MYO7B_HUMAN
ID MYO7B_HUMAN Reviewed; 2116 AA.
AC Q6PIF6; Q14786; Q8TEE1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Unconventional myosin-VIIb;
GN Name=MYO7B;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-196 (ISOFORMS 1/2).
RX PubMed=8022818; DOI=10.1073/pnas.91.14.6549;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RT "Identification and overlapping expression of multiple unconventional
RT myosin genes in vertebrate cell types.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994).
RN [3]
RP ERRATUM OF PUBMED:8022818.
RX PubMed=7972138; DOI=10.1073/pnas.91.24.11767-c;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1102-2116 (ISOFORM 2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1451-2116 (ISOFORM 1).
RC TISSUE=Testis;
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 FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF THE IMAC COMPLEX,
RP INTERACTION WITH CDHR2; CDHR5 AND USH1C, AND REGION.
RX PubMed=24725409; DOI=10.1016/j.cell.2014.01.067;
RA Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E.,
RA Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A.,
RA Kachar B., Tyska M.J.;
RT "Intestinal brush border assembly driven by protocadherin-based
RT intermicrovillar adhesion.";
RL Cell 157:433-446(2014).
RN [7]
RP INTERACTION WITH USH1C, AND REGION.
RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
RA Li J., He Y., Lu Q., Zhang M.;
RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush
RT border microvilli tip-link complex.";
RL Dev. Cell 36:179-189(2016).
RN [8]
RP FUNCTION, INTERACTION WITH ANKS4B AND USH1C, AND IDENTIFICATION OF THE IMAC
RP COMPLEX.
RX PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022;
RA Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., Tyska M.J.;
RT "ANKS4B is essential for intermicrovillar adhesion complex formation.";
RL Dev. Cell 36:190-200(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments. As part
CC of the intermicrovillar adhesion complex/IMAC plays a role in
CC epithelial brush border differentiation, controlling microvilli
CC organization and length. May link the complex to the actin core bundle
CC of microvilli (Probable). {ECO:0000305|PubMed:24725409,
CC ECO:0000305|PubMed:26812018}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5 (PubMed:24725409, PubMed:26812018). Interacts
CC with CDHR2 (PubMed:24725409). Interacts with CDHR5 (PubMed:24725409).
CC Interacts with USH1C (PubMed:24725409, PubMed:26812017,
CC PubMed:26812018). Interacts with ANKS4B; requires initial interaction
CC with USH1C (PubMed:26812018). {ECO:0000269|PubMed:24725409,
CC ECO:0000269|PubMed:26812017, ECO:0000269|PubMed:26812018}.
CC -!- INTERACTION:
CC Q6PIF6; Q9BYE9: CDHR2; NbExp=3; IntAct=EBI-4400912, EBI-493793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
CC projection, microvillus {ECO:0000269|PubMed:24725409}. Note=Enriched in
CC the microvilli of the intestinal brush border.
CC {ECO:0000269|PubMed:24725409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PIF6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PIF6-2; Sequence=VSP_032930, VSP_032931;
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-7 (MYH7). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35615.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC010976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L29147; AAA20910.1; -; mRNA.
DR EMBL; AK074183; BAB85009.1; -; mRNA.
DR EMBL; BC035615; AAH35615.2; ALT_INIT; mRNA.
DR CCDS; CCDS46405.1; -. [Q6PIF6-1]
DR RefSeq; NP_001073996.1; NM_001080527.1. [Q6PIF6-1]
DR PDB; 5MV7; X-ray; 2.44 A; A=1605-2116.
DR PDB; 5MV8; X-ray; 1.88 A; A=1609-2116.
DR PDB; 5XBF; X-ray; 1.80 A; A=1601-2116.
DR PDBsum; 5MV7; -.
DR PDBsum; 5MV8; -.
DR PDBsum; 5XBF; -.
DR AlphaFoldDB; Q6PIF6; -.
DR SMR; Q6PIF6; -.
DR BioGRID; 110732; 1.
DR IntAct; Q6PIF6; 4.
DR STRING; 9606.ENSP00000415090; -.
DR iPTMnet; Q6PIF6; -.
DR PhosphoSitePlus; Q6PIF6; -.
DR BioMuta; MYO7B; -.
DR DMDM; 182667924; -.
DR EPD; Q6PIF6; -.
DR jPOST; Q6PIF6; -.
DR MassIVE; Q6PIF6; -.
DR MaxQB; Q6PIF6; -.
DR PaxDb; Q6PIF6; -.
DR PeptideAtlas; Q6PIF6; -.
DR PRIDE; Q6PIF6; -.
DR ProteomicsDB; 67155; -. [Q6PIF6-1]
DR ProteomicsDB; 67156; -. [Q6PIF6-2]
DR Antibodypedia; 47564; 27 antibodies from 17 providers.
DR DNASU; 4648; -.
DR Ensembl; ENST00000428314.5; ENSP00000415090.1; ENSG00000169994.20. [Q6PIF6-1]
DR GeneID; 4648; -.
DR KEGG; hsa:4648; -.
DR UCSC; uc002top.3; human. [Q6PIF6-1]
DR CTD; 4648; -.
DR DisGeNET; 4648; -.
DR GeneCards; MYO7B; -.
DR HGNC; HGNC:7607; MYO7B.
DR HPA; ENSG00000169994; Tissue enriched (intestine).
DR MIM; 606541; gene.
DR neXtProt; NX_Q6PIF6; -.
DR OpenTargets; ENSG00000169994; -.
DR PharmGKB; PA31412; -.
DR VEuPathDB; HostDB:ENSG00000169994; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000157247; -.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q6PIF6; -.
DR OMA; TLGIADM; -.
DR OrthoDB; 527681at2759; -.
DR PhylomeDB; Q6PIF6; -.
DR TreeFam; TF335306; -.
DR PathwayCommons; Q6PIF6; -.
DR SignaLink; Q6PIF6; -.
DR BioGRID-ORCS; 4648; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; MYO7B; human.
DR GenomeRNAi; 4648; -.
DR Pharos; Q6PIF6; Tbio.
DR PRO; PR:Q6PIF6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6PIF6; protein.
DR Bgee; ENSG00000169994; Expressed in ileal mucosa and 123 other tissues.
DR ExpressionAtlas; Q6PIF6; baseline and differential.
DR Genevisible; Q6PIF6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0090651; C:apical cytoplasm; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:1904970; P:brush border assembly; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 1.25.40.530; -; 3.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Cell projection; Cytoplasm; Cytoskeleton; Differentiation; Motor protein;
KW Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..2116
FT /note="Unconventional myosin-VIIb"
FT /id="PRO_0000329046"
FT DOMAIN 65..760
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 745..765
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 763..792
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 786..815
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..834
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 832..861
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 855..884
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 989..1192
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1197..1506
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1501..1567
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1644..1793
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1790..1896
FT /note="MyTH4 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1799..2102
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 637..659
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 916..1542
FT /note="Mediates interaction with ANKS4B"
FT /evidence="ECO:0000269|PubMed:24725409"
FT REGION 1501..2116
FT /note="Mediates interaction with CDHR2, CDHR5 and USH1C"
FT /evidence="ECO:0000269|PubMed:24725409,
FT ECO:0000269|PubMed:26812017"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ6"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ6"
FT MOD_RES 1645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99MZ6"
FT VAR_SEQ 1851..1957
FT /note="ISQKEGDFFFDSLREVSDWVKKNKPQKEGAPVTLPYQVYFMRKLWLNISPGK
FT DVNADTILHYHQELPKYLRGFHKCSREDAIHLAGLIYKAQFNNDRSQLASVPKIL ->
FT GRAGAGQTVGGRAVSEALGAACGGLSLPGAPMLDQAAGTEVGGVLEQSQLHTPIAHAQP
FT TPAQHPGRRRPLDQNPAGSQEDSPRKPPNFPVPSPSPGHQPEGGRLLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_032930"
FT VAR_SEQ 1958..2116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_032931"
FT VARIANT 21
FT /note="G -> S (in dbSNP:rs2404991)"
FT /id="VAR_042626"
FT VARIANT 1264
FT /note="R -> Q (in dbSNP:rs2245408)"
FT /id="VAR_042627"
FT VARIANT 1647
FT /note="E -> D (in dbSNP:rs13025959)"
FT /id="VAR_042628"
FT VARIANT 2105
FT /note="Q -> R (in dbSNP:rs11686946)"
FT /id="VAR_042629"
FT CONFLICT 182
FT /note="H -> D (in Ref. 2; AAA20910)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102..1106
FT /note="LRPSL -> WSVSF (in Ref. 4; BAB85009)"
FT /evidence="ECO:0000305"
FT HELIX 1612..1618
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1655..1658
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1661..1663
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1664..1677
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1689..1702
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1705..1717
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1724..1738
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 1745..1747
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1748..1756
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 1757..1760
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1764..1777
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1786..1793
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 1799..1805
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 1806..1808
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 1809..1815
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1821..1832
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 1840..1846
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 1849..1852
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1859..1873
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 1886..1892
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1904..1909
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1911..1920
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1928..1943
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1947..1951
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1953..1956
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1957..1959
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 1963..1965
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1966..1968
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1971..1982
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1983..1985
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 1990..2001
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 2005..2008
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2010..2016
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2024..2031
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2034..2038
FT /evidence="ECO:0007829|PDB:5XBF"
FT TURN 2040..2042
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2045..2049
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 2051..2053
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2054..2059
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2061..2068
FT /evidence="ECO:0007829|PDB:5XBF"
FT STRAND 2075..2080
FT /evidence="ECO:0007829|PDB:5XBF"
FT HELIX 2084..2099
FT /evidence="ECO:0007829|PDB:5XBF"
SQ SEQUENCE 2116 AA; 241599 MW; 18E908998470E4FD CRC64;
MSGFRLGDHV WLEPPSTHKT GVAIGGIIKE AKPGKVLVED DEGKEHWIRA EDFGVLSPMH
PNSVQGVDDM IRLGDLNEAG MVHNLLIRYQ QHKIYTYTGS ILVAVNPFQV LPLYTLEQVQ
LYYSRHMGEL PPHVFAIANN CYFSMKRNKR DQCCIISGES GAGKTETTKL ILQFLATISG
QHSWIEQQVL EANPILEAFG NAKTIRNDNS SRFGKYIDIY FNPSGVIEGA RIEQFLLEKS
RVCRQAPEER NYHIFYCMLM GVSAEDKQLL SLGTPSEYHY LTMGNCTSCE GLNDAKDYAH
IRSAMKILQF SDSESWDVIK LLAAILHLGN VGFMASVFEN LDASDVMETP AFPTVMKLLE
VQHQELRDCL IKHTILIRGE FVTRSLNIAQ AADRRDAFVK GIYGHLFLWI VKKINAAIFT
PPAQDPKNVR RAIGLLDIFG FENFENNSFE QLCINFANEH LQQFFVQHVF TMEQEEYRSE
NISWDYIHYT DNRPTLDLLA LKPMSIISLL DEESRFPQGT DLTMLQKLNS VHANNKAFLQ
PKNIHDARFG IAHFAGEVYY QAEGFLEKNR DVLSTDILTL VYSSKNKFLR EIFNLELAET
KLGHGTIRQA KAGNHLFKSA DSNKRPSTLG SQFKQSLDQL MKILTNCQPY FIRCIKPNEY
KKPLLFDREL CLRQLRYSGM METVHIRKSG FPIRYTFEEF SQRFGVLLPN AMRMQLQGKL
RQMTLGITDV WLRTDKDWKA GKTKIFLRDH QDTLLEVQRS QVLDRAALSI QKVLRGYRYR
KEFLRQRRAA VTLQAWWRGY CNRRNFKLIL VGFERLQAIA RSQPLARQYQ AMRQRTVQLQ
ALCRGYLVRQ QVQAKRRAVV VIQAHARGMA ARRNFQQRKA NAPLVIPAEG QKSQGALPAK
KRRSIYDTVT DTEMVEKVFG FLPAMIGGQE GQASPHFEDL ESKTQKLLEV DLDTVPMAEE
PEEDVDGLAE YTFPKFAVTY FQKSASHTHI RRPLRYPLLY HEDDTDCLAA LVIWNVILRF
MGDLPEPVLY ARSSQQGSSV MRQIHDTLGR EHGAQVPQHS RSAQVASQLN IGEEALEPDG
LGADRPMSNL EKVHFIVGYA ILRPSLRDEI YCQICKQLSE NFKTSSLARG WILLSLCLGC
FPPSERFMKY LLNFIGQGPA TYGPFCAERL RRTYANGVRA EPPTWLELQA VKSKKHIPIQ
VILATGESLT VPVDSASTSR EMCMHIAHKQ GLSDHLGFSL QVAVYDKFWS LGSGRDHMMD
AIARCEQMAQ ERGESQRQSP WRIYFRKEFF TPWHDSREDP VSTELIYRQV LRGVWSGEYS
FEKEEELVEL LARHCYVQLG ASAESKAVQE LLPSCIPHKL YRTKPPDRWA SLVTAACAKA
PYTQKQVTPL AVREQVVDAA RLQWPLLFSR LFEVITLSGP RLPKTQLILA VNWKGLCFLD
QQEKMLLELS FPEVMGLATN REAQGGQRLL LSTMHEEYEF VSPSSVAIAE LVALFLEGLK
ERSIFAMALQ DRKATDDTTL LAFKKGDLLV LTKKQGLLAS ENWTLGQNDR TGKTGLVPMA
CLYTIPTVTK PSAQLLSLLA MSPEKRKLAA QEGQFTEPRP EEPPKEKLHT LEEFSYEFFR
APEKDMVSMA VLPLARARGH LWAYSCEPLR QPLLKRVHAN VDLWDIACQI FVAILRYMGD
YPSRQAWPTL ELTDQIFTLA LQHPALQDEV YCQILKQLTH NSNRHSEERG WQLLWLCTGL
FPPSKGLLPH AQKFIDTRRG KLLAPDCSRR IQKVLRTGPR KQPPHQVEVE AAEQNVSRIC
HKIYFPNDTS EMLEVVANTR VRDVCDSIAT RLQLASWEGC SLFIKISDKV ISQKEGDFFF
DSLREVSDWV KKNKPQKEGA PVTLPYQVYF MRKLWLNISP GKDVNADTIL HYHQELPKYL
RGFHKCSRED AIHLAGLIYK AQFNNDRSQL ASVPKILREL VPENLTRLMS SEEWKKSILL
AYDKHKDKTV EEAKVAFLKW ICRWPTFGSA FFEVKQTSEP SYPDVILIAI NRHGVLLIHP
KTKDLLTTYP FTKISSWSSG STYFHMALGS LGRGSRLLCE TSLGYKMDDL LTSYVQQLLS
AMNKQRGSKA PALAST
