GenomeNet

Database: UniProt/SWISS-PROT
Entry: DCE1_HUMAN
LinkDB: DCE1_HUMAN
Original site: DCE1_HUMAN 
ID   DCE1_HUMAN              Reviewed;         594 AA.
AC   Q99259; Q49AK1; Q53TQ7; Q9BU91; Q9UHH4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-OCT-2017, entry version 175.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
DE   AltName: Full=67 kDa glutamic acid decarboxylase;
DE            Short=GAD-67;
DE   AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN   Name=GAD1; Synonyms=GAD, GAD67;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=1549570; DOI=10.1073/pnas.89.6.2115;
RA   Bu D.-F., Erlander M.G., Hitz B.C., Tillakaratne N.J., Kaufman D.L.,
RA   Wagner-Mcpherson C.B., Evans G.A., Tobin A.J.;
RT   "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are
RT   each encoded by a single gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2115-2119(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8088791; DOI=10.1006/geno.1994.1246;
RA   Bu D.-F., Tobin A.J.;
RT   "The exon-intron organization of the genes (GAD1 and GAD2) encoding
RT   two human glutamate decarboxylases (GAD67 and GAD65) suggests that
RT   they derive from a common ancestral GAD.";
RL   Genomics 21:222-228(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1683462; DOI=10.1016/0140-6736(91)92780-6;
RA   Kelly C.D., Carter N.D., Johnstone A.P., Nussey S.S.;
RT   "Cloning of large isoform of human brain glutamic acid
RT   decarboxylase.";
RL   Lancet 338:1468-1469(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=1339255; DOI=10.1111/j.1469-1809.1992.tb01150.x;
RA   Kelly C.D., Edwards Y., Johnstone A.P., Harfst E., Nogradi A.,
RA   Nussey S.S., Povey S., Carter N.D.;
RT   "Nucleotide sequence and chromosomal assignment of a cDNA encoding the
RT   large isoform of human glutamate decarboxylase.";
RL   Ann. Hum. Genet. 56:255-265(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8507202; DOI=10.1006/bbrc.1993.1564;
RA   Yamashita K., Cram D.S., Harrison L.C.;
RT   "Molecular cloning of full-length glutamic acid decarboxylase 67 from
RT   human pancreas and islets.";
RL   Biochem. Biophys. Res. Commun. 192:1347-1352(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=8507203; DOI=10.1006/bbrc.1993.1565;
RA   Kawasaki E., Moriuchi R., Watanabe M., Saitoh K., Brunicardi F.C.,
RA   Watt P.C., Yamaguchi T., Mullen Y., Akazawa S., Miyamoto T.;
RT   "Cloning and expression of large isoform of glutamic acid
RT   decarboxylase from human pancreatic islet.";
RL   Biochem. Biophys. Res. Commun. 192:1353-1359(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Giorda R., Peakman M., Vergani D., Trucco M.;
RT   "Sequence of glutamic acid decarboxylase transcripts in human
RT   pancreatic islets and brain.";
RL   Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC   TISSUE=Pancreatic islet, and Testis;
RX   PubMed=10671565; DOI=10.1074/jbc.275.7.5188;
RA   Chessler S.D., Lernmark A.;
RT   "Alternative splicing of GAD67 results in the synthesis of a third
RT   form of glutamic-acid decarboxylase in human islets and other non-
RT   neural tissues.";
RL   J. Biol. Chem. 275:5188-5192(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-228 AND GLN-532.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 218-397.
RC   TISSUE=Brain;
RX   PubMed=2039509; DOI=10.1016/0006-291X(91)90418-7;
RA   Cram D.S., Barnett L.D., Joseph J.L., Harrison L.C.;
RT   "Cloning and partial nucleotide sequence of human glutamic acid
RT   decarboxylase cDNA from brain and pancreatic islets.";
RL   Biochem. Biophys. Res. Commun. 176:1239-1244(1991).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 527-594.
RC   TISSUE=Testis;
RX   PubMed=1697032; DOI=10.1128/MCB.10.9.4701;
RA   Persson H., Pelto-Huikko M., Metsis M., Soeder O., Brene S., Skog S.,
RA   Hoekfelt T., Ritzen E.M.;
RT   "Expression of the neurotransmitter-synthesizing enzyme glutamic acid
RT   decarboxylase in male germ cells.";
RL   Mol. Cell. Biol. 10:4701-4711(1990).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-594 IN COMPLEX WITH
RP   SUBSTRATE ANALOG, SUBUNIT, AND COFACTOR.
RX   PubMed=17384644; DOI=10.1038/nsmb1228;
RA   Fenalti G., Law R.H.P., Buckle A.M., Langendorf C., Tuck K.,
RA   Rosado C.J., Faux N.G., Mahmood K., Hampe C.S., Banga J.P., Wilce M.,
RA   Schmidberger J., Rossjohn J., El-Kabbani O., Pike R.N., Smith A.I.,
RA   Mackay I.R., Rowley M.J., Whisstock J.C.;
RT   "GABA production by glutamic acid decarboxylase is regulated by a
RT   dynamic catalytic loop.";
RL   Nat. Struct. Mol. Biol. 14:280-286(2007).
RN   [16]
RP   VARIANT CPSQ1 CYS-12.
RX   PubMed=15571623; DOI=10.1186/1471-2377-4-20;
RA   Lynex C.N., Carr I.M., Leek J.P., Achuthan R., Mitchell S.,
RA   Maher E.R., Woods C.G., Bonthon D.T., Markham A.F.;
RT   "Homozygosity for a missense mutation in the 67 kDa isoform of
RT   glutamate decarboxylase in a family with autosomal recessive spastic
RT   cerebral palsy: parallels with Stiff-Person Syndrome and other
RT   movement disorders.";
RL   BMC Neurol. 4:20-20(2004).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:17384644};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17384644}.
CC   -!- INTERACTION:
CC       Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-743184, EBI-741181;
CC       Q96DZ9:CMTM5; NbExp=4; IntAct=EBI-743184, EBI-2548702;
CC       Q96DZ9-2:CMTM5; NbExp=4; IntAct=EBI-743184, EBI-11522780;
CC       P46952:HAAO; NbExp=6; IntAct=EBI-743184, EBI-743215;
CC       P16333:NCK1; NbExp=2; IntAct=EBI-743184, EBI-389883;
CC       Q13188:STK3; NbExp=3; IntAct=EBI-743184, EBI-992580;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=GAD67;
CC         IsoId=Q99259-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99259-2; Sequence=Not described;
CC       Name=3; Synonyms=GAD25;
CC         IsoId=Q99259-3; Sequence=VSP_009123, VSP_009124;
CC         Note=Lacks enzymatic activity.;
CC       Name=4;
CC         IsoId=Q99259-4; Sequence=VSP_054473, VSP_054474;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Isoform 3 is expressed in pancreatic islets,
CC       testis, adrenal cortex, and perhaps other endocrine tissues, but
CC       not in brain. {ECO:0000269|PubMed:10671565}.
CC   -!- DISEASE: Cerebral palsy, spastic quadriplegic 1 (CPSQ1)
CC       [MIM:603513]: A non-progressive disorder of movement and/or
CC       posture resulting from defects in the developing central nervous
CC       system. Affected individuals manifest symmetrical, non-progressive
CC       spasticity and no adverse perinatal history or obvious underlying
CC       alternative diagnosis. Developmental delay, mental retardation and
CC       sometimes epilepsy can be part of the clinical picture.
CC       {ECO:0000269|PubMed:15571623}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/gad1/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Glutamate decarboxylase entry;
CC       URL="https://en.wikipedia.org/wiki/Glutamate_decarboxylase";
DR   EMBL; M81883; AAA62368.1; -; mRNA.
DR   EMBL; L16888; AAB59427.1; -; mRNA.
DR   EMBL; Z22750; CAA80435.1; -; mRNA.
DR   EMBL; S61897; AAB26937.1; -; mRNA.
DR   EMBL; S61898; AAB26938.1; -; mRNA.
DR   EMBL; M86522; AAA35900.1; -; Genomic_DNA.
DR   EMBL; AF178853; AAF18390.2; -; mRNA.
DR   EMBL; AY337516; AAP88035.1; -; Genomic_DNA.
DR   EMBL; AC007405; AAY24237.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11228.1; -; Genomic_DNA.
DR   EMBL; CH471058; EAX11229.1; -; Genomic_DNA.
DR   EMBL; BC002815; AAH02815.1; -; mRNA.
DR   EMBL; BC026349; AAH26349.1; -; mRNA.
DR   EMBL; BC036552; AAH36552.1; -; mRNA.
DR   EMBL; M70434; AAA52512.1; -; mRNA.
DR   EMBL; M55574; AAA72938.1; -; mRNA.
DR   CCDS; CCDS2239.1; -. [Q99259-1]
DR   CCDS; CCDS2240.1; -. [Q99259-3]
DR   PIR; B41935; B41935.
DR   PIR; S48135; S48135.
DR   PIR; S51775; S51775.
DR   PIR; S51776; S51776.
DR   RefSeq; NP_000808.2; NM_000817.2. [Q99259-1]
DR   RefSeq; NP_038473.2; NM_013445.3. [Q99259-3]
DR   RefSeq; XP_005246501.1; XM_005246444.2. [Q99259-3]
DR   RefSeq; XP_011509224.1; XM_011510922.1. [Q99259-1]
DR   RefSeq; XP_016859245.1; XM_017003756.1. [Q99259-1]
DR   RefSeq; XP_016859247.1; XM_017003758.1. [Q99259-3]
DR   UniGene; Hs.420036; -.
DR   PDB; 2OKJ; X-ray; 2.30 A; A/B=93-594.
DR   PDB; 3VP6; X-ray; 2.10 A; A/B=90-594.
DR   PDBsum; 2OKJ; -.
DR   PDBsum; 3VP6; -.
DR   ProteinModelPortal; Q99259; -.
DR   SMR; Q99259; -.
DR   BioGrid; 108845; 10.
DR   DIP; DIP-29292N; -.
DR   IntAct; Q99259; 10.
DR   MINT; MINT-3058814; -.
DR   STRING; 9606.ENSP00000350928; -.
DR   ChEMBL; CHEMBL2614; -.
DR   DrugBank; DB00142; L-Glutamic Acid.
DR   DrugBank; DB00114; Pyridoxal Phosphate.
DR   iPTMnet; Q99259; -.
DR   PhosphoSitePlus; Q99259; -.
DR   BioMuta; GAD1; -.
DR   DMDM; 1352213; -.
DR   EPD; Q99259; -.
DR   PaxDb; Q99259; -.
DR   PeptideAtlas; Q99259; -.
DR   PRIDE; Q99259; -.
DR   DNASU; 2571; -.
DR   Ensembl; ENST00000344257; ENSP00000341167; ENSG00000128683. [Q99259-3]
DR   Ensembl; ENST00000358196; ENSP00000350928; ENSG00000128683. [Q99259-1]
DR   Ensembl; ENST00000375272; ENSP00000364421; ENSG00000128683. [Q99259-3]
DR   Ensembl; ENST00000493875; ENSP00000434696; ENSG00000128683. [Q99259-4]
DR   Ensembl; ENST00000625689; ENSP00000486612; ENSG00000128683. [Q99259-4]
DR   GeneID; 2571; -.
DR   KEGG; hsa:2571; -.
DR   UCSC; uc002ugh.4; human. [Q99259-1]
DR   CTD; 2571; -.
DR   DisGeNET; 2571; -.
DR   EuPathDB; HostDB:ENSG00000128683.13; -.
DR   GeneCards; GAD1; -.
DR   HGNC; HGNC:4092; GAD1.
DR   HPA; CAB004415; -.
DR   HPA; CAB078176; -.
DR   HPA; HPA031949; -.
DR   HPA; HPA058412; -.
DR   MalaCards; GAD1; -.
DR   MIM; 603513; phenotype.
DR   MIM; 605363; gene.
DR   neXtProt; NX_Q99259; -.
DR   OpenTargets; ENSG00000128683; -.
DR   Orphanet; 210141; Inherited congenital spastic tetraplegia.
DR   PharmGKB; PA28507; -.
DR   eggNOG; KOG0629; Eukaryota.
DR   eggNOG; COG0076; LUCA.
DR   GeneTree; ENSGT00760000119205; -.
DR   HOGENOM; HOG000005382; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; Q99259; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; EOG091G07ZU; -.
DR   PhylomeDB; Q99259; -.
DR   TreeFam; TF314688; -.
DR   BioCyc; MetaCyc:HS05215-MONOMER; -.
DR   BRENDA; 4.1.1.15; 2681.
DR   Reactome; R-HSA-888568; GABA synthesis.
DR   Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR   SIGNOR; Q99259; -.
DR   ChiTaRS; GAD1; human.
DR   EvolutionaryTrace; Q99259; -.
DR   GenomeRNAi; 2571; -.
DR   PRO; PR:Q99259; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000128683; -.
DR   CleanEx; HS_GAD1; -.
DR   ExpressionAtlas; Q99259; baseline and differential.
DR   Genevisible; Q99259; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
DR   GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR   GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0012506; C:vesicle membrane; NAS:UniProtKB.
DR   GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006538; P:glutamate catabolic process; TAS:UniProtKB.
DR   GO; GO:0006540; P:glutamate decarboxylation to succinate; TAS:ProtInc.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
DR   GO; GO:0018352; P:protein-pyridoxal-5-phosphate linkage; TAS:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Decarboxylase;
KW   Disease mutation; Lyase; Neurotransmitter biosynthesis;
KW   Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    594       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146963.
FT   REGION      190    192       Substrate binding.
FT   BINDING     567    567       Substrate.
FT   MOD_RES      78     78       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P48318}.
FT   MOD_RES     405    405       N6-(pyridoxal phosphate)lysine.
FT   VAR_SEQ     214    224       FTYEIAPVFVL -> PSDMRECWLLR (in isoform
FT                                3). {ECO:0000303|PubMed:10671565,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_009123.
FT   VAR_SEQ     225    594       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10671565,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_009124.
FT   VAR_SEQ     374    425       AAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCS
FT                                AILVKEKGILQ -> GFNFSQLANRIICLATELMTNKGCVT
FT                                WHPNYSVNMHHGCLGRWAAHVQEAPP (in isoform
FT                                4). {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054473.
FT   VAR_SEQ     426    594       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_054474.
FT   VARIANT      12     12       S -> C (in CPSQ1; dbSNP:rs121918345).
FT                                {ECO:0000269|PubMed:15571623}.
FT                                /FTId=VAR_031021.
FT   VARIANT     228    228       I -> L (in dbSNP:rs45566933).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_018861.
FT   VARIANT     474    474       V -> G (in dbSNP:rs769403).
FT                                /FTId=VAR_011882.
FT   VARIANT     532    532       R -> Q (in dbSNP:rs769402).
FT                                {ECO:0000269|Ref.9}.
FT                                /FTId=VAR_011883.
FT   VARIANT     565    565       F -> L (in dbSNP:rs1049736).
FT                                /FTId=VAR_011884.
FT   CONFLICT      9      9       Missing (in Ref. 7; AAA35900).
FT                                {ECO:0000305}.
FT   CONFLICT     16     17       GA -> EP (in Ref. 4; AAB59427/CAA80435).
FT                                {ECO:0000305}.
FT   CONFLICT     17     17       A -> Q (in Ref. 7; AAA35900).
FT                                {ECO:0000305}.
FT   CONFLICT     18     18       D -> N (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT     31     31       T -> N (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT     68     68       K -> R (in Ref. 2; AAA62368).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       F -> L (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT    136    136       T -> A (in Ref. 7; AAA35900).
FT                                {ECO:0000305}.
FT   CONFLICT    140    140       D -> E (in Ref. 7; AAA35900).
FT                                {ECO:0000305}.
FT   CONFLICT    142    142       H -> R (in Ref. 7; AAA35900).
FT                                {ECO:0000305}.
FT   CONFLICT    155    155       N -> T (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT    206    206       T -> N (in Ref. 4; AAB59427/CAA80435).
FT                                {ECO:0000305}.
FT   CONFLICT    302    302       G -> C (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT    436    436       F -> L (in Ref. 5; AAB26937).
FT                                {ECO:0000305}.
FT   CONFLICT    477    477       E -> G (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT    492    492       A -> G (in Ref. 6; AAB26938).
FT                                {ECO:0000305}.
FT   CONFLICT    512    512       N -> S (in Ref. 5; AAB26937).
FT                                {ECO:0000305}.
FT   TURN         94     97       {ECO:0000244|PDB:2OKJ}.
FT   HELIX       100    102       {ECO:0000244|PDB:3VP6}.
FT   HELIX       110    131       {ECO:0000244|PDB:3VP6}.
FT   HELIX       144    149       {ECO:0000244|PDB:3VP6}.
FT   HELIX       165    177       {ECO:0000244|PDB:3VP6}.
FT   STRAND      187    192       {ECO:0000244|PDB:3VP6}.
FT   HELIX       197    209       {ECO:0000244|PDB:3VP6}.
FT   STRAND      212    214       {ECO:0000244|PDB:2OKJ}.
FT   TURN        216    218       {ECO:0000244|PDB:3VP6}.
FT   HELIX       220    237       {ECO:0000244|PDB:3VP6}.
FT   STRAND      241    243       {ECO:0000244|PDB:3VP6}.
FT   STRAND      245    251       {ECO:0000244|PDB:3VP6}.
FT   HELIX       252    267       {ECO:0000244|PDB:3VP6}.
FT   HELIX       270    274       {ECO:0000244|PDB:3VP6}.
FT   HELIX       276    278       {ECO:0000244|PDB:3VP6}.
FT   STRAND      282    287       {ECO:0000244|PDB:3VP6}.
FT   HELIX       293    300       {ECO:0000244|PDB:3VP6}.
FT   HELIX       305    307       {ECO:0000244|PDB:3VP6}.
FT   STRAND      308    311       {ECO:0000244|PDB:3VP6}.
FT   HELIX       321    333       {ECO:0000244|PDB:3VP6}.
FT   STRAND      337    346       {ECO:0000244|PDB:3VP6}.
FT   STRAND      348    350       {ECO:0000244|PDB:3VP6}.
FT   HELIX       356    366       {ECO:0000244|PDB:3VP6}.
FT   STRAND      369    374       {ECO:0000244|PDB:3VP6}.
FT   HELIX       377    382       {ECO:0000244|PDB:3VP6}.
FT   TURN        384    386       {ECO:0000244|PDB:3VP6}.
FT   HELIX       387    390       {ECO:0000244|PDB:3VP6}.
FT   HELIX       393    395       {ECO:0000244|PDB:3VP6}.
FT   STRAND      397    401       {ECO:0000244|PDB:3VP6}.
FT   STRAND      414    420       {ECO:0000244|PDB:3VP6}.
FT   HELIX       423    428       {ECO:0000244|PDB:3VP6}.
FT   TURN        433    435       {ECO:0000244|PDB:3VP6}.
FT   HELIX       444    446       {ECO:0000244|PDB:3VP6}.
FT   HELIX       449    451       {ECO:0000244|PDB:3VP6}.
FT   HELIX       461    495       {ECO:0000244|PDB:3VP6}.
FT   STRAND      500    506       {ECO:0000244|PDB:3VP6}.
FT   STRAND      509    511       {ECO:0000244|PDB:3VP6}.
FT   STRAND      513    517       {ECO:0000244|PDB:3VP6}.
FT   HELIX       520    522       {ECO:0000244|PDB:3VP6}.
FT   HELIX       529    549       {ECO:0000244|PDB:3VP6}.
FT   STRAND      553    559       {ECO:0000244|PDB:3VP6}.
FT   STRAND      562    568       {ECO:0000244|PDB:3VP6}.
FT   HELIX       577    591       {ECO:0000244|PDB:3VP6}.
SQ   SEQUENCE   594 AA;  66897 MW;  6D761C471C81FDAE CRC64;
     MASSTPSSSA TSSNAGADPN TTNLRPTTYD TWCGVAHGCT RKLGLKICGF LQRTNSLEEK
     SRLVSAFKER QSSKNLLSCE NSDRDARFRR TETDFSNLFA RDLLPAKNGE EQTVQFLLEV
     VDILLNYVRK TFDRSTKVLD FHHPHQLLEG MEGFNLELSD HPESLEQILV DCRDTLKYGV
     RTGHPRFFNQ LSTGLDIIGL AGEWLTSTAN TNMFTYEIAP VFVLMEQITL KKMREIVGWS
     SKDGDGIFSP GGAISNMYSI MAARYKYFPE VKTKGMAAVP KLVLFTSEQS HYSIKKAGAA
     LGFGTDNVIL IKCNERGKII PADFEAKILE AKQKGYVPFY VNATAGTTVY GAFDPIQEIA
     DICEKYNLWL HVDAAWGGGL LMSRKHRHKL NGIERANSVT WNPHKMMGVL LQCSAILVKE
     KGILQGCNQM CAGYLFQPDK QYDVSYDTGD KAIQCGRHVD IFKFWLMWKA KGTVGFENQI
     NKCLELAEYL YAKIKNREEF EMVFNGEPEH TNVCFWYIPQ SLRGVPDSPQ RREKLHKVAP
     KIKALMMESG TTMVGYQPQG DKANFFRMVI SNPAATQSDI DFLIEEIERL GQDL
//
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