OTOF_RAT
ID OTOF_RAT Reviewed; 1993 AA.
AC Q9ERC5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Otoferlin;
DE AltName: Full=Fer-1-like protein 2;
GN Name=Otof; Synonyms=Fer1l2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1554-1819.
RC STRAIN=Sprague-Dawley;
RA Beisel K.W., Nelson N.C., Beisel C.L., Delimont D.C., He D.Z.Z.,
RA Fritzsch B.;
RT "Dynamic developmental expression of cochlear hair cell genes: prestin and
RT otoferlin.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17229086; DOI=10.1111/j.1460-9568.2006.05225.x;
RA Schug N., Braig C., Zimmermann U., Engel J., Winter H., Ruth P., Blin N.,
RA Pfister M., Kalbacher H., Knipper M.;
RT "Differential expression of otoferlin in brain, vestibular system, immature
RT and mature cochlea of the rat.";
RL Eur. J. Neurosci. 24:3372-3380(2006).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=18772196; DOI=10.1093/hmg/ddn279;
RA Heidrych P., Zimmermann U., Bress A., Pusch C.M., Ruth P., Pfister M.,
RA Knipper M., Blin N.;
RT "Rab8b GTPase, a protein transport regulator, is an interacting partner of
RT otoferlin, defective in a human autosomal recessive deafness form.";
RL Hum. Mol. Genet. 17:3814-3821(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-124, CIRCULAR DICHROISM, AND
RP DOMAIN.
RX PubMed=21216247; DOI=10.1016/j.jmb.2010.12.031;
RA Helfmann S., Neumann P., Tittmann K., Moser T., Ficner R., Reisinger E.;
RT "The crystal structure of the CA domain of otoferlin reveals an
RT unconventional top loop region.";
RL J. Mol. Biol. 406:479-490(2011).
CC -!- FUNCTION: Key calcium ion sensor involved in the Ca(2+)-triggered
CC synaptic vesicle-plasma membrane fusion and in the control of
CC neurotransmitter release at these output synapses. Interacts in a
CC calcium-dependent manner to the presynaptic SNARE proteins at ribbon
CC synapses of cochlear inner hair cells (IHCs) to trigger exocytosis of
CC neurotransmitter. Also essential to synaptic exocytosis in immature
CC outer hair cells (OHCs). May also play a role within the recycling of
CC endosomes (By similarity). {ECO:0000250|UniProtKB:Q9ESF1}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds Ca(2+). The ions are bound to the C2 1 domain.
CC {ECO:0000250};
CC -!- SUBUNIT: Interacts with SNAP25; the interaction is direct. Interacts
CC with STX1; the interaction is direct. Interacts with RAB8B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:Q9ESF1}. Basolateral cell
CC membrane {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:Q9ESF1}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9ESF1}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9ESF1}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9ESF1}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9ESF1}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9ESF1}. Note=Detected at basolateral cell
CC membrane with synaptic vesicles surrounding the ribbon and at the
CC presynaptic plasma membrane in the inner hair cells (IHCs) at postnatal
CC day 30 (P30). Colocalizes with GPR25 and RAB8B in inner hair cells.
CC {ECO:0000250|UniProtKB:Q9ESF1}.
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the cochlea and brain.
CC Expressed in cerebellum (Purkinje cells), hippocampus (granule cells of
CC the dentate gyrus and in pyramidal cells of the CA1-CA3 region) and
CC cortex (stellate and pyramidal cells). Expressed in hair cells of
CC vestibular organs such as the saccule, utricle and crista ampullari.
CC Expressed in the cochlear inner and outer cells (IHCs and OHCs) (at
CC protein level). Expressed in brain: brainstem, cerebellum (granules
CC cells and Purkinje cell layer), cortex (layers IV and V), inferior
CC colliculus, superior colliculus and hippocampus (granule cells of the
CC dentate gyrus and in pyramidal cells of the CA1-CA3 region).
CC {ECO:0000269|PubMed:17229086, ECO:0000269|PubMed:18772196}.
CC -!- DOMAIN: The N-terminal first 124 residues can be classified as C2
CC domain, based on their 3D-structure. They are not sufficient for
CC calcium ion or phospholipid binding. {ECO:0000269|PubMed:21216247}.
CC -!- SIMILARITY: Belongs to the ferlin family. {ECO:0000305}.
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DR EMBL; AABR03048736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03049539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF315944; AAG30298.1; -; mRNA.
DR RefSeq; XP_006239895.1; XM_006239833.2.
DR PDB; 3L9B; X-ray; 1.95 A; A=1-124.
DR PDBsum; 3L9B; -.
DR AlphaFoldDB; Q9ERC5; -.
DR SMR; Q9ERC5; -.
DR STRING; 10116.ENSRNOP00000046997; -.
DR iPTMnet; Q9ERC5; -.
DR PhosphoSitePlus; Q9ERC5; -.
DR PaxDb; Q9ERC5; -.
DR PRIDE; Q9ERC5; -.
DR Ensembl; ENSRNOT00000044278; ENSRNOP00000046997; ENSRNOG00000009967.
DR GeneID; 84573; -.
DR CTD; 9381; -.
DR RGD; 620646; Otof.
DR eggNOG; KOG1326; Eukaryota.
DR GeneTree; ENSGT00940000155086; -.
DR HOGENOM; CLU_001183_3_1_1; -.
DR InParanoid; Q9ERC5; -.
DR OrthoDB; 20162at2759; -.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; Q9ERC5; -.
DR PRO; PR:Q9ERC5; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000009967; Expressed in frontal cortex and 1 other tissue.
DR ExpressionAtlas; Q9ERC5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0045178; C:basal part of cell; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR CDD; cd08373; C2A_Ferlin; 1.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04018; C2C_Ferlin; 1.
DR CDD; cd04017; C2D_Ferlin; 1.
DR CDD; cd04037; C2E_Ferlin; 1.
DR CDD; cd08374; C2F_Ferlin; 1.
DR Gene3D; 2.60.40.150; -; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037726; C2A_Ferlin.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037722; C2C_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR InterPro; IPR029996; Otoferlin.
DR PANTHER; PTHR12546; PTHR12546; 1.
DR PANTHER; PTHR12546:SF32; PTHR12546:SF32; 1.
DR Pfam; PF00168; C2; 6.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF08151; FerI; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 6.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; SSF49562; 7.
DR PROSITE; PS50004; C2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Hearing;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal-anchor;
KW Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..1993
FT /note="Otoferlin"
FT /id="PRO_0000057883"
FT TOPO_DOM 1..1959
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1960..1980
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1981..1993
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 1..98
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 251..372
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 415..546
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 959..1084
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1131..1257
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1460..1589
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1710..1861
FT /note="C2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 127..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 807..836
FT /evidence="ECO:0000255"
FT COMPBIAS 164..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..695
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 997
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1053
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1053
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1055
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1055
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1061
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1561
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1567
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1832
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1835
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1838
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 1629
FT /note="H -> P (in Ref. 2; AAG30298)"
FT /evidence="ECO:0000305"
FT CONFLICT 1811
FT /note="F -> C (in Ref. 2; AAG30298)"
FT /evidence="ECO:0000305"
FT STRAND 1..12
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 42..54
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:3L9B"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:3L9B"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:3L9B"
SQ SEQUENCE 1993 AA; 226339 MW; 23F6321854110EC8 CRC64;
MALIVHLKTV SELRGRADRI AKVTFRGQSF YSRVLENCED VADFDETFRW PVASSIDRNE
VLEIQIFNYS KVFSNKLIGT FRMVLQKVVE ENRVEVSDTL IDDNNAIIKT SLSMEVRYQA
ADGTVGPWDD GDFLGDESLQ EEEKDSQETD GLLPGSRPST RTPGEKSFRS KGKEKTKGGR
DGEHKAGRSV FSAMKLGKTR SHKEEPQRQD EPAVLEMEDL DHLAIRLGDG LDPDSVSLAS
VTALTSNVSN KRSKPDIKME PSAGRPMDYQ VSITVIEARQ LVGLNMDPVV CVEVGDDKKY
TSMKESTNCP YYNEYFVFDF HVSPDVMFDK IIKISVIHSK NLLRSGTLVG SFKMDVGTVY
SQPEHQFHHK WAILSDPDDI SAGLKGYVKC DVAVVGKGDN IKTPHKANET DEDDIEGNLL
LPEGVPPERQ WARFYVKIYR AEGLPRMNTS LMANVKKAFI GENKDLVDPY VQVFFAGQKG
KTSVQKSSYE PLWNEQVVFT DLFPPLCKRM KVQIRDSDKV NDVAIGTHFI DLRKISNDGD
KGFLPTLGPA WVNMYGSTRN YTLLDEHQDL NEGLGEGVSF RARLMLGLAV EILDTSNPEL
TSSTEVQVEQ ATPVSESCTG RMEEFFLFGA FLEASMIDRK NGDKPVTFEV TIGNYGNEVD
GTSRPQRPRP RKEPGDEEEV DLIQNSSDDE GDEAGDLASV SSTPPMRPQI TDRNYFHLPY
LERKPCIYIK SWWPDQRRRL YNANIMDHIA DKLEEGLNDV QEMIKTEKSY PERRLRGVLE
ELSCGCHRFL SLSDKDQGHS SRTRLDRERL KSCMRELESM GQQAKSLRAQ VKRHTVRDKL
RLCQNFLQKL RFLADEPQHS IPDVFIWMMS NNKRIAYARV PSKDLLFSIV EEELGKDCAK
VKTLFLKLPG KRGFGSAGWT VQAKLELYLW LGLSKQRKDF LCGLPCGFEE VKAAQGLGLH
SFPPISLVYT KKQTFQLRAH MYQARSLFAA DSTGLSDPFA RVFFINQSQC TEVLNETLCP
TWDQMLVFDN LELYGEAHEL RDDPPIIVIE IYDQDSMGKA DFMGRTFAKP LVKMADEAYC
PPRFPPQLEY YQIYRGNATA GDLLAAFELL QIGPSGKADL PPINGPVDMD RGPIMPVPVG
IRPVLSKYRV EVLFWGLRDL KRVNLAQVDR PRVDIECAGK GVQSSLIHNY KKNPNFNTLV
KWFEVDLPEN ELLHPPLNIR VVDCRAFGRY TLVGSHAVSS LRRFIYRPPD RSAANWNTTG
EVVVSMEPEV PVKKLETLVK LDATSDAVVK VDVAEDEKER KKKKKKGPSE EAEEEEPDES
MLDWWSKYFA SIDTMKEQLR QHETSGIDLE EKEEMDSTEG LKGPVKNKEK SRAAKEEKKK
KNQNPGPGQG SEAPEKKKAK IDELKVYPKE LESEFDNFED WLHTFNLLRG KTGDDEDGST
EEERIVGRFK GSLCVYKVPL PEDVSREAGY DPTYGMFQGI PSNDPINVLV RIYVVRATDL
HPADINGKAD PYIAIKLGKT DIRDKENYIS KQLNPVFGKS FDIEASFPME SMLTVAVYDW
DLVGTDDLIG ETKIDLENRF YSKHRATCGI AQTYSIHGYN IWRDPMKPSQ ILTRLCKEGK
VDGPHFGPHG RVKVANRVFT GPSEIEDENG QRKPTDEHVA LSALRHWEDI PRVGCRLVPE
HVETRPLLNP DKPGIEQGRL ELWVDMFPMD MPAPGTPLDI SPRKPKKYEL RVIVWNTDEV
VLEDDDFFTG EKSSDIFVRG WLKGQQEDKQ DTDVHYHSLT GEGNFNWRYL FPFDYLAAEE
KIVMSKKESM FSWDETEYKI PARLTLQIWD ADHFSADDFL GAIELDLNRF PRGAKTAKQC
TMEMATGEVD VPLVSIFKQK RVKGWWPLLA RNENDEFELT GKVEAELHLL TAEEAEKNPV
GLARNEPDPL EKPNRPDTAF VWFLNPLKSI KYLICTRYKW LIIKIVLALL GLLMLALFLY
SLPGYMVKKL LGA
