MYO6_PIG
ID MYO6_PIG Reviewed; 1254 AA.
AC Q29122;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Unconventional myosin-VI;
DE AltName: Full=Unconventional myosin-6;
GN Name=MYO6;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ACTN1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=7929586; DOI=10.1083/jcb.127.2.425;
RA Hasson T., Mooseker M.S.;
RT "Porcine myosin-VI: characterization of a new mammalian unconventional
RT myosin.";
RL J. Cell Biol. 127:425-440(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION AT THR-406, CALCIUM-BINDING, AND MUTAGENESIS OF THR-406.
RX PubMed=12682054; DOI=10.1074/jbc.m208957200;
RA Morris C.A., Wells A.L., Yang Z., Chen L.Q., Baldacchino C.V.,
RA Sweeney H.L.;
RT "Calcium functionally uncouples the heads of myosin VI.";
RL J. Biol. Chem. 278:23324-23330(2003).
RN [5]
RP CALCIUM-CALMODULIN BINDING SITE, AND DOMAIN.
RX PubMed=15037754; DOI=10.1073/pnas.0306892101;
RA Bahloul A., Chevreux G., Wells A.L., Martin D., Nolt J., Yang Z.,
RA Chen L.-Q., Potier N., van Dorsselaer A., Rosenfeld S., Houdusse A.,
RA Sweeney H.L.;
RT "The unique insert in myosin VI is a structural calcium-calmodulin binding
RT site.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4787-4792(2004).
RN [6]
RP MUTAGENESIS OF THR-406, POSSIBLE FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16917816; DOI=10.1002/cm.20150;
RA Naccache S.N., Hasson T.;
RT "Myosin VI altered at threonine 406 stabilizes actin filaments in vivo.";
RL Cell Motil. Cytoskeleton 63:633-645(2006).
RN [7]
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF PHE-854; VAL-857; VAL-858 AND LEU-861.
RX PubMed=25159143; DOI=10.1016/j.celrep.2014.07.041;
RA Mukherjea M., Ali M.Y., Kikuti C., Safer D., Yang Z., Sirkia H., Ropars V.,
RA Houdusse A., Warshaw D.M., Sweeney H.L.;
RT "Myosin VI must dimerize and deploy its unusual lever arm in order to
RT perform its cellular roles.";
RL Cell Rep. 8:1522-1532(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-859 IN COMPLEX WITH CALMODULIN,
RP AND ATPASE ACTIVITY.
RX PubMed=15944696; DOI=10.1038/nature03592;
RA Menetrey J., Bahloul A., Wells A.L., Yengo C.M., Morris C.A., Sweeney H.L.,
RA Houdusse A.;
RT "The structure of the myosin VI motor reveals the mechanism of
RT directionality reversal.";
RL Nature 435:779-785(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 771-918, SUBUNIT, AND DOMAIN.
RX PubMed=19664948; DOI=10.1016/j.molcel.2009.07.010;
RA Mukherjea M., Llinas P., Kim H., Travaglia M., Safer D., Menetrey J.,
RA Franzini-Armstrong C., Selvin P.R., Houdusse A., Sweeney H.L.;
RT "Myosin VI dimerization triggers an unfolding of a three-helix bundle in
RT order to extend its reach.";
RL Mol. Cell 35:305-315(2009).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC (By similarity). Unconventional myosins serve in intracellular
CC movements (By similarity). Myosin 6 is a reverse-direction motor
CC protein that moves towards the minus-end of actin filaments (By
CC similarity). Has slow rate of actin-activated ADP release due to weak
CC ATP binding (PubMed:15944696). Functions in a variety of intracellular
CC processes such as vesicular membrane trafficking and cell migration
CC (PubMed:16917816). Required for the structural integrity of the Golgi
CC apparatus via the p53-dependent pro-survival pathway (By similarity).
CC Appears to be involved in a very early step of clathrin-mediated
CC endocytosis in polarized epithelial cells (By similarity). May act as a
CC regulator of F-actin dynamics (PubMed:7929586). As part of the DISP
CC complex, may regulate the association of septins with actin and thereby
CC regulate the actin cytoskeleton (By similarity). May play a role in
CC transporting DAB2 from the plasma membrane to specific cellular targets
CC (By similarity). May play a role in the extension and network
CC organization of neurites (By similarity). Required for structural
CC integrity of inner ear hair cells (By similarity). Modulates RNA
CC polymerase II-dependent transcription (By similarity).
CC {ECO:0000250|UniProtKB:Q64331, ECO:0000250|UniProtKB:Q9UM54,
CC ECO:0000269|PubMed:15944696, ECO:0000269|PubMed:16917816,
CC ECO:0000269|PubMed:7929586}.
CC -!- SUBUNIT: Homodimer; dimerization seems to implicate the unfolding of
CC the three-helix bundle region creating an additional calmodulin binding
CC site, and cargo binding (PubMed:25159143, PubMed:19664948). Component
CC of the DISP/DOCK7-induced septin displacement complex, at least
CC composed of DOCK7, LRCH3 and MYO6 (By similarity). Able to function as
CC a monomer under specific conditions in vitro (By similarity). Forms a
CC complex with CFTR and DAB2 in the apical membrane of epithelial cells
CC (By similarity). Binding to calmodulin through a unique insert, not
CC found in other myosins, located in the neck region between the motor
CC domain and the IQ domain appears to contribute to the directionality
CC reversal (PubMed:15037754). This interaction occurs only if the C-
CC terminal lobe of calmodulin is occupied by calcium (PubMed:12682054,
CC PubMed:15037754). Interaction with F-actin/ACTN1 occurs only at the
CC apical brush border domain of the proximal tubule cells
CC (PubMed:7929586). Interacts with DAB2 (By similarity). In vitro, the C-
CC terminal globular tail binds a C-terminal region of DAB2 (By
CC similarity). Interacts with CFTR (By similarity). Interacts with OPTN
CC (By similarity). Interacts with CABP5 (By similarity).
CC {ECO:0000250|UniProtKB:E1BPK6, ECO:0000250|UniProtKB:Q64331,
CC ECO:0000250|UniProtKB:Q9I8D1, ECO:0000250|UniProtKB:Q9UM54,
CC ECO:0000269|PubMed:12682054, ECO:0000269|PubMed:15037754,
CC ECO:0000269|PubMed:19664948, ECO:0000269|PubMed:25159143,
CC ECO:0000269|PubMed:7929586}.
CC -!- INTERACTION:
CC Q29122; P98082-1: DAB2; Xeno; NbExp=2; IntAct=EBI-15804516, EBI-15804617;
CC Q29122; Q96CV9: OPTN; Xeno; NbExp=3; IntAct=EBI-15804516, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9UM54}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UM54}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UM54}. Nucleus {ECO:0000250|UniProtKB:Q9UM54}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9UM54}. Membrane,
CC clathrin-coated pit {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9UM54}. Cell
CC projection, filopodium {ECO:0000250|UniProtKB:Q9UM54}. Cell projection,
CC ruffle membrane {ECO:0000269|PubMed:16917816}. Cell projection,
CC microvillus {ECO:0000250|UniProtKB:Q9UM54}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:7929586}. Note=Also present in endocytic vesicles
CC (PubMed:16917816). Translocates from membrane ruffles, endocytic
CC vesicles and cytoplasm to Golgi apparatus, perinuclear membrane and
CC nucleus through induction by p53 and p53-induced DNA damage (By
CC similarity). Recruited into membrane ruffles from cell surface by EGF-
CC stimulation (By similarity). Colocalizes with DAB2 in clathrin-coated
CC pits/vesicles (By similarity). Colocalizes with OPTN at the Golgi
CC complex and in vesicular structures close to the plasma membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q9I8D1,
CC ECO:0000250|UniProtKB:Q9UM54, ECO:0000269|PubMed:16917816}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined including kidney
CC cortex, intestinal mucosa, liver, lung, heart, jowl muscle, brain
CC cortex and medulla, and in the epithelial cell line, LLC-PK1 (at
CC protein level) (PubMed:7929586). In the kidney, located to the brush
CC border of adult kidney proximal tubule cells (PubMed:7929586).
CC {ECO:0000269|PubMed:7929586}.
CC -!- DEVELOPMENTAL STAGE: Locates to the apical domain only during the final
CC stages of kidney proximal tubule development.
CC -!- DOMAIN: Divided into three regions: a N-terminal motor (head) domain,
CC followed by a neck domain consisting of a calmodulin-binding linker
CC domain and a single IQ motif, and a C-terminal tail region with a
CC three-helix bundle region, a SAH domain and a unique globular domain
CC required for interaction with other proteins such as cargo-binding.
CC {ECO:0000269|PubMed:19664948, ECO:0000269|PubMed:25159143}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. Its contribution to the mechanism
CC confering the myosin movement on actin filaments is debated.
CC {ECO:0000250|UniProtKB:Q9UM54}.
CC -!- PTM: Phosphorylation in the motor domain, induced by EGF, results in
CC translocation of MYO6 from the cell surface to membrane ruffles and
CC affects F-actin dynamics. Phosphorylated in vitro by p21-activated
CC kinase (PAK). {ECO:0000269|PubMed:12682054}.
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-6 (MYH6). {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but
CC generally accepted to contain a stable SAH domain instead.
CC {ECO:0000305}.
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DR EMBL; Z35331; CAA84559.1; -; mRNA.
DR PIR; A54818; A54818.
DR RefSeq; NP_999186.1; NM_214021.1.
DR PDB; 2BKH; X-ray; 2.40 A; A=2-816.
DR PDB; 2BKI; X-ray; 2.90 A; A=1-859.
DR PDB; 2V26; X-ray; 1.75 A; A=5-789.
DR PDB; 2VAS; X-ray; 2.40 A; A=2-816.
DR PDB; 2VB6; X-ray; 2.30 A; A=2-816.
DR PDB; 2X51; X-ray; 2.20 A; A=1-816.
DR PDB; 3GN4; X-ray; 2.70 A; A/E=771-918.
DR PDB; 3L9I; X-ray; 2.20 A; A=2-816.
DR PDB; 4ANJ; X-ray; 2.60 A; A=1-817.
DR PDB; 4DBP; X-ray; 2.20 A; A=2-816.
DR PDB; 4DBQ; X-ray; 2.60 A; A=2-816.
DR PDB; 4DBR; X-ray; 1.95 A; A=5-790.
DR PDB; 5O2L; X-ray; 2.20 A; A=5-790.
DR PDB; 6BNP; EM; 4.60 A; I/J/K/L/M/N=2-706.
DR PDB; 6BNQ; EM; 5.50 A; I/J/K/L/M/N=2-706.
DR PDB; 6BNV; EM; 4.60 A; I/J/K/L/M/N=2-818.
DR PDB; 6BNW; EM; 5.50 A; I/J/K/L/M/N=2-818.
DR PDBsum; 2BKH; -.
DR PDBsum; 2BKI; -.
DR PDBsum; 2V26; -.
DR PDBsum; 2VAS; -.
DR PDBsum; 2VB6; -.
DR PDBsum; 2X51; -.
DR PDBsum; 3GN4; -.
DR PDBsum; 3L9I; -.
DR PDBsum; 4ANJ; -.
DR PDBsum; 4DBP; -.
DR PDBsum; 4DBQ; -.
DR PDBsum; 4DBR; -.
DR PDBsum; 5O2L; -.
DR PDBsum; 6BNP; -.
DR PDBsum; 6BNQ; -.
DR PDBsum; 6BNV; -.
DR PDBsum; 6BNW; -.
DR AlphaFoldDB; Q29122; -.
DR SMR; Q29122; -.
DR BioGRID; 1149220; 2.
DR DIP; DIP-48994N; -.
DR IntAct; Q29122; 2.
DR STRING; 9823.ENSSSCP00000004831; -.
DR iPTMnet; Q29122; -.
DR PaxDb; Q29122; -.
DR PeptideAtlas; Q29122; -.
DR PRIDE; Q29122; -.
DR GeneID; 397085; -.
DR KEGG; ssc:397085; -.
DR CTD; 4646; -.
DR eggNOG; KOG0163; Eukaryota.
DR InParanoid; Q29122; -.
DR OrthoDB; 122881at2759; -.
DR EvolutionaryTrace; Q29122; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IMP:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IPI:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; IDA:UniProtKB.
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:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IBA:GO_Central.
DR GO; GO:0042472; P:inner ear morphogenesis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051046; P:regulation of secretion; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01382; MYSc_Myo6; 1.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR032412; Myosin-VI_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR036114; MYSc_Myo6.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF16521; Myosin-VI_CBD; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Coated pit; Cytoplasm; Cytoplasmic vesicle;
KW Endocytosis; Golgi apparatus; Hearing; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1254
FT /note="Unconventional myosin-VI"
FT /id="PRO_0000271746"
FT DOMAIN 2..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 57..772
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 814..843
FT /note="IQ"
FT /evidence="ECO:0000269|PubMed:15037754"
FT REGION 273..317
FT /note="Responsible for slow ATPase activity"
FT /evidence="ECO:0000269|PubMed:15944696"
FT REGION 666..673
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 783..811
FT /note="Required for binding calmodulin"
FT /evidence="ECO:0000269|PubMed:15037754"
FT REGION 836..917
FT /note="Three-helix bundle"
FT /evidence="ECO:0000305|PubMed:19664948"
FT REGION 918..985
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT REGION 935..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1087
FT /note="Interaction with OPTN"
FT /evidence="ECO:0000250|UniProtKB:Q9I8D1"
FT REGION 1096..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UM54"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12682054"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64331"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64331"
FT MUTAGEN 406
FT /note="T->E: Greatly reduced phosphorylation. Transports
FT uncoated endocytic vesicles to clusters at distinct
FT peripheral sites and alters actin filament structure."
FT /evidence="ECO:0000269|PubMed:12682054,
FT ECO:0000269|PubMed:16917816"
FT MUTAGEN 851
FT /note="L->A: Abolishes additional calmodulin-binding upon
FT unfolding three-helix bundle; when associated with A-854,
FT A-857, A-858 and A-861."
FT /evidence="ECO:0000269|PubMed:25159143"
FT MUTAGEN 854
FT /note="F->A: Abolishes additional calmodulin-binding upon
FT unfolding three-helix bundle; when associated with A-851,
FT A-857, A-858 and A-861."
FT /evidence="ECO:0000269|PubMed:25159143"
FT MUTAGEN 857
FT /note="V->A: Abolishes additional calmodulin-binding upon
FT unfolding three-helix bundle; when associated with A-851,
FT A-854, A-858 and A-861."
FT /evidence="ECO:0000269|PubMed:25159143"
FT MUTAGEN 858
FT /note="V->A: Abolishes additional calmodulin-binding upon
FT unfolding three-helix bundle; when associated with A-851,
FT A-851, A-857 and A-861."
FT /evidence="ECO:0000269|PubMed:25159143"
FT MUTAGEN 861
FT /note="L->A: Abolishes additional calmodulin-binding upon
FT unfolding three-helix bundle; when associated with A-851,
FT A-854, A-857 and A-858."
FT /evidence="ECO:0000269|PubMed:25159143"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2BKH"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2X51"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4DBP"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:5O2L"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5O2L"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2BKI"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 331..348
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:3L9I"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 414..441
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:2X51"
FT HELIX 469..489
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 541..551
FT /evidence="ECO:0007829|PDB:2V26"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:2BKI"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:2VB6"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 576..582
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 604..611
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 616..621
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 624..629
FT /evidence="ECO:0007829|PDB:2BKI"
FT HELIX 634..638
FT /evidence="ECO:0007829|PDB:2BKI"
FT HELIX 644..660
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 662..670
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 683..692
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 695..702
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 704..706
FT /evidence="ECO:0007829|PDB:2VAS"
FT STRAND 707..711
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 712..719
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 725..728
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 732..742
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 754..759
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 764..771
FT /evidence="ECO:0007829|PDB:2V26"
FT HELIX 775..788
FT /evidence="ECO:0007829|PDB:2V26"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:2BKI"
FT TURN 822..825
FT /evidence="ECO:0007829|PDB:2BKI"
FT HELIX 867..886
FT /evidence="ECO:0007829|PDB:3GN4"
FT HELIX 893..913
FT /evidence="ECO:0007829|PDB:3GN4"
SQ SEQUENCE 1254 AA; 144859 MW; 0A72C1A7991CF763 CRC64;
MEDGKPVWAP HPTDGFQVGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE TIKSYQGKSL
GTMPPHVFAI ADKAFRDMKV LKLSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
EERNYHIFYR LCAGASEDIR ERLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY
LKAGSLKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG
GCNLKNKSTQ ALEYCAEKLL GLDQDDLRVS LTTRVMLTTA GGAKGTVIKV PLKVEQANNA
RDALAKTVYS HLFDHVVNRV NQCFPFETSS YFIGVLDIAG FEYFEHNSFE QFCINYCNEK
LQQFFNERIL KEEQELYQKE GLGVNEVHYV DNQDCIDLIE ARLVGILDIL DEENRLPQPS
DQHFTSAGHQ KHKDHFRLSI PRKSKLAIHR NIAYDEGFII RHFAGAVCYE TTQFVEKNND
ALHMSLESLI CESRDKFIRE LFESSTNNNK DTKQKAGKLS FISVGNKFKT QLNLLLDKLR
STGASFIRCI KPNLKMTSHH FEGAQILSQL QCSGMVSVLD LMQGGFPSRA SFHEVYNMYK
KSLPDKLARL DPRLFCKALF KALGLNEIDY KFGLTKVFFR PGKFAEFDQI MKSDPDHLAE
LVKRVNHWLI CSRWKKVQWC SLSVIKLKNK IKYRAEACIK MQKTIRMWLC KRRHKPRIDG
LVKVGTLKKR LDKFNEVVSA LKDGKQEMSK QVKDLEISID ALMAKIKSTM MTREQIQKEY
DALVKSSAVL LSALQKKKQQ EEEAERLRRI QEEMEKERKR REEDEQRRRK EEEERRMKLE
MEAKRKQEEE ERKKREDDEK RIQAEVEAQL ARQREEESQQ QAVLEQERRD RELALRIAQS
EAELISDEAQ ADPGLRRGPA VQATKAAAGT KKYDLSKWKY AELRDTINTS CDIELLAACR
EEFHRRLKVY HAWKSKNKKR NTETEQRAPK SVTDYAQQNP AVQLPARQQE IEMNRQQRFF
RIPFIRSADQ YKDPQNKKKG WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL
EETGLTRKRG AEILPRQFEE IWERCGGIQY LQNAIESRQA RPTYATAMLQ NLLK
