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 12-AUG-2020, entry version 147. 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.91.24.11767c; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q6PIF6; -. 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; 23 antibodies. DR Ensembl; ENST00000409816; ENSP00000386461; ENSG00000169994. [Q6PIF6-1] DR Ensembl; ENST00000428314; ENSP00000415090; ENSG00000169994. [Q6PIF6-1] DR GeneID; 4648; -. DR KEGG; hsa:4648; -. DR UCSC; uc002top.3; human. [Q6PIF6-1] DR CTD; 4648; -. DR DisGeNET; 4648; -. DR EuPathDB; HostDB:ENSG00000169994.18; -. 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 eggNOG; KOG4229; Eukaryota. DR GeneTree; ENSGT00940000157247; -. DR HOGENOM; CLU_000192_14_1_1; -. DR InParanoid; Q6PIF6; -. DR KO; K21868; -. DR OMA; LTNCQPY; -. DR OrthoDB; 527681at2759; -. DR PhylomeDB; Q6PIF6; -. DR TreeFam; TF335306; -. DR PathwayCommons; Q6PIF6; -. DR BioGRID-ORCS; 4648; 3 hits in 870 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 duodenum and 151 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:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005902; C:microvillus; IDA:UniProtKB. DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW. DR GO; GO:0031982; C:vesicle; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0030898; F:actin-dependent ATPase activity; 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; -; 2. DR Gene3D; 2.30.29.30; -; 2. DR Gene3D; 2.30.30.360; -; 1. 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; IPR008989; Myosin_S1_N. 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 Pfam; PF07653; SH3_2; 1. 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; Polymorphism; KW Reference proteome; Repeat; 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 NP_BIND 158..165 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782" 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 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:0000244|PDB:5XBF" FT HELIX 1655..1658 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1661..1663 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1664..1677 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1689..1702 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1705..1717 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1724..1738 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 1745..1747 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1748..1756 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 1757..1760 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1764..1777 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1786..1793 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 1799..1805 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 1806..1808 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 1809..1815 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1821..1832 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 1840..1846 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 1849..1852 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1859..1873 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 1886..1892 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1904..1909 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1911..1920 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1928..1943 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1947..1951 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1953..1956 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1957..1959 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 1963..1965 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1966..1968 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1971..1982 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1983..1985 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 1990..2001 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 2005..2008 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2010..2016 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2024..2031 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2034..2038 FT /evidence="ECO:0000244|PDB:5XBF" FT TURN 2040..2042 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2045..2049 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 2051..2053 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2054..2059 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2061..2068 FT /evidence="ECO:0000244|PDB:5XBF" FT STRAND 2075..2080 FT /evidence="ECO:0000244|PDB:5XBF" FT HELIX 2084..2099 FT /evidence="ECO:0000244|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 //