UN13C_HUMAN
ID UN13C_HUMAN Reviewed; 2214 AA.
AC Q8NB66; Q0P613; Q8ND48; Q96NP3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein unc-13 homolog C;
DE AltName: Full=Munc13-3;
GN Name=UNC13C;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1025-1925 AND 2019-2214.
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1580-2214.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2036-2214.
RC 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 [5]
RP VARIANTS GLU-304 AND ALA-2196.
RX PubMed=22365152; DOI=10.1016/j.ajhg.2012.01.006;
RA Veeramah K.R., O'Brien J.E., Meisler M.H., Cheng X., Dib-Hajj S.D.,
RA Waxman S.G., Talwar D., Girirajan S., Eichler E.E., Restifo L.L.,
RA Erickson R.P., Hammer M.F.;
RT "de novo pathogenic SCN8A mutation identified by whole-genome sequencing of
RT a family quartet affected by infantile epileptic encephalopathy and
RT SUDEP.";
RL Am. J. Hum. Genet. 90:502-510(2012).
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 (By similarity). {ECO:0000250}.
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: Exclusively expressed in brain.
CC -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB70836.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03675.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03675.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AC010867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK054981; BAB70836.1; ALT_INIT; mRNA.
DR EMBL; AK091491; BAC03675.1; ALT_INIT; mRNA.
DR EMBL; AL834407; CAD39069.2; -; mRNA.
DR EMBL; BC040740; AAH40740.1; ALT_INIT; mRNA.
DR CCDS; CCDS45264.1; -.
DR RefSeq; NP_001074003.1; NM_001080534.2.
DR RefSeq; XP_005254451.1; XM_005254394.4.
DR RefSeq; XP_016877709.1; XM_017022220.1.
DR RefSeq; XP_016877710.1; XM_017022221.1.
DR RefSeq; XP_016877711.1; XM_017022222.1.
DR AlphaFoldDB; Q8NB66; -.
DR SMR; Q8NB66; -.
DR BioGRID; 136430; 4.
DR IntAct; Q8NB66; 3.
DR STRING; 9606.ENSP00000260323; -.
DR iPTMnet; Q8NB66; -.
DR PhosphoSitePlus; Q8NB66; -.
DR BioMuta; UNC13C; -.
DR DMDM; 148887448; -.
DR EPD; Q8NB66; -.
DR jPOST; Q8NB66; -.
DR MassIVE; Q8NB66; -.
DR PaxDb; Q8NB66; -.
DR PeptideAtlas; Q8NB66; -.
DR PRIDE; Q8NB66; -.
DR ProteomicsDB; 72744; -.
DR Antibodypedia; 51911; 32 antibodies from 10 providers.
DR Ensembl; ENST00000260323.16; ENSP00000260323.11; ENSG00000137766.18.
DR GeneID; 440279; -.
DR KEGG; hsa:440279; -.
DR MANE-Select; ENST00000260323.16; ENSP00000260323.11; NM_001080534.3; NP_001074003.1.
DR UCSC; uc002acm.4; human.
DR CTD; 440279; -.
DR DisGeNET; 440279; -.
DR GeneCards; UNC13C; -.
DR HGNC; HGNC:23149; UNC13C.
DR HPA; ENSG00000137766; Tissue enriched (brain).
DR MIM; 614568; gene.
DR neXtProt; NX_Q8NB66; -.
DR OpenTargets; ENSG00000137766; -.
DR PharmGKB; PA134870087; -.
DR VEuPathDB; HostDB:ENSG00000137766; -.
DR eggNOG; KOG1011; Eukaryota.
DR GeneTree; ENSGT00940000155174; -.
DR HOGENOM; CLU_001304_0_0_1; -.
DR InParanoid; Q8NB66; -.
DR OMA; QEYDHLS; -.
DR OrthoDB; 117172at2759; -.
DR PhylomeDB; Q8NB66; -.
DR TreeFam; TF312844; -.
DR PathwayCommons; Q8NB66; -.
DR SignaLink; Q8NB66; -.
DR BioGRID-ORCS; 440279; 5 hits in 1064 CRISPR screens.
DR ChiTaRS; UNC13C; human.
DR GenomeRNAi; 440279; -.
DR Pharos; Q8NB66; Tdark.
DR PRO; PR:Q8NB66; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8NB66; protein.
DR Bgee; ENSG00000137766; Expressed in secondary oocyte and 120 other tissues.
DR ExpressionAtlas; Q8NB66; baseline and differential.
DR Genevisible; Q8NB66; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048786; C:presynaptic active zone; TAS: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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IEA:Ensembl.
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:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Exocytosis; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..2214
FT /note="Protein unc-13 homolog C"
FT /id="PRO_0000188578"
FT DOMAIN 1203..1327
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1637..1780
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 1886..2028
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 2044..2169
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 1097..1147
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..135
FT /evidence="ECO:0000255"
FT COILED 971..995
FT /evidence="ECO:0000255"
FT COMPBIAS 128..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1307
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 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62770"
FT VARIANT 304
FT /note="D -> E (rare variant; may act as a phenotype
FT modifier in EIEE13 patients carrying SCN8A mutations;
FT dbSNP:rs149448818)"
FT /evidence="ECO:0000269|PubMed:22365152"
FT /id="VAR_067540"
FT VARIANT 609
FT /note="G -> S (in dbSNP:rs12437941)"
FT /id="VAR_061873"
FT VARIANT 942
FT /note="S -> L (in dbSNP:rs17731958)"
FT /id="VAR_052468"
FT VARIANT 2196
FT /note="V -> A (rare variant; may act as a phenotype
FT modifier in EIEE13 patients carrying SCN8A mutations;
FT dbSNP:rs146433220)"
FT /evidence="ECO:0000269|PubMed:22365152"
FT /id="VAR_067541"
FT CONFLICT 2036
FT /note="S -> C (in Ref. 4; AAH40740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2214 AA; 250911 MW; C8287DAD9DF99B7D CRC64;
MVANFFKSLI LPYIHKLCKG MFTKKLGNTN KNKEYRQQKK DQDFPTAGQT KSPKFSYTFK
STVKKIAKCS STHNLSTEED EASKEFSLSP TFSYRVAIAN GLQKNAKVTN SDNEDLLQEL
SSIESSYSES LNELRSSTEN QAQSTHTMPV RRNRKSSSSL APSEGSSDGE RTLHGLKLGA
LRKLRKWKKS QECVSSDSEL STMKKSWGIR SKSLDRTVRN PKTNALEPGF SSSGCISQTH
DVMEMIFKEL QGISQIETEL SELRGHVNAL KHSIDEISSS VEVVQSEIEQ LRTGFVQSRR
ETRDIHDYIK HLGHMGSKAS LRFLNVTEER FEYVESVVYQ ILIDKMGFSD APNAIKIEFA
QRIGHQRDCP NAKPRPILVY FETPQQRDSV LKKSYKLKGT GIGISTDILT HDIRERKEKG
IPSSQTYESM AIKLSTPEPK IKKNNWQSPD DSDEDLESDL NRNSYAVLSK SELLTKGSTS
KPSSKSHSAR SKNKTANSSR ISNKSDYDKI SSQLPESDIL EKQTTTHYAD ATPLWHSQSD
FFTAKLSRSE SDFSKLCQSY SEDFSENQFF TRTNGSSLLS SSDRELWQRK QEGTATLYDS
PKDQHLNGGV QGIQGQTETE NTETVDSGMS NGMVCASGDR SHYSDSQLSL HEDLSPWKEW
NQGADLGLDS STQEGFDYET NSLFDQQLDV YNKDLEYLGK CHSDLQDDSE SYDLTQDDNS
SPCPGLDNEP QGQWVGQYDS YQGANSNELY QNQNQLSMMY RSQSELQSDD SEDAPPKSWH
SRLSIDLSDK TFSFPKFGST LQRAKSALEV VWNKSTQSLS GYEDSGSSLM GRFRTLSQST
ANESSTTLDS DVYTEPYYYK AEDEEDYTEP VADNETDYVE VMEQVLAKLE NRTSITETDE
QMQAYDHLSY ETPYETPQDE GYDGPADDMV SEEGLEPLNE TSAEMEIRED ENQNIPEQPV
EITKPKRIRP SFKEAALRAY KKQMAELEEK ILAGDSSSVD EKARIVSGND LDASKFSALQ
VCGGAGGGLY GIDSMPDLRR KKTLPIVRDV AMTLAARKSG LSLAMVIRTS LNNEELKMHV
FKKTLQALIY PMSSTIPHNF EVWTATTPTY CYECEGLLWG IARQGMKCLE CGVKCHEKCQ
DLLNADCLQR AAEKSSKHGA EDKTQTIITA MKERMKIREK NRPEVFEVIQ EMFQISKEDF
VQFTKAAKQS VLDGTSKWSA KITITVVSAQ GLQAKDKTGS SDPYVTVQVG KNKRRTKTIF
GNLNPVWDEK FYFECHNSTD RIKVRVWDED DDIKSRVKQH FKKESDDFLG QTIVEVRTLS
GEMDVWYNLE KRTDKSAVSG AIRLKINVEI KGEEKVAPYH IQYTCLHENL FHYLTEVKSN
GGVKIPEVKG DEAWKVFFDD ASQEIVDEFA MRYGIESIYQ AMTHFSCLSS KYMCPGVPAV
MSTLLANINA FYAHTTVSTN IQVSASDRFA ATNFGREKFI KLLDQLHNSL RIDLSKYREN
FPASNTERLQ DLKSTVDLLT SITFFRMKVL ELQSPPKASM VVKDCVRACL DSTYKYIFDN
CHELYSQLTD PSKKQDIPRE DQGPTTKNLD FWPQLITLMV TIIDEDKTAY TPVLNQFPQE
LNMGKISAEI MWTLFALDMK YALEEHENQR LCKSTDYMNL HFKVKWFYNE YVRELPAFKD
AVPEYSLWFE PFVMQWLDEN EDVSMEFLHG ALGRDKKDGF QQTSEHALFS CSVVDVFAQL
NQSFEIIKKL ECPNPEALSH LMRRFAKTIN KVLLQYAAIV SSDFSSHCDK ENVPCILMNN
IQQLRVQLEK MFESMGGKEL DSEASTILKE LQVKLSGVLD ELSVTYGESF QVIIEECIKQ
MSFELNQMRA NGNTTSNKNS AAMDAEIVLR SLMDFLDKTL SLSAKICEKT VLKRVLKELW
KLVLNKIEKQ IVLPPLTDQT GPQMIFIAAK DLGQLSKLKE HMIREDARGL TPRQCAIMEV
VLATIKQYFH AGGNGLKKNF LEKSPDLQSL RYALSLYTQT TDALIKKFID TQTSQSRSSK
DAVGQISVHV DITATPGTGD HKVTVKVIAI NDLNWQTTAM FRPFVEVCIL GPNLGDKKRK
QGTKTKSNTW SPKYNETFQF ILGKENRPGA YELHLSVKDY CFAREDRIIG MTVIQLQNIA
EKGSYGAWYP LLKNISMDET GLTILRILSQ RTSDDVAKEF VRLKSETRST EESA
