GenomeNet

Database: UniProt
Entry: P46662
LinkDB: P46662
Original site: P46662 
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   29-OCT-2014, entry version 133.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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
RT   with 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)
RT   gene are conserved and code for schwannomins with distinct C-terminal
RT   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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   and radixin.";
RL   Exp. Cell Res. 308:177-187(2005).
RN   [6]
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)
CC       signaling pathway, a signaling pathway that plays a pivotal role
CC       in tumor suppression by restricting proliferation and promoting
CC       apoptosis. Along with WWC1 can synergistically induce the
CC       phosphorylation of LATS1 and LATS2 and can probably function in
CC       the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway.
CC       May act as a membrane stabilizing protein. May inhibit PI3 kinase
CC       by binding to AGAP2 and impairing its stimulating activity.
CC       Suppresses cell proliferation and tumorigenesis by inhibiting the
CC       CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex
CC       (By similarity). Plays a role in lens development and is required
CC       for complete fiber cell terminal differentiation, maintenance of
CC       cell polarity and separation of the lens vesicle from the corneal
CC       epithelium. {ECO:0000250, ECO:0000269|PubMed:20181838}.
CC   -!- SUBUNIT: Interacts with SLC9A3R1, HGS and AGAP2. Interacts with
CC       SGSM3. Interacts (via FERM domain) with MPP1 (By similarity).
CC       Interacts with LAYN and WWC1. Interacts with the CUL4A-RBX1-DDB1-
CC       VprBP/DCAF1 E3 ubiquitin-protein ligase complex. The
CC       unphosphorylated form interacts (via FERM domain) with VPRBP/DCAF1
CC       (By similarity). {ECO:0000250}.
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
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Cell projection {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with MPP1
CC       in non-myelin-forming Schwann cells. Binds with VPRBP in the
CC       nucleus. The intramolecular association of the FERM domain with
CC       the C-terminal tail promotes nuclear accumulation. The
CC       unphosphorylated form accumulates predominantly in the nucleus
CC       while the phosphorylated form is largely confined to the non-
CC       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
CC       the C-terminal tail. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3
CC       ubiquitin-protein ligase complex for ubiquitination and subsequent
CC       proteasome-dependent degradation. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice are born with abnormally small lenses
CC       with serious structural defects. Failure of lens vesicle
CC       separation and the resulting changes in cell organization causes
CC       lenses to herniate, leading to expulsion of lens fiber cells
CC       through a perforation in the cornea. Developing lenses show loss
CC       of cell apical-basal polarity, failure of the lens vesicle to
CC       separate from the surface ectoderm, failure to properly exit the
CC       cell cycle during fiber cell differentiation and incomplete
CC       terminal differentiation of fiber cells.
CC       {ECO:0000269|PubMed:20181838}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
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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_006514570.1. [P46662-2]
DR   UniGene; Mm.297109; -.
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   PDBsum; 1ISN; -.
DR   PDBsum; 3WA0; -.
DR   PDBsum; 4P7I; -.
DR   ProteinModelPortal; P46662; -.
DR   SMR; P46662; 18-382.
DR   BioGrid; 201737; 4.
DR   IntAct; P46662; 8.
DR   MINT; MINT-242068; -.
DR   PhosphoSite; P46662; -.
DR   MaxQB; 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   CTD; 4771; -.
DR   MGI; MGI:97307; Nf2.
DR   eggNOG; NOG328202; -.
DR   GeneTree; ENSGT00760000119078; -.
DR   HOGENOM; HOG000007113; -.
DR   HOVERGEN; HBG002185; -.
DR   InParanoid; P46662; -.
DR   KO; K16684; -.
DR   OMA; ITNEMER; -.
DR   OrthoDB; EOG7BGHK6; -.
DR   PhylomeDB; P46662; -.
DR   TreeFam; TF313935; -.
DR   ChiTaRS; NF2; mouse.
DR   EvolutionaryTrace; P46662; -.
DR   NextBio; 293053; -.
DR   PRO; PR:P46662; -.
DR   Bgee; P46662; -.
DR   CleanEx; MM_NF2; -.
DR   ExpressionAtlas; P46662; baseline and differential.
DR   Genevestigator; P46662; -.
DR   GO; GO:0005912; C:adherens junction; IMP:MGI.
DR   GO; GO:0045177; C:apical part of cell; 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:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
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:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0008156; P:negative regulation of DNA replication; IEA:Ensembl.
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:0042518; P:negative regulation of tyrosine phosphorylation of Stat3 protein; IEA:Ensembl.
DR   GO; GO:0042524; P:negative regulation of tyrosine phosphorylation of Stat5 protein; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0035330; P:regulation of hippo signaling; IEA:Ensembl.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; 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:0014010; P:Schwann cell proliferation; IEA:Ensembl.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C_dom.
DR   InterPro; IPR000798; Ez/rad/moesin_like.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
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   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   Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Tumor suppressor; Ubl conjugation.
FT   CHAIN         1    596       Merlin.
FT                                /FTId=PRO_0000219413.
FT   DOMAIN       22    311       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
FT   COMPBIAS    327    465       Glu-rich.
FT   MOD_RES     518    518       Phosphoserine; by PAK. {ECO:0000250}.
FT   VAR_SEQ     581    596       LTLQSAKSRVAFFEEL -> PQAQGRRPICI (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_000493.
FT   CONFLICT    475    475       I -> T (in Ref. 2; AAA39808).
FT                                {ECO:0000305}.
FT   CONFLICT    554    554       R -> A (in Ref. 1; AAA39807/AAA63648).
FT                                {ECO:0000305}.
FT   CONFLICT    570    570       G -> A (in Ref. 2; AAA39808).
FT                                {ECO:0000305}.
FT   STRAND       25     27       {ECO:0000244|PDB:3WA0}.
FT   STRAND       32     34       {ECO:0000244|PDB:3WA0}.
FT   HELIX        43     54       {ECO:0000244|PDB:3WA0}.
FT   HELIX        59     61       {ECO:0000244|PDB:4P7I}.
FT   STRAND       62     68       {ECO:0000244|PDB:3WA0}.
FT   STRAND       71     74       {ECO:0000244|PDB:3WA0}.
FT   STRAND       77     80       {ECO:0000244|PDB:3WA0}.
FT   HELIX        81     83       {ECO:0000244|PDB:3WA0}.
FT   STRAND       84     86       {ECO:0000244|PDB:3WA0}.
FT   STRAND       89     91       {ECO:0000244|PDB:3WA0}.
FT   STRAND       93    100       {ECO:0000244|PDB:3WA0}.
FT   HELIX       105    108       {ECO:0000244|PDB:3WA0}.
FT   HELIX       112    127       {ECO:0000244|PDB:3WA0}.
FT   HELIX       135    150       {ECO:0000244|PDB:3WA0}.
FT   TURN        155    157       {ECO:0000244|PDB:3WA0}.
FT   TURN        160    165       {ECO:0000244|PDB:3WA0}.
FT   HELIX       171    175       {ECO:0000244|PDB:3WA0}.
FT   HELIX       181    193       {ECO:0000244|PDB:3WA0}.
FT   TURN        194    197       {ECO:0000244|PDB:3WA0}.
FT   HELIX       200    211       {ECO:0000244|PDB:3WA0}.
FT   TURN        215    218       {ECO:0000244|PDB:3WA0}.
FT   STRAND      220    226       {ECO:0000244|PDB:3WA0}.
FT   STRAND      231    237       {ECO:0000244|PDB:3WA0}.
FT   STRAND      240    244       {ECO:0000244|PDB:3WA0}.
FT   STRAND      249    251       {ECO:0000244|PDB:3WA0}.
FT   STRAND      253    257       {ECO:0000244|PDB:3WA0}.
FT   HELIX       258    260       {ECO:0000244|PDB:3WA0}.
FT   STRAND      261    267       {ECO:0000244|PDB:3WA0}.
FT   STRAND      270    277       {ECO:0000244|PDB:3WA0}.
FT   TURN        278    280       {ECO:0000244|PDB:1ISN}.
FT   STRAND      283    286       {ECO:0000244|PDB:3WA0}.
FT   HELIX       290    310       {ECO:0000244|PDB:3WA0}.
FT   HELIX       316    337       {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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