MERL_MOUSE
ID MERL_MOUSE Reviewed; 596 AA.
AC P46662; Q8BR03;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Merlin;
DE AltName: Full=Moesin-ezrin-radixin-like protein;
DE AltName: Full=Neurofibromin-2;
DE AltName: Full=Schwannomin;
GN Name=Nf2; Synonyms=Nf-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8012352; DOI=10.1093/hmg/3.3.407;
RA Haase V.H., Trofatter J.A., Maccollin M., Tarttelin E., Gusella J.F.,
RA Ramesh V.;
RT "The murine NF2 homologue encodes a highly conserved merlin protein with
RT alternative forms.";
RL Hum. Mol. Genet. 3:407-411(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7981675; DOI=10.1093/hmg/3.7.1075;
RA Huynh D.P., Nechiporuk T., Pulst S.M.;
RT "Alternative transcripts in the mouse neurofibromatosis type 2 (NF2) gene
RT are conserved and code for schwannomins with distinct C-terminal domains.";
RL Hum. Mol. Genet. 3:1075-1079(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 400-596.
RC TISSUE=Brain;
RX PubMed=8088840; DOI=10.1006/geno.1994.1291;
RA Claudio J.O., Marineau C., Rouleau G.A.;
RT "The mouse neurofibromatosis type 2 gene maps to chromosome 11.";
RL Genomics 21:437-439(1994).
RN [5]
RP INTERACTION WITH LAYN.
RX PubMed=15913605; DOI=10.1016/j.yexcr.2005.04.017;
RA Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T.,
RA Hynes R.O.;
RT "Layilin, a cell surface hyaluronan receptor, interacts with merlin and
RT radixin.";
RL Exp. Cell Res. 308:177-187(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20181838; DOI=10.1167/iovs.09-4371;
RA Wiley L.A., Dattilo L.K., Kang K.B., Giovannini M., Beebe D.C.;
RT "The tumor suppressor merlin is required for cell cycle exit, terminal
RT differentiation, and cell polarity in the developing murine lens.";
RL Invest. Ophthalmol. Vis. Sci. 51:3611-3618(2010).
CC -!- FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling
CC pathway, a signaling pathway that plays a pivotal role in tumor
CC suppression by restricting proliferation and promoting apoptosis. Along
CC with WWC1 can synergistically induce the phosphorylation of LATS1 and
CC LATS2 and can probably function in the regulation of the Hippo/SWH
CC (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing
CC protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its
CC stimulating activity. Suppresses cell proliferation and tumorigenesis
CC by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein
CC ligase complex (By similarity). Plays a role in lens development and is
CC required for complete fiber cell terminal differentiation, maintenance
CC of cell polarity and separation of the lens vesicle from the corneal
CC epithelium. {ECO:0000250|UniProtKB:P35240,
CC ECO:0000269|PubMed:20181838}.
CC -!- SUBUNIT: Interacts with SLC9A3R1, HGS and AGAP2. Interacts with SGSM3.
CC Interacts (via FERM domain) with MPP1 (By similarity). Interacts with
CC LAYN (PubMed:15913605). Interacts with WWC1. Interacts with the CUL4A-
CC RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The
CC unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1.
CC Interacts (via FERM domain) with NOP53; the interaction is direct (By
CC similarity). Interacts with SCHIP1; the interaction is direct (By
CC similarity). {ECO:0000250|UniProtKB:P35240,
CC ECO:0000269|PubMed:15913605}.
CC -!- INTERACTION:
CC P46662; Q4VCS5: AMOT; Xeno; NbExp=2; IntAct=EBI-644586, EBI-2511319;
CC P46662; O95835: LATS1; Xeno; NbExp=5; IntAct=EBI-644586, EBI-444209;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Colocalizes with MPP1 in non-myelin-forming Schwann
CC cells. Binds with DCAF1 in the nucleus. The intramolecular association
CC of the FERM domain with the C-terminal tail promotes nuclear
CC accumulation. The unphosphorylated form accumulates predominantly in
CC the nucleus while the phosphorylated form is largely confined to the
CC non-nuclear fractions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P46662-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46662-2; Sequence=VSP_000493;
CC -!- PTM: Phosphorylation of Ser-518 inhibits nuclear localization by
CC disrupting the intramolecular association of the FERM domain with the
CC C-terminal tail. The dephosphorylation of Ser-518 favors the
CC interaction with NOP53. {ECO:0000250|UniProtKB:P35240}.
CC -!- PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-
CC protein ligase complex for ubiquitination and subsequent proteasome-
CC dependent degradation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are born with abnormally small lenses with
CC serious structural defects. Failure of lens vesicle separation and the
CC resulting changes in cell organization causes lenses to herniate,
CC leading to expulsion of lens fiber cells through a perforation in the
CC cornea. Developing lenses show loss of cell apical-basal polarity,
CC failure of the lens vesicle to separate from the surface ectoderm,
CC failure to properly exit the cell cycle during fiber cell
CC differentiation and incomplete terminal differentiation of fiber cells.
CC {ECO:0000269|PubMed:20181838}.
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DR EMBL; X74671; CAA52737.1; -; mRNA.
DR EMBL; L27105; AAA39807.1; -; mRNA.
DR EMBL; L27090; AAA63648.1; -; mRNA.
DR EMBL; L28176; AAA39808.1; -; mRNA.
DR EMBL; AK045998; BAC32567.1; -; mRNA.
DR EMBL; X75759; CAA53386.1; -; mRNA.
DR CCDS; CCDS24391.1; -. [P46662-1]
DR CCDS; CCDS56757.1; -. [P46662-2]
DR PIR; I48683; I48683.
DR PIR; I54368; I54368.
DR PIR; I68664; I68664.
DR RefSeq; NP_001239179.1; NM_001252250.1. [P46662-2]
DR RefSeq; NP_001239180.1; NM_001252251.1. [P46662-2]
DR RefSeq; NP_001239181.1; NM_001252252.1.
DR RefSeq; NP_001239182.1; NM_001252253.1.
DR RefSeq; NP_035028.2; NM_010898.4. [P46662-1]
DR RefSeq; XP_006514633.1; XM_006514570.2. [P46662-2]
DR RefSeq; XP_011241971.1; XM_011243669.2. [P46662-2]
DR PDB; 1ISN; X-ray; 2.90 A; A=18-340.
DR PDB; 3WA0; X-ray; 2.31 A; A/B/C/D/E/F=19-314.
DR PDB; 4P7I; X-ray; 2.60 A; A/B=1-313.
DR PDB; 4ZRK; X-ray; 2.32 A; A/B/C/D=1-320.
DR PDBsum; 1ISN; -.
DR PDBsum; 3WA0; -.
DR PDBsum; 4P7I; -.
DR PDBsum; 4ZRK; -.
DR AlphaFoldDB; P46662; -.
DR SMR; P46662; -.
DR BioGRID; 201737; 15.
DR IntAct; P46662; 10.
DR MINT; P46662; -.
DR STRING; 10090.ENSMUSP00000105536; -.
DR iPTMnet; P46662; -.
DR PhosphoSitePlus; P46662; -.
DR EPD; P46662; -.
DR jPOST; P46662; -.
DR PaxDb; P46662; -.
DR PRIDE; P46662; -.
DR ProteomicsDB; 295856; -. [P46662-1]
DR ProteomicsDB; 295857; -. [P46662-2]
DR Antibodypedia; 319; 683 antibodies from 44 providers.
DR DNASU; 18016; -.
DR Ensembl; ENSMUST00000053079; ENSMUSP00000055033; ENSMUSG00000009073. [P46662-2]
DR Ensembl; ENSMUST00000056290; ENSMUSP00000055061; ENSMUSG00000009073. [P46662-2]
DR Ensembl; ENSMUST00000109910; ENSMUSP00000105536; ENSMUSG00000009073. [P46662-1]
DR GeneID; 18016; -.
DR KEGG; mmu:18016; -.
DR UCSC; uc007hvf.2; mouse. [P46662-1]
DR UCSC; uc007hvg.2; mouse. [P46662-2]
DR CTD; 4771; -.
DR MGI; MGI:97307; Nf2.
DR VEuPathDB; HostDB:ENSMUSG00000009073; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01020000230354; -.
DR HOGENOM; CLU_003623_6_1_1; -.
DR InParanoid; P46662; -.
DR OMA; KERVDYW; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; P46662; -.
DR TreeFam; TF313935; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 18016; 20 hits in 79 CRISPR screens.
DR ChiTaRS; Nf2; mouse.
DR EvolutionaryTrace; P46662; -.
DR PRO; PR:P46662; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P46662; protein.
DR Bgee; ENSMUSG00000009073; Expressed in gastrula and 282 other tissues.
DR ExpressionAtlas; P46662; baseline and differential.
DR Genevisible; P46662; MM.
DR GO; GO:0005912; C:adherens junction; IMP:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IMP:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IMP:MGI.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0033687; P:osteoblast proliferation; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0014013; P:regulation of gliogenesis; IMP:MGI.
DR GO; GO:0035330; P:regulation of hippo signaling; ISO:MGI.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0014010; P:Schwann cell proliferation; IMP:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..596
FT /note="Merlin"
FT /id="PRO_0000219413"
FT DOMAIN 22..311
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 560..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35240"
FT MOD_RES 518
FT /note="Phosphoserine; by PAK"
FT /evidence="ECO:0000250|UniProtKB:P35240"
FT VAR_SEQ 581..596
FT /note="LTLQSAKSRVAFFEEL -> PQAQGRRPICI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_000493"
FT CONFLICT 475
FT /note="I -> T (in Ref. 2; AAA39808)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="R -> A (in Ref. 1; AAA39807/AAA63648)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="G -> A (in Ref. 2; AAA39808)"
FT /evidence="ECO:0000305"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4ZRK"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:3WA0"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:3WA0"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:3WA0"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:3WA0"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:3WA0"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3WA0"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1ISN"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:3WA0"
FT HELIX 316..337
FT /evidence="ECO:0007829|PDB:1ISN"
SQ SEQUENCE 596 AA; 69776 MW; 8D06F557E3435851 CRC64;
MAGAIASRMS FSSLKRKQPK TFTVRIVTMD AEMEFNCEMK WKGKDLFDLV CRTLGLRETW
FFGLQYTIKD TVAWLKMDKK VLDHDVSKEE PVTFHFLAKF YPENAEEELV QEITQHLFFL
QVKKQILDEK VYCPPEASVL LASYAVQAKY GDYDPSVHKR GFLAQEELLP KRVINLYQMT
PEMWEERITA WYAEHRGRAR DEAEMEYLKI AQDLEMYGVN YFTIRNKKGT ELLLGVDALG
LHIYDPENRL TPKISFPWNE IRNISYSDKE FTIKPLDKKI DVFKFNSSKL RVNKLILQLC
IGNHDLFMRR RKADSLEVQQ MKAQAREEKA RKQMERQRLA REKQMREEAE RTRDELERRL
LQMKEEATMA NEALMRSEET ADLLAEKAQI TEEEAKLLAQ KAAEAEQEMQ RIKATAIRTE
EEKRLMEQKV LEAEVLALKM AEESERRAKE ADQLKQDLQE AREAERRAKQ KLLEIATKPT
YPPMNPIPPP LPPDIPSFDI IADSLSFDFK DTDMKRLSME IEKEKVEYME KSKHLQEQLN
ELKTEIEALK LKERETALDV LHSESSDRGG PSSKHNTIKK LTLQSAKSRV AFFEEL
