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Database: UniProt
Entry: Q64018
LinkDB: Q64018
Original site: Q64018 
ID   GLRA1_MOUSE             Reviewed;         457 AA.
AC   Q64018; Q5NCT8; Q64019; Q9R0Y6; Q9R0Y7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   11-MAY-2016, entry version 149.
DE   RecName: Full=Glycine receptor subunit alpha-1;
DE   AltName: Full=Glycine receptor 48 kDa subunit;
DE   AltName: Full=Glycine receptor strychnine-binding subunit;
DE   Flags: Precursor;
GN   Name=Glra1;
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] (ISOFORMS A AND B), VARIANT SPD SER-80, AND
RP   DISEASE.
RX   PubMed=7920629; DOI=10.1038/ng0694-131;
RA   Ryan S.G., Buckwalter M.S., Lynch J.W., Handford C.A., Segura L.,
RA   Shiang R., Wasmuth J.J., Camper S.A., Schofield P., O'Connell P.;
RT   "A missense mutation in the gene encoding the alpha 1 subunit of the
RT   inhibitory glycine receptor in the spasmodic mouse.";
RL   Nat. Genet. 7:131-135(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/cJ;
RX   PubMed=7507926;
RA   Matzenbach B., Maulet Y., Sefton L., Courtier B., Avner P.,
RA   Guenet J.-L., Betz H.;
RT   "Structural analysis of mouse glycine receptor alpha subunit genes.
RT   Identification and chromosomal localization of a novel variant.";
RL   J. Biol. Chem. 269:2607-2612(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   DISEASE.
RX   PubMed=7874121; DOI=10.1093/hmg/3.11.2025;
RA   Buckwalter M.S., Cook S.A., Davisson M.T., White W.F., Camper S.A.;
RT   "A frameshift mutation in the mouse alpha 1 glycine receptor gene
RT   (Glra1) results in progressive neurological symptoms and juvenile
RT   death.";
RL   Hum. Mol. Genet. 3:2025-2030(1994).
RN   [5]
RP   DISEASE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9145798; DOI=10.1016/S0306-4522(96)00567-2;
RA   Kling C., Koch M., Saul B., Becker C.M.;
RT   "The frameshift mutation oscillator (Glra1(spd-ot)) produces a
RT   complete loss of glycine receptor alpha1-polypeptide in mouse central
RT   nervous system.";
RL   Neuroscience 78:411-417(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12975813; DOI=10.1002/cne.10852;
RA   Haverkamp S., Mueller U., Harvey K., Harvey R.J., Betz H., Waessle H.;
RT   "Diversity of glycine receptors in the mouse retina: localization of
RT   the alpha3 subunit.";
RL   J. Comp. Neurol. 465:524-539(2003).
RN   [7]
RP   FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DISEASE.
RX   PubMed=16672662; DOI=10.1523/JNEUROSCI.3991-05.2006;
RA   Graham B.A., Schofield P.R., Sah P., Margrie T.W., Callister R.J.;
RT   "Distinct physiological mechanisms underlie altered glycinergic
RT   synaptic transmission in the murine mutants spastic, spasmodic, and
RT   oscillator.";
RL   J. Neurosci. 26:4880-4890(2006).
RN   [8]
RP   FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF ASP-108.
RX   PubMed=17114051; DOI=10.1016/j.neuron.2006.09.035;
RA   Hirzel K., Mueller U., Latal A.T., Huelsmann S., Grudzinska J.,
RA   Seeliger M.W., Betz H., Laube B.;
RT   "Hyperekplexia phenotype of glycine receptor alpha1 subunit mutant
RT   mice identifies Zn(2+) as an essential endogenous modulator of
RT   glycinergic neurotransmission.";
RL   Neuron 52:679-690(2006).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   420-LYS-LYS-421.
RX   PubMed=24801766; DOI=10.1038/npp.2014.100;
RA   Aguayo L.G., Castro P., Mariqueo T., Munoz B., Xiong W., Zhang L.,
RA   Lovinger D.M., Homanics G.E.;
RT   "Altered sedative effects of ethanol in mice with alpha1 glycine
RT   receptor subunits that are insensitive to Gbetagamma modulation.";
RL   Neuropsychopharmacology 39:2538-2548(2014).
CC   -!- FUNCTION: Glycine receptors are ligand-gated chloride channels.
CC       Channel opening is triggered by extracellular glycine
CC       (PubMed:16672662, PubMed:17114051, PubMed:24801766). Channel
CC       opening is also triggered by taurine and beta-alanine (By
CC       similarity). Channel characteristics depend on the subunit
CC       composition; heteropentameric channels are activated by lower
CC       glycine levels and display faster desensitization (By similarity).
CC       Plays an important role in the down-regulation of neuronal
CC       excitability (PubMed:9145798). Contributes to the generation of
CC       inhibitory postsynaptic currents (PubMed:16672662,
CC       PubMed:17114051, PubMed:24801766). Channel activity is potentiated
CC       by ethanol. Potentiation of channel activity by intoxicating
CC       levels ot ethanol contribute to the sedative effects of ethanol
CC       (PubMed:24801766). {ECO:0000250|UniProtKB:P23415,
CC       ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051,
CC       ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}.
CC   -!- ENZYME REGULATION: Inhibited by strychnine. Inhibited by
CC       picrotoxin (PubMed:16672662). Channel activity is enhanced by 5 uM
CC       Zn(2+) and inhibited by 100 uM Zn(2+) (PubMed:17114051).
CC       {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051}.
CC   -!- SUBUNIT: Homopentamer (in vitro). Interacts with GLRB to form
CC       heteropentameric channels; this is probably the predominant form
CC       in vivo. Heteropentamer composed of two GLRA1 and three GLRB.
CC       Heteropentamer composed of three GLRA1 and two GLRB. Both
CC       homopentamers and heteropentamers form functional ion channels,
CC       but their characteristics are subtly different.
CC       {ECO:0000250|UniProtKB:P23415}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000305|PubMed:12975813,
CC       ECO:0000305|PubMed:17114051, ECO:0000305|PubMed:24801766}; Multi-
CC       pass membrane protein {ECO:0000305}. Cell junction, synapse
CC       {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:17114051,
CC       ECO:0000269|PubMed:24801766}. Perikaryon
CC       {ECO:0000269|PubMed:24801766}. Cell projection, dendrite
CC       {ECO:0000269|PubMed:24801766}. Cell membrane
CC       {ECO:0000269|PubMed:16672662, ECO:0000305|PubMed:9145798}; Multi-
CC       pass membrane protein {ECO:0000250|UniProtKB:P23415, ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a; Synonyms=Long;
CC         IsoId=Q64018-1; Sequence=Displayed;
CC       Name=b; Synonyms=Short;
CC         IsoId=Q64018-2; Sequence=VSP_000080;
CC   -!- TISSUE SPECIFICITY: Detected in spinal cord neurons
CC       (PubMed:9145798, PubMed:17114051, PubMed:24801766). Detected in
CC       brain stem neurons (PubMed:16672662, PubMed:24801766). Detected at
CC       lower levels in hippocampus and cerebellum (PubMed:24801766).
CC       Detected in the inner plexiform layer of the retina (at protein
CC       level) (PubMed:12975813). {ECO:0000269|PubMed:12975813,
CC       ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051,
CC       ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}.
CC   -!- DOMAIN: The channel pore is formed by pentameric assembly of the
CC       second transmembrane domain from all five subunits. Channel
CC       opening is effected by an outward rotation of the transmembrane
CC       domains that increases the diameter of the pore.
CC       {ECO:0000250|UniProtKB:O93430}.
CC   -!- DISEASE: Note=Defects in Glra1 are the cause of the spasmodic
CC       (spd) phenotype, a mouse mutant which resembles the human
CC       neurological disease, hyperekplexia (or startle disease (STHE))
CC       (PubMed:7920629). Defects in Glra1 are the cause of the lethal
CC       oscillator (spd-ot) phenotype. Mutant mice display a fine motor
CC       tremor and muscle spasms that begin at 2 weeks of age and
CC       progressively worsen, resulting in death by 3 weeks of age
CC       (PubMed:7874121). Heterozygous mice show an increased acoustic
CC       startle response (PubMed:9145798). Neurons from homozygous
CC       oscillator mice have dramatically reduced amplitude and frequency
CC       of glycinergic inhibitory postsynaptic currents (PubMed:16672662).
CC       The oscillator phenotype is due to the complete absence of Glra1
CC       protein (PubMed:9145798). {ECO:0000269|PubMed:16672662,
CC       ECO:0000269|PubMed:7874121, ECO:0000269|PubMed:7920629,
CC       ECO:0000269|PubMed:9145798}.
CC   -!- MISCELLANEOUS: The alpha subunit binds strychnine.
CC       {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121,
CC       ECO:0000269|PubMed:9145798}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-
CC       subfamily. {ECO:0000305}.
DR   EMBL; S73717; AAB32157.2; -; mRNA.
DR   EMBL; S73718; AAB32158.2; -; mRNA.
DR   EMBL; X75832; CAB52398.1; -; Genomic_DNA.
DR   EMBL; X75833; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75834; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75835; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75836; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75837; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75838; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75839; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75840; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75832; CAB52399.1; -; Genomic_DNA.
DR   EMBL; X75833; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75834; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75835; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75836; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75837; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75838; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75839; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75840; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; AL596207; CAI35359.1; -; Genomic_DNA.
DR   CCDS; CCDS24715.1; -. [Q64018-2]
DR   CCDS; CCDS70190.1; -. [Q64018-1]
DR   PIR; C49970; C49970.
DR   RefSeq; NP_001277750.1; NM_001290821.1. [Q64018-1]
DR   UniGene; Mm.89320; -.
DR   ProteinModelPortal; Q64018; -.
DR   SMR; Q64018; 42-340, 418-446.
DR   STRING; 10090.ENSMUSP00000099777; -.
DR   iPTMnet; Q64018; -.
DR   PhosphoSite; Q64018; -.
DR   MaxQB; Q64018; -.
DR   PaxDb; Q64018; -.
DR   PRIDE; Q64018; -.
DR   Ensembl; ENSMUST00000075603; ENSMUSP00000075032; ENSMUSG00000000263. [Q64018-1]
DR   Ensembl; ENSMUST00000102716; ENSMUSP00000099777; ENSMUSG00000000263. [Q64018-2]
DR   GeneID; 14654; -.
DR   KEGG; mmu:14654; -.
DR   UCSC; uc007izo.2; mouse. [Q64018-1]
DR   CTD; 2741; -.
DR   MGI; MGI:95747; Glra1.
DR   eggNOG; KOG3643; Eukaryota.
DR   eggNOG; ENOG410XPWH; LUCA.
DR   GeneTree; ENSGT00760000118821; -.
DR   HOGENOM; HOG000231336; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; Q64018; -.
DR   KO; K05193; -.
DR   OMA; FNFAYGM; -.
DR   PhylomeDB; Q64018; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-MMU-975298; Ligand-gated ion channel transport.
DR   PRO; PR:Q64018; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; Q64018; -.
DR   CleanEx; MM_GLRA1; -.
DR   ExpressionAtlas; Q64018; baseline and differential.
DR   Genevisible; Q64018; MM.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0016934; F:extracellular-glycine-gated chloride channel activity; IMP:UniProtKB.
DR   GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR   GO; GO:0030977; F:taurine binding; ISS:UniProtKB.
DR   GO; GO:0022824; F:transmitter-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR   GO; GO:0001508; P:action potential; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0071361; P:cellular response to ethanol; ISS:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR   GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:UniProtKB.
DR   GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR   GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISS:UniProtKB.
DR   GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:MGI.
DR   GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
DR   GO; GO:0097305; P:response to alcohol; IMP:UniProtKB.
DR   GO; GO:0060013; P:righting reflex; IMP:MGI.
DR   GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008127; Glycine_rcpt_A.
DR   InterPro; IPR008128; Glycine_rcpt_A1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01673; GLYRALPHA.
DR   PRINTS; PR01674; GLYRALPHA1.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Chloride; Chloride channel; Complete proteome; Disease mutation;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Metal-binding;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
FT   SIGNAL        1     28       {ECO:0000250|UniProtKB:P07727}.
FT   CHAIN        29    457       Glycine receptor subunit alpha-1.
FT                                /FTId=PRO_0000000413.
FT   TOPO_DOM     29    250       Extracellular.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TRANSMEM    251    272       Helical; Name=1.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TOPO_DOM    273    277       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TRANSMEM    278    298       Helical; Name=2.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TOPO_DOM    299    309       Extracellular.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TRANSMEM    310    330       Helical; Name=3.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TOPO_DOM    331    425       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TRANSMEM    426    446       Helical; Name=4.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   TOPO_DOM    447    457       Extracellular.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   REGION      230    235       Strychnine-binding.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   METAL       220    220       Zinc. {ECO:0000250|UniProtKB:P23415}.
FT   METAL       222    222       Zinc. {ECO:0000250|UniProtKB:P23415}.
FT   METAL       243    243       Zinc. {ECO:0000250|UniProtKB:P23415}.
FT   SITE        289    289       Important for obstruction of the ion pore
FT                                in the closed conformation.
FT                                {ECO:0000250|UniProtKB:O93430}.
FT   CARBOHYD     66     66       N-linked (GlcNAc...). {ECO:0000305}.
FT   DISULFID    166    180       {ECO:0000250|UniProtKB:P23415}.
FT   DISULFID    226    237       {ECO:0000250|UniProtKB:P23415}.
FT   VAR_SEQ     354    361       Missing (in isoform b).
FT                                {ECO:0000303|PubMed:7920629}.
FT                                /FTId=VSP_000080.
FT   VARIANT      80     80       A -> S (in spd).
FT                                {ECO:0000269|PubMed:7920629}.
FT   MUTAGEN     108    108       D->A: Eliminates potentiation of glycine-
FT                                mediated currents by Zn(2+) and causes
FT                                neuromotor defects similar to human
FT                                startle disease.
FT                                {ECO:0000269|PubMed:17114051}.
FT   MUTAGEN     421    422       KK->AA: Reduces the increase of channel
FT                                activity in response to ethanol and
FT                                improves tolerance of intoxicating levels
FT                                of alcohol.
FT                                {ECO:0000269|PubMed:24801766}.
FT   CONFLICT     84     84       M -> I (in Ref. 2; CAB52398/CAB52399).
FT                                {ECO:0000305}.
FT   CONFLICT    426    429       ISRI -> NISH (in Ref. 2; CAB52398/
FT                                CAB52399). {ECO:0000305}.
SQ   SEQUENCE   457 AA;  52657 MW;  29268DC4991A6E20 CRC64;
     MYSFNTLRFY LWETIVFFSL AASKEAEAAR SAPKPMSPSD FLDKLMGRTS GYDARIRPNF
     KGPPVNVSCN IFINSFGSIA ETTMDYRVNI FLRQQWNDPR LAYNEYPDDS LDLDPSMLDS
     IWKPDLFFAN EKGAHFHEIT TDNKLLRISR NGNVLYSIRI TLTLACPMDL KNFPMDVQTC
     IMQLESFGYT MNDLIFEWQE QGAVQVADGL TLPQFILKEE KDLRYCTKHY NTGKFTCIEA
     RFHLERQMGY YLIQMYIPSL LIVILSWISF WINMDAAPAR VGLGITTVLT MTTQSSGSRA
     SLPKVSYVKA IDIWMAVCLL FVFSALLEYA AVNFVSRQHK ELLRFRRKRR HHKSPMLNLF
     QDDEGGEGRF NFSAYGMGPA CLQAKDGISV KGANNNNTTN PPPAPSKSPE EMRKLFIQRA
     KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNK
//
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