bruederle C.E., Enk C., Voets T., Varoqueaux F., Reim K.,
RA Becherer U., Fornai F., Ruggieri S., Holighaus Y., Weihe E., Bruns D.,
RA Brose N., Rettig J.;
RT "CAPS1 regulates catecholamine loading of large dense-core vesicles.";
RL Neuron 46:75-88(2005).
RN [8]
RP REVIEW.
RX PubMed=15820687; DOI=10.1016/j.neuron.2005.03.017;
RA Suedhof T.C.;
RT "CAPS in search of a lost function.";
RL Neuron 46:2-4(2005).
RN [9]
RP INTERACTION WITH RASL10B, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=17984325; DOI=10.1083/jcb.200707101;
RA Rybkin I.I., Kim M.S., Bezprozvannaya S., Qi X., Richardson J.A.,
RA Plato C.F., Hill J.A., Bassel-Duby R., Olson E.N.;
RT "Regulation of atrial natriuretic peptide secretion by a novel Ras-like
RT protein.";
RL J. Cell Biol. 179:527-537(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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, ECO:0000269|PubMed:15820695}.
CC -!- SUBUNIT: Homodimer. Interacts with the dopamine receptor DRD2 (By
CC similarity). Interacts with RASL10B. {ECO:0000250,
CC ECO:0000269|PubMed:17984325}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:14530279}.
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:0000269|PubMed:14530279, ECO:0000269|PubMed:15820695}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80TJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TJ1-2; Sequence=VSP_016809, VSP_016811, VSP_016813;
CC Name=4;
CC IsoId=Q80TJ1-4; Sequence=VSP_016814;
CC -!- TISSUE SPECIFICITY: Present in brain and adrenal glands (at protein
CC level). Specifically expressed in neural and endocrine secretory
CC tissues. Strongly expressed in almost all nerve cells of the brain,
CC although it is absent from glial cells. Expressed in the cardiac atria,
CC but not ventricles. {ECO:0000269|PubMed:14530279,
CC ECO:0000269|PubMed:15820695, ECO:0000269|PubMed:17984325}.
CC -!- DEVELOPMENTAL STAGE: During brain development, its expression is
CC similar to that of synaptic markers. Expression is first detectable
CC late in embryogenesis (14 dpc) and increases to reach a plateau about
CC 20 days after birth, when most synapses have been formed (at protein
CC level).
CC -!- INDUCTION: In the heart, up-regulated by hypertrophic stimuli.
CC {ECO:0000269|PubMed:17984325}.
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 -!- DISRUPTION PHENOTYPE: Mice die within 30 minutes after birth but do not
CC display obvious developmental or biochemical abnormalities. They show a
CC strong reduction in the frequency of amperometrically detectable
CC release events of transmitter-filled vesicles, while the total number
CC of fusing vesicles, as judged by capacitance recordings or total
CC internal reflection microscopy, remains unchanged.
CC {ECO:0000269|PubMed:15820695}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13044.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown due to a duplication of 90 bp after position 107.; Evidence={ECO:0000305};
CC Sequence=BAC65735.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86214; BAA13044.1; ALT_SEQ; mRNA.
DR EMBL; AK122453; BAC65735.1; ALT_INIT; mRNA.
DR EMBL; AC116395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK161919; BAE36633.1; -; mRNA.
DR EMBL; BC057065; AAH57065.1; -; mRNA.
DR CCDS; CCDS36806.1; -. [Q80TJ1-2]
DR CCDS; CCDS36807.1; -. [Q80TJ1-1]
DR RefSeq; NP_001036082.1; NM_001042617.1. [Q80TJ1-1]
DR RefSeq; NP_036191.2; NM_012061.3. [Q80TJ1-2]
DR RefSeq; XP_006518098.1; XM_006518035.3.
DR AlphaFoldDB; Q80TJ1; -.
DR SMR; Q80TJ1; -.
DR BioGRID; 205117; 5.
DR IntAct; Q80TJ1; 4.
DR MINT; Q80TJ1; -.
DR STRING; 10090.ENSMUSP00000064706; -.
DR iPTMnet; Q80TJ1; -.
DR PhosphoSitePlus; Q80TJ1; -.
DR SwissPalm; Q80TJ1; -.
DR MaxQB; Q80TJ1; -.
DR PaxDb; Q80TJ1; -.
DR PeptideAtlas; Q80TJ1; -.
DR PRIDE; Q80TJ1; -.
DR ProteomicsDB; 265528; -. [Q80TJ1-1]
DR ProteomicsDB; 265529; -. [Q80TJ1-2]
DR ProteomicsDB; 265530; -. [Q80TJ1-4]
DR DNASU; 27062; -.
DR Ensembl; ENSMUST00000067491; ENSMUSP00000064706; ENSMUSG00000054423. [Q80TJ1-2]
DR Ensembl; ENSMUST00000112658; ENSMUSP00000108277; ENSMUSG00000054423. [Q80TJ1-1]
DR GeneID; 27062; -.
DR KEGG; mmu:27062; -.
DR UCSC; uc007sfu.1; mouse. [Q80TJ1-1]
DR UCSC; uc007sfv.1; mouse. [Q80TJ1-2]
DR CTD; 8618; -.
DR MGI; MGI:1350922; Cadps.
DR VEuPathDB; HostDB:ENSMUSG00000054423; -.
DR eggNOG; KOG3543; Eukaryota.
DR GeneTree; ENSGT00590000083094; -.
DR HOGENOM; CLU_007068_0_0_1; -.
DR InParanoid; Q80TJ1; -.
DR OMA; RWEIKGN; -.
DR OrthoDB; 138870at2759; -.
DR TreeFam; TF312963; -.
DR BioGRID-ORCS; 27062; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cadps; mouse.
DR PRO; PR:Q80TJ1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80TJ1; protein.
DR Bgee; ENSMUSG00000054423; Expressed in pontine nuclear group and 171 other tissues.
DR ExpressionAtlas; Q80TJ1; baseline and differential.
DR Genevisible; Q80TJ1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0031045; C:dense core granule; ISO:MGI.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0050432; P:catecholamine secretion; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IDA:SynGO.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR GO; GO:0016050; P:vesicle organization; IMP:MGI.
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; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..1355
FT /note="Calcium-dependent secretion activator 1"
FT /id="PRO_0000053865"
FT DOMAIN 378..493
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 519..622
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 933..1113
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..1131
FT /note="Interaction with DRD2"
FT /evidence="ECO:0000250"
FT REGION 1179..1355
FT /note="Mediates targeting and association with DCVs"
FT /evidence="ECO:0000250"
FT REGION 1331..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62717"
FT VAR_SEQ 654..658
FT /note="SGLKD -> Y (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016809"
FT VAR_SEQ 863..869
FT /note="ENQKDAE -> GKKREMYEHPVFCLASQVMDLTIQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016811"
FT VAR_SEQ 904..910
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016813"
FT VAR_SEQ 905..910
FT /note="PHVDKG -> GK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016814"
FT CONFLICT 19
FT /note="R -> S (in Ref. 1; BAA13044 and 2; BAC65735)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> W (in Ref. 2; BAC65735)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="D -> V (in Ref. 4; BAE36633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="P -> S (in Ref. 4; BAE36633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="E -> G (in Ref. 4; BAE36633)"
FT /evidence="ECO:0000305"
FT CONFLICT 1354
FT /note="D -> E (in Ref. 1; BAA13044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1355 AA; 153113 MW; 59596BAD74C6AE56 CRC64;
MLDPSSSEEE SDEILEEERG KDVLGSAASG ARLSPSRTSE GSAGSAGMGG SGAGAGVGAG
GGGGSGASSG GGAGGLQPSS RAGGGRPSSP SPSVVSEKEK EELERLQKEE EERKKRLQLY
VFVMRCIAYP FNAKQPTDMA RRQQKISKQQ LQTVKDRFQA FLNGETQIVA DEAFMNAVQS
YYEVFLKSDR VARMVQSGGC SANDSREVFK KHIEKRVRSL PEIDGLSKET VLSSWMAKFD
AIYRGEEDPR KQQARMTASA ASELILSKEQ LYEMFQNILG IKKFEHQLLY NACQLDNPDE
QAAQIRRELD GRLQMADQIA RERKFPKFVS KEMENMYIEE LKSSVNLLMA NLESMPVSKG
GEFKLQKLKR SHNASIIDMG EESENQLSKS DVLLSFSLEV VIMEVQGLKS LAPNRIVYCT
MEVEGGEKLQ TDQAEASKPT WGTQGDFSTT HALPAVKVKL FTESTGVLAL EDKELGRVIL
HPTPNSPKQS EWHKMTVSKN CPDQDLKIKL AVRMDKPQNM KHSGYLWTIG KNVWKRWKKR
FFVLVQVSQY TFAMCSYREK KAEPQELLQL DGYTVDYTDP QPGLEGGRAF FNAVKEGDTV
IFASDDEQDR ILWVQAMYRA TGQSHKPVPP TQVQKLNAKG GNVPQLDAPI SQFSGLKDAD
RAQKHGMDEF ISSNPCNFDH ASLFEMVQRL TLDHRLNDSY SCLGWFSPGQ VFVLDEYCAR
NGVRGCHRHL CYLRDLLERA ENGAMIDPTL LHYSFAFCAS HVHGNRPDGI GTVTVEEKER
FEEIKERLRV LLENQITHFR YCFPFGRPEG ALKATLSLLE RVLMKDIVTP VPQEEVKTVI
RKCLEQAALV NYSRLSEYAK IEENQKDAEN VGRLITPAKK LEDTIRLAEL VIEVLQQNEE
HHAEPHVDKG EAFAWWSDLM VEHAETFLSL FAVDMDAALE VQPPDTWDSF PLFQLLNDFL
RTDYNLCNGK FHKHLQDLFA PLVVRYVDLM ESSIAQSIHR GFERESWEPV KSLTSNLPNV
NLPNVNLPKV PNLPVNIPLG IPQMPTFSAP SWMAAIYDAD NGSGTSEDLF WKLDALQTFI
RDLHWPEEEF GKHLEQRLKL MASDMIESCV KRTRIAFEVK LQKTSRSTDF RVPQSICTMF
NVMVDAKAQS TKLCSMEMGQ EHQYHSKIDE LIEETVKEMI TLLVAKFVTI LEGVLAKLSR
YDEGTLFSSF LSFTVKAASK YVDVPKPGMD VADAYVTFVR HSQDVLRDKV NEEMYIERLF
DQWYNSSMNI ICTWLTDRMD LQLHIYQLKT LIRMVKKTYR DFRLQGVLDS TLNSKTYETI
RNRLTVEEAT ASVSEGGGLQ GISMKDSDEE DEEDD
