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Unconventional myosin-Va (Dilute myosin heavy chain, non-muscle)

 MYO5A_MOUSE             Reviewed;        1853 AA.
Q99104; E9PUE5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
31-JAN-2018, entry version 169.
RecName: Full=Unconventional myosin-Va;
AltName: Full=Dilute myosin heavy chain, non-muscle;
Name=Myo5a; Synonyms=Dilute;
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].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=1996138; DOI=10.1038/349709a0;
Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A.;
"Novel myosin heavy chain encoded by murine dilute coat colour
locus.";
Nature 349:709-712(1991).
[2]
ERRATUM, AND SEQUENCE REVISION.
Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A.;
Nature 352:547-547(1991).
[3]
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).
[4]
INTERACTION WITH FMR1.
PubMed=12147688; DOI=10.1074/jbc.M203608200;
Ohashi S., Koike K., Omori A., Ichinose S., Ohara S., Kobayashi S.,
Sato T.A., Anzai K.;
"Identification of mRNA/protein (mRNP) complexes containing Puralpha,
mStaufen, fragile X protein, and myosin Va and their association with
rough endoplasmic reticulum equipped with a kinesin motor.";
J. Biol. Chem. 277:37804-37810(2002).
[5]
INTERACTION WITH MYRIP.
PubMed=12221080; DOI=10.1074/jbc.M203862200;
Fukuda M., Kuroda T.S.;
"Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c),
a novel linker protein that interacts with Rab27, myosin Va/VIIa, and
actin.";
J. Biol. Chem. 277:43096-43103(2002).
[6]
INTERACTION WITH MLPH.
PubMed=11887186; DOI=10.1038/ncb760;
Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E.,
Copeland N.G., Jenkins N.A., Hammer J.A. III;
"Identification of an organelle receptor for myosin-Va.";
Nat. Cell Biol. 4:271-278(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-1450 AND
SER-1650, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, 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).
[11]
FUNCTION IN VESICULAR TRANSPORT, AND INTERACTION WITH RAB10.
PubMed=22908308; DOI=10.1083/jcb.201111091;
Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S.,
Hammer J.A., Xu T., Lippincott-Schwartz J.;
"Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle
translocation in adipocytes.";
J. Cell Biol. 198:545-560(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 763-820 IN COMPLEX WITH CALM,
AND SUBUNIT.
PubMed=17151196; DOI=10.1073/pnas.0609436103;
Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M.,
Cohen C.;
"Crystal structure of apo-calmodulin bound to the first two IQ motifs
of myosin V reveals essential recognition features.";
Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1469-1853 OF APOPROTEIN AND
IN COMPLEX WITH RIPL2 AND MLPH, INTERACTION WITH SYTL4; RIPL2 AND
MLPH, AND MUTAGENESIS OF ARG-1528; ILE-1535 AND LYS-1539.
PubMed=23798443; DOI=10.1073/pnas.1306768110;
Wei Z., Liu X., Yu C., Zhang M.;
"Structural basis of cargo recognitions for class V myosins.";
Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013).
-!- FUNCTION: Processive actin-based motor that can move in large
steps approximating the 36-nm pseudo-repeat of the actin filament.
Involved in melanosome transport. Also mediates the transport of
vesicles to the plasma membrane. May also be required for some
polarization process involved in dendrite formation.
{ECO:0000269|PubMed:22908308}.
-!- SUBUNIT: May be a homodimer, which associates with multiple
calmodulin or myosin light chains (PubMed:17151196). Interacts
with RIPL2, the interaction is required for its role in dendrite
formation (PubMed:23798443). Interacts with MLPH
(PubMed:11887186). Interacts with SYTL4 (PubMed:23798443).
Interacts with MYRIP (PubMed:12221080). Interacts with RAB10;
mediates the transport to the plasma membrane of SLC2A4/GLUT4
storage vesicles (PubMed:22908308). Interacts with FMR1; this
interaction occurs in association with polyribosome
(PubMed:12147688). {ECO:0000269|PubMed:11887186,
ECO:0000269|PubMed:12147688, ECO:0000269|PubMed:12221080,
ECO:0000269|PubMed:17151196, ECO:0000269|PubMed:22908308,
ECO:0000269|PubMed:23798443}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-400199, EBI-400199;
-!- TISSUE SPECIFICITY: Detected in melanocytes.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
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EMBL; X57377; CAA40651.1; -; mRNA.
EMBL; AC133947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CT033761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS52860.1; -.
PIR; A46761; A46761.
RefSeq; NP_034994.2; NM_010864.2.
UniGene; Mm.3645; -.
PDB; 2IX7; X-ray; 2.50 A; C=763-820.
PDB; 3WB8; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1469-1853.
PDB; 4KP3; X-ray; 2.40 A; A/B=1469-1853.
PDB; 4ZLK; X-ray; 2.50 A; A=1-791.
PDBsum; 2IX7; -.
PDBsum; 3WB8; -.
PDBsum; 4KP3; -.
PDBsum; 4ZLK; -.
ProteinModelPortal; Q99104; -.
SMR; Q99104; -.
BioGrid; 201666; 22.
CORUM; Q99104; -.
DIP; DIP-29542N; -.
IntAct; Q99104; 14.
MINT; MINT-243234; -.
STRING; 10090.ENSMUSP00000116028; -.
iPTMnet; Q99104; -.
PhosphoSitePlus; Q99104; -.
SwissPalm; Q99104; -.
EPD; Q99104; -.
MaxQB; Q99104; -.
PaxDb; Q99104; -.
PeptideAtlas; Q99104; -.
PRIDE; Q99104; -.
Ensembl; ENSMUST00000123128; ENSMUSP00000116028; ENSMUSG00000034593.
GeneID; 17918; -.
KEGG; mmu:17918; -.
UCSC; uc009qrr.1; mouse.
CTD; 4644; -.
MGI; MGI:105976; Myo5a.
eggNOG; KOG0160; Eukaryota.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00900000140810; -.
HOGENOM; HOG000171839; -.
HOVERGEN; HBG052556; -.
InParanoid; Q99104; -.
KO; K10357; -.
TreeFam; TF328771; -.
ChiTaRS; Myo5a; mouse.
EvolutionaryTrace; Q99104; -.
PRO; PR:Q99104; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000034593; -.
CleanEx; MM_MYO5A; -.
ExpressionAtlas; Q99104; baseline and differential.
Genevisible; Q99104; MM.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0042641; C:actomyosin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0032433; C:filopodium tip; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0016459; C:myosin complex; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0016461; C:unconventional myosin complex; IMP:CAFA.
GO; GO:0003779; F:actin binding; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0005516; F:calmodulin binding; IDA:MGI.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
GO; GO:0003774; F:motor activity; IDA:MGI.
GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0051643; P:endoplasmic reticulum localization; IMP:MGI.
GO; GO:0099089; P:establishment of endoplasmic reticulum localization to postsynapse; IMP:SynGO.
GO; GO:0006887; P:exocytosis; IMP:MGI.
GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
GO; GO:0030073; P:insulin secretion; IMP:MGI.
GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
GO; GO:0006582; P:melanin metabolic process; IMP:MGI.
GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
GO; GO:0032400; P:melanosome localization; IMP:MGI.
GO; GO:0032402; P:melanosome transport; IDA:MGI.
GO; GO:0042552; P:myelination; IMP:MGI.
GO; GO:0042476; P:odontogenesis; IDA:MGI.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IMP:MGI.
GO; GO:0032252; P:secretory granule localization; IMP:MGI.
GO; GO:0050808; P:synapse organization; IMP:MGI.
GO; GO:0030050; P:vesicle transport along actin filament; ISO:MGI.
GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IMP:MGI.
CDD; cd01380; MYSc_Myo5; 1.
InterPro; IPR002710; Dilute_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR036103; MYSc_Myo5.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01843; DIL; 1.
Pfam; PF00612; IQ; 6.
Pfam; PF00063; Myosin_head; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM01132; DIL; 1.
SMART; SM00015; IQ; 6.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51126; DILUTE; 1.
PROSITE; PS50096; IQ; 6.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51844; SH3_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; ATP-binding;
Calmodulin-binding; Coiled coil; Complete proteome; Motor protein;
Myosin; Nucleotide-binding; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9Y4I1}.
CHAIN 2 1853 Unconventional myosin-Va.
/FTId=PRO_0000123457.
DOMAIN 8 60 Myosin N-terminal SH3-like.
{ECO:0000255|PROSITE-ProRule:PRU01190}.
DOMAIN 69 763 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 766 788 IQ 1. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 789 813 IQ 2. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 814 836 IQ 3. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 837 861 IQ 4. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 862 884 IQ 5. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 885 913 IQ 6. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1532 1808 Dilute. {ECO:0000255|PROSITE-
ProRule:PRU00503}.
NP_BIND 163 170 ATP. {ECO:0000255}.
REGION 643 665 Actin-binding. {ECO:0000255}.
COILED 914 1237 {ECO:0000255}.
COILED 1314 1443 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9Y4I1}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1032 1032 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QYF3}.
MOD_RES 1450 1450 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1650 1650 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1758 1758 Phosphothreonine. {ECO:0000255}.
MUTAGEN 1528 1528 R->H: Slightly reduces affinity for MLPH.
{ECO:0000269|PubMed:23798443}.
MUTAGEN 1535 1535 I->E: Strongly reduces affinity for MLPH
and SYTL4. {ECO:0000269|PubMed:23798443}.
MUTAGEN 1539 1539 K->E: Strongly reduces affinity for MLPH
and SYTL4. {ECO:0000269|PubMed:23798443}.
CONFLICT 695 695 A -> R (in Ref. 1; CAA40651).
{ECO:0000305}.
CONFLICT 904 905 EL -> DV (in Ref. 1; CAA40651).
{ECO:0000305}.
STRAND 12 17 {ECO:0000244|PDB:4ZLK}.
TURN 18 20 {ECO:0000244|PDB:4ZLK}.
STRAND 21 29 {ECO:0000244|PDB:4ZLK}.
STRAND 36 41 {ECO:0000244|PDB:4ZLK}.
STRAND 47 51 {ECO:0000244|PDB:4ZLK}.
TURN 66 70 {ECO:0000244|PDB:4ZLK}.
HELIX 74 76 {ECO:0000244|PDB:4ZLK}.
HELIX 82 94 {ECO:0000244|PDB:4ZLK}.
STRAND 100 103 {ECO:0000244|PDB:4ZLK}.
STRAND 106 110 {ECO:0000244|PDB:4ZLK}.
HELIX 121 127 {ECO:0000244|PDB:4ZLK}.
TURN 132 134 {ECO:0000244|PDB:4ZLK}.
HELIX 139 153 {ECO:0000244|PDB:4ZLK}.
STRAND 157 164 {ECO:0000244|PDB:4ZLK}.
HELIX 169 183 {ECO:0000244|PDB:4ZLK}.
HELIX 192 207 {ECO:0000244|PDB:4ZLK}.
STRAND 215 218 {ECO:0000244|PDB:4ZLK}.
STRAND 220 228 {ECO:0000244|PDB:4ZLK}.
STRAND 234 242 {ECO:0000244|PDB:4ZLK}.
HELIX 246 249 {ECO:0000244|PDB:4ZLK}.
HELIX 260 266 {ECO:0000244|PDB:4ZLK}.
TURN 267 270 {ECO:0000244|PDB:4ZLK}.
HELIX 272 277 {ECO:0000244|PDB:4ZLK}.
HELIX 282 284 {ECO:0000244|PDB:4ZLK}.
HELIX 286 289 {ECO:0000244|PDB:4ZLK}.
HELIX 301 314 {ECO:0000244|PDB:4ZLK}.
HELIX 319 335 {ECO:0000244|PDB:4ZLK}.
STRAND 344 346 {ECO:0000244|PDB:4ZLK}.
HELIX 355 363 {ECO:0000244|PDB:4ZLK}.
HELIX 368 376 {ECO:0000244|PDB:4ZLK}.
STRAND 377 380 {ECO:0000244|PDB:4ZLK}.
STRAND 387 390 {ECO:0000244|PDB:4ZLK}.
HELIX 393 421 {ECO:0000244|PDB:4ZLK}.
STRAND 431 438 {ECO:0000244|PDB:4ZLK}.
STRAND 445 447 {ECO:0000244|PDB:4ZLK}.
HELIX 449 479 {ECO:0000244|PDB:4ZLK}.
HELIX 493 500 {ECO:0000244|PDB:4ZLK}.
HELIX 505 513 {ECO:0000244|PDB:4ZLK}.
HELIX 520 531 {ECO:0000244|PDB:4ZLK}.
TURN 532 534 {ECO:0000244|PDB:4ZLK}.
STRAND 545 551 {ECO:0000244|PDB:4ZLK}.
STRAND 553 560 {ECO:0000244|PDB:4ZLK}.
HELIX 564 568 {ECO:0000244|PDB:4ZLK}.
HELIX 574 581 {ECO:0000244|PDB:4ZLK}.
HELIX 587 591 {ECO:0000244|PDB:4ZLK}.
HELIX 635 651 {ECO:0000244|PDB:4ZLK}.
STRAND 653 661 {ECO:0000244|PDB:4ZLK}.
HELIX 674 683 {ECO:0000244|PDB:4ZLK}.
HELIX 686 693 {ECO:0000244|PDB:4ZLK}.
STRAND 699 702 {ECO:0000244|PDB:4ZLK}.
HELIX 703 710 {ECO:0000244|PDB:4ZLK}.
HELIX 711 713 {ECO:0000244|PDB:4ZLK}.
STRAND 716 718 {ECO:0000244|PDB:4ZLK}.
HELIX 723 734 {ECO:0000244|PDB:4ZLK}.
HELIX 738 740 {ECO:0000244|PDB:4ZLK}.
STRAND 741 743 {ECO:0000244|PDB:4ZLK}.
STRAND 745 750 {ECO:0000244|PDB:4ZLK}.
HELIX 765 818 {ECO:0000244|PDB:2IX7}.
STRAND 1473 1476 {ECO:0000244|PDB:4KP3}.
HELIX 1479 1481 {ECO:0000244|PDB:4KP3}.
HELIX 1482 1489 {ECO:0000244|PDB:4KP3}.
HELIX 1498 1502 {ECO:0000244|PDB:4KP3}.
HELIX 1506 1520 {ECO:0000244|PDB:4KP3}.
HELIX 1524 1544 {ECO:0000244|PDB:4KP3}.
HELIX 1549 1568 {ECO:0000244|PDB:4KP3}.
HELIX 1573 1575 {ECO:0000244|PDB:4KP3}.
HELIX 1581 1584 {ECO:0000244|PDB:4KP3}.
STRAND 1589 1592 {ECO:0000244|PDB:4KP3}.
HELIX 1594 1627 {ECO:0000244|PDB:4KP3}.
HELIX 1659 1675 {ECO:0000244|PDB:4KP3}.
HELIX 1680 1704 {ECO:0000244|PDB:4KP3}.
HELIX 1706 1708 {ECO:0000244|PDB:3WB8}.
HELIX 1711 1730 {ECO:0000244|PDB:4KP3}.
HELIX 1740 1742 {ECO:0000244|PDB:4KP3}.
HELIX 1743 1753 {ECO:0000244|PDB:4KP3}.
HELIX 1759 1768 {ECO:0000244|PDB:4KP3}.
HELIX 1774 1783 {ECO:0000244|PDB:4KP3}.
HELIX 1796 1805 {ECO:0000244|PDB:4KP3}.
TURN 1806 1808 {ECO:0000244|PDB:3WB8}.
HELIX 1836 1838 {ECO:0000244|PDB:4KP3}.
HELIX 1843 1845 {ECO:0000244|PDB:4KP3}.
STRAND 1850 1853 {ECO:0000244|PDB:4KP3}.
SEQUENCE 1853 AA; 215538 MW; D729DF9222EBCAA0 CRC64;
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTGELP
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI PPKHEPLTIF
CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDHVN
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
PRMSNKAFII KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
GDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA
TIVIQSYLRG YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV YLQCCFRRMM
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGVYNSE
TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKSIE ERADKYKQET
DQLVSNLKEE NTLLKQEKET LNHRIVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN
LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT
EEPIEKKVPL DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR
LLESQLQSQK RSHENEAEAL RGEIQSLKEE NNRQQQLLAQ NLQLPPEARI EASLQHEITR
LTNENLYFEE LYADDPKKYQ SYRISLYKRM IDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE
LEVGQMENIS PGQIIDEPIR PVNIPRKEKD FQGMLEYKRE DEQKLVKNLI LELKPRGVAV
NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE TVSFWLSNTC
RFLHCLKQYS GEEGFMKHNT SRQNEHCLTN FDLAEYRQVL SDLAIQIYQQ LVRVLENILQ
PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS IADEGTYTLD SILRQLNSFH SVMCQHGMDP
ELIKQVVKQM FYIVGAITLN NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE
TLEPLIQAAQ LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVSFIR
TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI ARV


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