(data stored in ACNUC9306 zone)

SWISSPROT: 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   11-DEC-2019, entry version 177.
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       Q4VCS5:AMOT (xeno); NbExp=2; IntAct=EBI-644586, EBI-2511319;
CC       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}.
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   SMR; P46662; -.
DR   BioGrid; 201737; 5.
DR   IntAct; P46662; 9.
DR   STRING; 10090.ENSMUSP00000105536; -.
DR   iPTMnet; P46662; -.
DR   PhosphoSitePlus; P46662; -.
DR   EPD; P46662; -.
DR   jPOST; P46662; -.
DR   PaxDb; P46662; -.
DR   PRIDE; P46662; -.
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   eggNOG; KOG3529; Eukaryota.
DR   eggNOG; ENOG410XQFP; LUCA.
DR   GeneTree; ENSGT00960000186596; -.
DR   HOGENOM; HOG000007113; -.
DR   InParanoid; P46662; -.
DR   KO; K16684; -.
DR   OMA; PRQKTYL; -.
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   ChiTaRS; Nf2; mouse.
DR   EvolutionaryTrace; P46662; -.
DR   PRO; PR:P46662; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P46662; protein.
DR   Bgee; ENSMUSG00000009073; Expressed in 314 organ(s), highest expression level in submandibular gland.
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: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: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: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: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; ISO:MGI.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.1020; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C_dom.
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   Pfam; PF00769; ERM; 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;
DR   PRODOM; P46662.
DR   SWISS-2DPAGE; P46662.
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   COMPBIAS        327..465
FT                   /note="Glu-rich"
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:0000244|PDB:3WA0"
FT   STRAND          32..34
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           43..54
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           59..61
FT                   /evidence="ECO:0000244|PDB:4ZRK"
FT   STRAND          62..68
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          71..74
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          77..80
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           81..83
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          84..86
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          89..91
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          93..100
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           105..108
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           112..127
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           135..150
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   TURN            155..157
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   TURN            160..165
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           171..175
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           181..193
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   TURN            194..197
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           200..211
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   TURN            215..218
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          220..226
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          231..237
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          240..244
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          249..251
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          253..257
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           258..260
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          261..267
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   STRAND          270..277
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   TURN            278..280
FT                   /evidence="ECO:0000244|PDB:1ISN"
FT   STRAND          283..286
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           290..310
FT                   /evidence="ECO:0000244|PDB:3WA0"
FT   HELIX           316..337
FT                   /evidence="ECO:0000244|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
//

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