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Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog)

 KMT2C_MOUSE             Reviewed;        4903 AA.
Q8BRH4; Q5YLV9; Q8BK12; Q8C6M3; Q923H5; Q923H6;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
10-OCT-2003, sequence version 2.
22-NOV-2017, entry version 149.
RecName: Full=Histone-lysine N-methyltransferase 2C;
Short=Lysine N-methyltransferase 2C;
EC=2.1.1.43;
AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog;
Name=Kmt2c; Synonyms=Mll3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=16459028; DOI=10.1016/j.gene.2005.11.013;
Brun M.-E., Gasca S., Girard C., Bouton K., De Massy B., De Sario A.;
"Characterization and expression analysis during embryo development of
the mouse ortholog of MLL3.";
Gene 371:25-33(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-814 AND 4803-4903.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 957-1376 AND 4214-4894.
TISSUE=Myeloma;
PubMed=11718452;
Tan Y.C., Chow V.T.;
"Novel human HALR (MLL3) gene encodes a protein homologous to ALR and
to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated
with leukemia and developmental defects.";
Cancer Detect. Prev. 25:454-469(2001).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2824, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1761; LYS-2005; LYS-2796 AND
LYS-2862, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-2447; ARG-2563 AND ARG-4132,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
H3. H3 'Lys-4' methylation represents a specific tag for
epigenetic transcriptional activation. Central component of the
MLL2/3 complex, a coactivator complex of nuclear receptors,
involved in transcriptional coactivation. KMT2C/MLL3 may be a
catalytic subunit of this complex (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Component of the MLL2/3 complex (also named ASCOM
complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L,
RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and
alpha- and beta-tubulin. Interacts with histone H3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BRH4-1; Sequence=Displayed;
Name=2;
IsoId=Q8BRH4-2; Sequence=VSP_020568, VSP_020569, VSP_020570,
VSP_020571, VSP_020572;
-!- TISSUE SPECIFICITY: In adult, detected in testis, kidney, spleen
and lung, weakly expressed in brain and absent in heart and liver.
First detected throughout the embryo at 8 dpc when expression is
strong in forebrain neuroepithelium and absent in heart. Expressed
in the eye lens between 10 and 14.5 dpc. By 13 dpc, expressed
strongly in spinal cord, hand/foot plates and gonads.
{ECO:0000269|PubMed:16459028}.
-!- DOMAIN: The SET domain interacts with histone H3 but not H2A, H2B
and H4, and may have a H3 lysine specific methylation activity.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAN11291.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY138582; AAN11291.1; ALT_INIT; mRNA.
EMBL; AC116469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC134910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK044828; BAC32109.1; -; mRNA.
EMBL; AK054270; BAC35712.2; -; mRNA.
EMBL; AK077567; BAC36867.1; -; mRNA.
EMBL; AY036886; AAK70213.1; -; mRNA.
EMBL; AY036887; AAK70214.1; -; mRNA.
UniGene; Mm.332268; -.
ProteinModelPortal; Q8BRH4; -.
SMR; Q8BRH4; -.
DIP; DIP-61282N; -.
IntAct; Q8BRH4; 6.
STRING; 10090.ENSMUSP00000043874; -.
iPTMnet; Q8BRH4; -.
PhosphoSitePlus; Q8BRH4; -.
PaxDb; Q8BRH4; -.
PRIDE; Q8BRH4; -.
MGI; MGI:2444959; Kmt2c.
eggNOG; KOG4443; Eukaryota.
eggNOG; COG2940; LUCA.
HOGENOM; HOG000113602; -.
HOVERGEN; HBG045586; -.
InParanoid; Q8BRH4; -.
PhylomeDB; Q8BRH4; -.
PRO; PR:Q8BRH4; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MLL3; -.
GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007338; P:single fertilization; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 3.30.40.10; -; 6.
InterPro; IPR034732; EPHD.
InterPro; IPR003889; FYrich_C.
InterPro; IPR003888; FYrich_N.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF05965; FYRC; 1.
Pfam; PF05964; FYRN; 1.
Pfam; PF00628; PHD; 2.
Pfam; PF00856; SET; 1.
SMART; SM00542; FYRC; 1.
SMART; SM00541; FYRN; 1.
SMART; SM00398; HMG; 1.
SMART; SM00249; PHD; 8.
SMART; SM00508; PostSET; 1.
SMART; SM00184; RING; 4.
SMART; SM00317; SET; 1.
SUPFAM; SSF47095; SSF47095; 1.
SUPFAM; SSF57903; SSF57903; 6.
PROSITE; PS50216; DHHC; 1.
PROSITE; PS51805; EPHD; 2.
PROSITE; PS51543; FYRC; 1.
PROSITE; PS51542; FYRN; 1.
PROSITE; PS00354; HMGI_Y; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 5.
PROSITE; PS50016; ZF_PHD_2; 6.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Acyltransferase; Alternative splicing;
Chromatin regulator; Coiled coil; Complete proteome; DNA-binding;
Lipoprotein; Metal-binding; Methylation; Methyltransferase; Nucleus;
Palmitate; Phosphoprotein; Reference proteome; Repeat;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Zinc; Zinc-finger.
CHAIN 1 4903 Histone-lysine N-methyltransferase 2C.
/FTId=PRO_0000124880.
DOMAIN 435 488 DHHC. {ECO:0000255|PROSITE-
ProRule:PRU00067}.
DOMAIN 4537 4597 FYR N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00875}.
DOMAIN 4598 4683 FYR C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00876}.
DOMAIN 4763 4879 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 4887 4903 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DNA_BIND 34 46 A.T hook.
ZN_FING 226 261 C2HC pre-PHD-type 1; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU01146}.
ZN_FING 282 330 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
ZN_FING 340 390 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 343 388 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 387 437 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 463 519 PHD-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 950 1003 PHD-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1000 1050 PHD-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1077 1132 PHD-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 4391 4431 C2HC pre-PHD-type 2.
{ECO:0000255|PROSITE-ProRule:PRU01146}.
ZN_FING 4452 4499 PHD-type 8. {ECO:0000255|PROSITE-
ProRule:PRU01146}.
REGION 4840 4841 S-adenosyl-L-methionine binding.
{ECO:0000250}.
COILED 1330 1352 {ECO:0000255}.
COILED 1743 1790 {ECO:0000255}.
COILED 3047 3074 {ECO:0000255}.
COILED 3166 3193 {ECO:0000255}.
COILED 3224 3270 {ECO:0000255}.
COILED 3387 3432 {ECO:0000255}.
COMPBIAS 384 487 Cys-rich.
COMPBIAS 970 1099 Cys-rich.
COMPBIAS 1519 1568 Pro-rich.
COMPBIAS 1708 1787 Gln-rich.
COMPBIAS 1831 2622 Pro-rich.
COMPBIAS 2682 2780 Asp-rich.
COMPBIAS 3022 3504 Gln-rich.
METAL 4843 4843 Zinc. {ECO:0000250}.
METAL 4891 4891 Zinc. {ECO:0000250}.
METAL 4893 4893 Zinc. {ECO:0000250}.
METAL 4898 4898 Zinc. {ECO:0000250}.
BINDING 4817 4817 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 751 751 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 847 847 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 1294 1294 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 1497 1497 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 1761 1761 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1983 1983 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 2005 2005 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2447 2447 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2563 2563 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2796 2796 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2803 2803 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 2822 2822 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 2824 2824 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2826 2826 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 2862 2862 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 3709 3709 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 4027 4027 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
MOD_RES 4132 4132 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 4260 4260 Phosphoserine.
{ECO:0000250|UniProtKB:Q8NEZ4}.
VAR_SEQ 839 878 Missing (in isoform 2).
{ECO:0000303|PubMed:16459028}.
/FTId=VSP_020568.
VAR_SEQ 1414 1448 Missing (in isoform 2).
{ECO:0000303|PubMed:16459028}.
/FTId=VSP_020569.
VAR_SEQ 1791 3080 Missing (in isoform 2).
{ECO:0000303|PubMed:16459028}.
/FTId=VSP_020570.
VAR_SEQ 3814 3884 Missing (in isoform 2).
{ECO:0000303|PubMed:16459028}.
/FTId=VSP_020571.
VAR_SEQ 4714 4717 Missing (in isoform 2).
{ECO:0000303|PubMed:16459028}.
/FTId=VSP_020572.
CONFLICT 28 36 SPAAADKRP -> RSFVCGCGA (in Ref. 1;
AAN11291). {ECO:0000305}.
CONFLICT 276 276 V -> A (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 433 440 NCRICIEC -> VSDFLICF (in Ref. 3;
BAC32109). {ECO:0000305}.
CONFLICT 533 533 E -> G (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 577 577 D -> DA (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 675 675 S -> C (in Ref. 3; BAC35712).
{ECO:0000305}.
CONFLICT 720 720 K -> E (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 763 763 F -> L (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 791 791 H -> Y (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 1324 1325 VD -> LH (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 1737 1737 E -> V (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 1776 1776 Q -> R (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 3236 3236 M -> MM (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 3423 3424 QR -> P (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 3657 3657 E -> G (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 3668 3668 A -> V (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 4283 4283 C -> Y (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 4306 4306 E -> D (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 4520 4520 Q -> R (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 4531 4531 V -> G (in Ref. 1; AAN11291).
{ECO:0000305}.
CONFLICT 4649 4649 Y -> H (in Ref. 1; AAN11291).
{ECO:0000305}.
SEQUENCE 4903 AA; 540187 MW; 0B896490B081BA6C CRC64;
MSSEEDRSAE QQQPPPAPPE EPGAPAPSPA AADKRPRGRP RKDGASPFQR ARKKPRSRGK
STVEDEDSMD GLETTETENI VETEIKEQSV EEDAETEVDS SKQPVSALQR SVSEESANSL
VSVGVEAKIS EQLCAFCYCG EKSSLGQGDL KQFRVTPGLT LPWKDQPSNK DIDDNSSGTC
EKIQNYAPRK QRGQRKERPP QQSAVSCVSV STQTACEDQA GKLWDELSLV GLPDAIDVQA
LFDSTGTCWA HHRCVEWSLG ICQMEEPLLV NVDKAVVSGS TERCAFCKHL GATIKCCEEK
CTQMYHYPCA AGAGTFQDFS HFFLLCPEHI DQAPERSKED ANCAVCDSPG DLLDQFFCTT
CGQHYHGMCL DIAVTPLKRA GWQCPECKVC QNCKQSGEDS KMLVCDTCDK GYHTFCLQPV
MKSVPTNGWK CKNCRICIEC GTRSSTQWHH NCLICDTCYQ QQDNLCPFCG KCYHPELQKD
MLHCNMCKRW VHLECDKPTD QELDSQLKED YICMYCKHLG AEIDPLHPGN EVEMPELPTD
YASGMEIEGT EDEVVFLEQT VNKDVSDHQC RPGIVPDVQV YTEEPQKSNP LESPDTVGLI
TSESSDNKMN PDLANEIAHE VDTEKTEMLS KGRHVCEEDQ NEDRMEVTEN IEVLPHQTIV
PQEDLLLSED SEVASKELSP PKSAPETAAP EALLSPHSER SLSCKEPLLT ERVQEEMEQK
ENSEFSTGCV DFEMTLAVDS CDKDSSCQGD KYVELPAEEE STFSSATDLN KADVSSSSTL
CSDLPSCDML HGYPPAFNSA AGSIMPTTYI SVTPKIGMGK PAITKRKFSP GRPRSKQGAW
SNHNTVSPPS WAPDTSEGRE IFKPRQLSGS AIWSIKVGRG SGFPGKRRPR GAGLSGRGGR
GRSKLKSGIG AVVLPGVSAA DISSNKDEEE NSMHNTVVLF SSSDKFTLQQ DMCVVCGSFG
QGAEGRLLAC SQCGQCYHPY CVSIKITKVV LSKGWRCLEC TVCEACGKAT DPGRLLLCDD
CDISYHTYCL DPPLQTVPKG GWKCKWCVWC RHCGATSAGL RCEWQNNYTQ CAPCASLSSC
PVCCRNYREE DLILQCRQCD RWMHAVCQNL NTEEEVENVA DIGFDCSMCR PYMPVSNVPS
SDCCDSSLVA QIVTKVKELD PPKTYTQDGV CLTESGMSQL QSLTVTAPRR KRTKPKLKLK
IINQNSVAVL QTPPDIQSEH SRDGEMDDSR EGELMDCDGK SESSPEREAG DDETKGIEGT
DAIKKRKRKP YRPGIGGFMV RQRSRTGQGK AKRSVVRKDS SGSISEQLPS RDDGWREQLP
DTLVDEPVSV AENTDKIKKR YRKRKNKLEE TFPAYLQEAF FGKDLLDTSR QNKLSVDNLS
EDAAQLSFKT GFLDPSSDPL LSSSSTSAKP GTQGTADDPL ADISEVLNTD DDILGIISDD
LAKSVDHSDI GPTTADASSL PQPGVSQSSR PLTEEQLDGI LSPELDKMVT DGAILGKLYK
IPELGGKDVE DLFTAVLSPA TTQPAPLPQP PPPPQLLPMH NQDVFSRMPL MNGLIGPSPH
LPHNSLPPGS GLGTFPAIAQ SPYTDVRDKS PAFNAIASDP NSSWAPTTPS MEGENDTLSN
AQRSTLKWEK EEALGEMATV APVLYTNINF PNLKEEFPDW TTRVKQIAKL WRKASSQERA
PYVQKARDNR AALRINKVQM SNDSMKRQQQ QDSIDPSSRI DSDLFKDPLK QRESEHEQEW
KFRQQMRQKS KQQAKIEATQ KLEQVKNEQQ QQQQQQQQQQ QQQLASQHLL VAPGSDTPSS
GAQSPLTPQA GNGNVSPAQT FHKDLFSKHL PGTPASTPSD GVFVKPQPPP PPSTPSRIPV
QESLSQSQNS QPPSPQMFSP GSSHSRPPSP VDPYAKMVGT PRPPPGGHSF PRRNSVTPVE
NCVPLSSVPR PIHMNETSAT RPSPARDLCA SSMTNSDPYA KPPDTPRPMM TDQFSKPFSL
PRSPVISEQS TKGPLTTGTS DHFTKPSPRT DAFQRQRLPD PYAGPSLTPA PLGNGPFKTP
LHPPPSQDPY GSVSQTSRRL SVDPYERPAL TPRPVDNFSH SQSNDPYSHP PLTPHPAMTE
SFTHASRAFP QPGTISRSAS QDPYSQPPGT PRPLIDSYSQ TSGTARSNPD PYSQPPGTPR
PNTIDPYSQQ PPTPRPSPQT DMFVSSVANQ RHTDPYTHHL GPPRPGISVP YSQPPAVPRP
RTSEGFTRPS SARPALMPNQ DPFLQAAQNR VPGLPGPLIR PPDTCSQTPR PPGPGRIDTF
THASSSAVRD PYDQPPVTPR PHSESFGTSQ VVHDLVDRPV PGSEGNFSTS SNLPVSSQGQ
QFSSVSQLPG PVPTSGGTDT QNTVNMSQAD TEKLRQRQKL REIILQQQQQ KKIASRQEKG
PQDTAVVPHP VPLPHWQPES INQAFTRPPP PYPGSTRSPV IPPLGPRYAV FPKDQRGPYP
PEVAGMGMRP HGFRFGFPGA GHGPMPSQDR FHVPQQIQGS GIPPHIRRPM SMEMPRPSNN
PPLNNPVGLP QHFPPQGLPV QQHNILGQAF IELRHRAPDG RSRLPFAASP SSVIESPSHP
RHGNFLPRPD FPGPRHTDPI RQPSQCLSNQ LPVHPNLEQV PPSQQEQGHP AHQSSIVMRP
LNHPLSGEFS EAPLSTSTPA ETSPDNLEIA GQSSAGLEEK LDSDDPSVKE LDVKDLEGVE
VKDLDDEDLE NLNLDTEDGK GDDLDTLDNL ETNDPNLDDL LRSGEFDIIA YTDPELDLGD
KKSMFNEELD LNVPIDDKLD NQCASVEPKT RDQGDKTMVL EDKDLPQRKS SVSSEIKTEA
LSPYSKEEIQ SEIKNHDDSR GDADTACSQA ASAQTNHSDR GKTALLTTDQ DMLEKRCNQE
NAGPVVSAIQ GSTPLPARDV MNSCDITGST PVLSSLLSNE KCDDSDIRPS GSSPPSLPIS
PSTHGSSLPP TLIVPPSPLL DNTVNSNVTV VPRINHAFSQ GVPVNPGFIQ GQSSVNHNLG
TGKPTNQTVP LTNQSSTMSG PQQLMIPQTL AQQNRERPLL LEEQPLLLQD LLDQERQEQQ
QQRQMQAMIR QRSEPFFPNI DFDAITDPIM KAKMVALKGI NKVMAQNSLG MPPMVMSRFP
FMGPSVAGTQ NNDGQTLVPQ AVAQDGSITH QISRPNPPNF GPGFVNDSQR KQYEEWLQET
QQLLQMQQKY LEEQIGAHRK SKKALSAKQR TAKKAGREFP EEDAEQLKHV TEQQSMVQKQ
LEQIRKQQKE HAELIEDYRI KQQQQQQQCA LAPPILMPGV QPQPPLVPGA TSLTMSQPNF
PMVPQQLQHQ QHTAVISGHT SPARMPSLPG WQSNSASAHL PLNPPRIQPP IAQLSLKTCT
PAPGTVSSAN PQNGPPPRVE FDDNNPFSES FQERERKERL REQQERQRVQ LMQEVDRQRA
LQQRMEMEQH CLMGAELANR TPVSQMPFYG SDRPCDFLQP PRPLQQSPQH QQQIGPVLQQ
QNVQQGSVNS PPNQTFMQTN EQRQVGPPSF VPDSPSASGG SPNFHSVKPG HGNLPGSSFQ
QSPLRPPFTP ILPGTSPVAN SNVPCGQDPA VTQGQNYSGS SQSLIQLYSD IIPEEKGKKK
RTRKKKKDDD AESGKAPSTP HSDCAAPLTP GLSETTSTPA VSSPSELPQQ RQQEPVEPVP
VPTPNVSAGQ PCIESENKLP NSEFIKETSN QQTHVNAEAD KPSVETPNKT EEIKLEKAET
QPSQEDTKVE EKTGNKIKDI VAGPVSSIQC PSHPVGTPTT KGDTGNELLK HLLKNKKASS
LLTQKPEGTL SSDESSTKDG KLIEKQSPAE GLQTLGAQMQ GGFGGGNSQL PKTDGASENK
KQRSKRTQRT GEKAAPRSKK RKKDEEEKQA MYSSSDSFTH LKQQNNLSNP PTPPASLPPT
PPPMACQKMA NGFATTEELA GKAGVLVSHE VARALGPKPF QLPFRPQDDL LARAIAQGPK
TVDVPASLPT PPHNNHEELR IQDHYGDRDT PDSFVPSSSP ESVVGVEVNK YPDLSLVKEE
PPEPVPSPII PILPSISGKN SESRRNDIKT EPGTLFFTSP FGSSPNGPRS GLISVAITLH
PTAAENISSV VAAFSDLLHV RIPNSYEVSN APDVPPMGLV SSHRVNPSLE YRQHLLLRGP
PPGSANPPRL ATSYRLKQPN VPFPPTSNGL SGYKDSSHGP AEGASLRPQW CCHCKVVILG
SGVRKSCKDL TFVNKGSREN TKRMEKDIVF CSNNCFILYS SAAQAKNSDN KESLPSLPQS
PMKEPSKAFH QYSNNISTLD VHCLPQFQEK VSPPASPPIS FPPAFEAAKV ESKPDELKVT
VKLKPRLRTV PVGLEDCRPL NKKWRGMKWK KWSIHIVIPK GTFKPPCEDE IDEFLKKLGT
CLKPDPVPKD CRKCCFCHEE GDGLTDGPAR LLNLDLDLWV HLNCALWSTE VYETQAGALI
NVELALRRGL QMKCVFCHKT GATSGCHRFR CTNIYHFTCA TKAQCMFFKD KTMLCPMHKP
KGIHEQQLSY FAVFRRVYVQ RDEVRQIASI VQRGERDHTF RVGSLIFHTI GQLLPQQMQA
FHSPKALFPV GYEASRLYWS TRYANRRCRY LCSIEEKDGR PVFVIRIVEQ GHEDLVLSDS
SPKDVWDKIL EPVACVRKKS EMLQLFPAYL KGEDLFGLTV SAVARIAESL PGVEACENYT
FRYGRNPLME LPLAVNPTGC ARSEPKMSAH VKRFVLRPHT LNSTSTSKSF QSTVTGELNA
PYSKQFVHSK SSQYRRMKTE WKSNVYLARS RIQGLGLYAA RDIEKHTMVI EYIGTIIRNE
VANRKEKLYE SQNRGVYMFR MDNDHVIDAT LTGGPARYIN HSCAPNCVAE VVTFERGHKI
IISSNRRIQK GEELCYDYKF DFEDDQHKIP CHCGAVNCRK WMN


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