UN13C_MOUSE
ID UN13C_MOUSE Reviewed; 2210 AA.
AC Q8K0T7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein unc-13 homolog C;
DE AltName: Full=Munc13-3;
GN Name=Unc13c;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-30.
RC TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 700-1430.
RC TISSUE=Eye;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11150314; DOI=10.1523/jneurosci.21-01-00010.2001;
RA Augustin I., Korte S., Rickmann M., Kretzschmar H.A., Sudhof T.C.,
RA Herms J.W., Brose N.;
RT "The cerebellum-specific Munc13 isoform Munc13-3 regulates cerebellar
RT synaptic transmission and motor learning in mice.";
RL J. Neurosci. 21:10-17(2001).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1023, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May play a role in vesicle maturation during exocytosis as a
CC target of the diacylglycerol second messenger pathway. May be involved
CC in the regulation of synaptic transmission at parallel fiber - Purkinje
CC cell synapses. {ECO:0000269|PubMed:11150314}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with STX1A and/or STX1B1, VAMP2 and SNAP25.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Presynaptic cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Localized to presynaptic structures. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Restricted to cerebellum, predominantly in the
CC granule cell layer. Almost exclusively present in the molecular layer
CC in which the parallel fiber axons of granule cells terminate on
CC dendrites of Purkinje neurons (at protein level).
CC {ECO:0000269|PubMed:11150314}.
CC -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice showed no obvious physical or
CC behavioral abnormalities. Some deficiency in motor learning can be
CC observed, compared to wild type, in a motor performance and learning
CC test on a rotating rod, but only at high rotation speed.
CC {ECO:0000269|PubMed:11150314}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30416.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N- terminal and C-terminal parts.; Evidence={ECO:0000305};
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DR EMBL; AC112267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK005367; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC030416; AAH30416.1; ALT_SEQ; mRNA.
DR CCDS; CCDS40690.1; -.
DR RefSeq; NP_001074622.1; NM_001081153.1.
DR RefSeq; XP_006510996.1; XM_006510933.3.
DR AlphaFoldDB; Q8K0T7; -.
DR SMR; Q8K0T7; -.
DR BioGRID; 229022; 1.
DR STRING; 10090.ENSMUSP00000139027; -.
DR iPTMnet; Q8K0T7; -.
DR PhosphoSitePlus; Q8K0T7; -.
DR jPOST; Q8K0T7; -.
DR MaxQB; Q8K0T7; -.
DR PaxDb; Q8K0T7; -.
DR PeptideAtlas; Q8K0T7; -.
DR PRIDE; Q8K0T7; -.
DR ProteomicsDB; 298196; -.
DR Antibodypedia; 51911; 32 antibodies from 10 providers.
DR DNASU; 208898; -.
DR Ensembl; ENSMUST00000075245; ENSMUSP00000074726; ENSMUSG00000062151.
DR Ensembl; ENSMUST00000184666; ENSMUSP00000139027; ENSMUSG00000062151.
DR GeneID; 208898; -.
DR KEGG; mmu:208898; -.
DR UCSC; uc033jlk.1; mouse.
DR CTD; 440279; -.
DR MGI; MGI:2149021; Unc13c.
DR VEuPathDB; HostDB:ENSMUSG00000062151; -.
DR eggNOG; KOG1011; Eukaryota.
DR GeneTree; ENSGT00940000155174; -.
DR HOGENOM; CLU_001304_0_0_1; -.
DR InParanoid; Q8K0T7; -.
DR OMA; QEYDHLS; -.
DR OrthoDB; 117172at2759; -.
DR PhylomeDB; Q8K0T7; -.
DR TreeFam; TF312844; -.
DR BioGRID-ORCS; 208898; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Unc13c; mouse.
DR PRO; PR:Q8K0T7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K0T7; protein.
DR Bgee; ENSMUSG00000062151; Expressed in globus pallidus and 147 other tissues.
DR Genevisible; Q8K0T7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IMP:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098793; C:presynapse; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0001566; F:non-kinase phorbol ester receptor activity; TAS:MGI.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IBA:GO_Central.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR InterPro; IPR027087; Unc13C.
DR PANTHER; PTHR10480; PTHR10480; 3.
DR PANTHER; PTHR10480:SF2; PTHR10480:SF2; 3.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Exocytosis; Membrane; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..2210
FT /note="Protein unc-13 homolog C"
FT /id="PRO_0000188579"
FT DOMAIN 1199..1323
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1633..1776
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 1882..2024
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 2038..2165
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 1093..1143
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 28..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 967..991
FT /evidence="ECO:0000255"
FT COMPBIAS 28..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 1023
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 2210 AA; 249844 MW; ED6A02639FC6FA3F CRC64;
MVASLFKSLI LAYIHKLCKG MFTKKLGNTT KKKENRQQKK DQDFPTAGHT KPPKLSNALK
STVKKIAKCS STRNFSIEDE EGHKDFSLSP TFSYRVAIAN GLQTAVTNSD EDLLQELSSI
ESSYSESFNE LRSSTENQVQ STHTMPVRRN RKSSSSLAPS EGSSDGERTL HTLKLGALRK
LRKWKKSQEC VSSDSELSTV KKTWGIRSKS LDRTARNPKT NVLEPGFSSS GCISQTHDVM
EMIFKELQGI SQIETELSEL RGHVNALKYS IDEISSSVEV VQSEIEQLRT GFVQARRETR
DIHDYIKHLG HMGSKVSLRF LNVPEERHEY VESVVYQILI DKMGFSDVPN AIKIEFAQRI
GQQRDCPNAK PRPILVYFET PQQRDSVLKK SYKLKGTGIG ISTDILTYDI RERKEKGVLP
SSQTYESMDM KLSTPEPKAK KNAWLSPNDS DRELESDLSR SSYADSPAKG SSSKSSSKSH
SARSKNKAAN SRTSQKSDYN KRPSQPPASS TPEKQTPHYV EATPPLWHSQ SDFFTLKLSR
SESDFSKLCQ SYSEDFSESQ FFCRTNGSSL LSSSDRELWQ RKQEGMPALY HRLQDQGLDE
TIPAVPGQAE IENTETVDSG MSNSMVCASG DRSNYSGSQL SLHEDLSPWK EWNQAGQGTD
DVGLDSSTQE PFDYDTNSLS DQQLDLSSKD LDDLGKCHSD LQDDSESYDL TQDDNSSPCP
GLDNEPQGQW VGQYDSYQEA NSNDLYPNQS HPSMMYRSQS ELQSDDSEGA QPKSWHSRLS
IDLSDKTFKF PKFGSTLQRA KSALEVVWNK STQSLSGCED SGSSLMGRFR TLSQSTANES
STTLDSDIYT EPYYYKAEEE EDYCEPVADS ETDYVEVMEQ VLAKLENRTS ITEVNEHIKD
YDHPSYETPY ETPQDEGYDG QADDIISEGE LETLNEPAVE MELAEDENQN LPAESLEVMK
PKRIRPSFKE AALRAYKKQM AELEEKILAG DSSSMDEKAR IVSGNDLDAS KFSALQVFGG
AGRGLYGIDS MPDLRRKKTL PIVRDVAMTL AARKSGLSLA MVIRTSLNNE ELKMHVFRKT
LQALIYPISS TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ GMKCLECGVK CHEKCQDLLN
ADCLQRAAEK SSKHGAEDKT QTIITAMKER MKIRERNRPE VFEVIQEMFQ ISKEDFVQYT
KAAKQSVLDG TSKWSAKITI TVVSAQGLQA KDKTGSSDPY VTVQVGKNKR RTKTIFGNLN
PVWDEKFFFE CHNSTDRIKV RVWDEDDDIK SRVKQHFKKE SDDFLGQTIV EVRTLSGEMD
VWYNLEKRTD KSAVSGAIRL KINVEIKGEE KVAPYHIQYT CLHENLFHYL TEVKSNGSVK
IPEVKGDEAW KVFFDDASQE IVDEFAMRYG VESIYQAMTH FSCLSSKYMC PGVPAVMSAL
LANINAFYAH TTVSTNVQVS ASDRFAATNF GREKFIKLLD QLHNSLRIDL SKYRENFPAS
NSERLQDLKS TVDLLTSITF FRMKVLELQS PPKASAVVKD CVRACLDSTY KYIFDNCHEL
YSQLIDPSKK QDVPREDQGP TTKNLDFWPQ LITLMVTIID EDKTAYTPVL NQFPQELNMG
KISAEIMWSL FALDMKYALE EHEKQRLCKS TDYMNLHFKV KWFYNEYVRE LPAFKDAVPE
YSLWFEPFVM QWLDENEDVS MEFLHGALGR DKKDGFQQTS DHALFSCSVV DVFAQLNQSF
EIIKKLECPN PEALSHLMRR FAKTINKVLV QYAAIVSNDF SSYCDKETVP CILMNNIQQL
RVQLEKMFES MGGKELDPEA STILKELQIK LNGVLDALSI TYGESFQLTI EECIKQMGAE
LNQMRANGNS TANKNSAAMD AEIVLRPLMD FLDKTLSLSA KICEKTVLKR VLKELWKLVL
NKIEKQIVLP PLTDQTGPQM IFIAAKDLGQ LSKLKEHMIR EDAKGLTPRQ CAIVEVVLAT
IKQYFHAGGN GLKKNFLEKS PDLHSLRYAL SLYTQTTDAL IKKFIETQGS QSRSSKDAVG
QISVHVDVTT TPGTGDHKVT VKVIAINDLN WQTTAMFRPF VEVCMLGPSL GDKKRKQGTK
TKSNTWSPKY NETFQFILGN ENRPGAYELH LSVKDYCFAR EDRIIGMTVI QLQNIAEKGS
YGAWYPLLKN LSMDETGLTI LRILSQRTSD DVAKEFVRLK SETRSIEESA
