LOCUS NP_000809 585 aa linear PRI 26-MAY-2023
DEFINITION glutamate decarboxylase 2 [Homo sapiens].
ACCESSION NP_000809
VERSION NP_000809.1
DBSOURCE REFSEQ: accession NM_000818.3
KEYWORDS RefSeq.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 585)
AUTHORS Su Z, Ma C, Zhao R, Jiang Y, Cai Y, Yong G, Yang T and Xu X.
TITLE Heterogeneity of circulating CXCR5-PD-1hiTph cells in patients of
type 2 and type 1 diabetes in Chinese population
JOURNAL Acta Diabetol 60 (6), 767-776 (2023)
PUBMED 36879107
REMARK GeneRIF: Heterogeneity of circulating CXCR5-PD-1[hi]Tph cells in
patients of type 2 and type 1 diabetes in Chinese population.
REFERENCE 2 (residues 1 to 585)
AUTHORS Cai R, Zhao F, Zhou H, Wang Z, Lin D, Huang L, Xie W, Chen J, Zhou
L, Zhang N and Huang C.
TITLE A tumor-associated autoantibody panel for the detection of
non-small cell lung cancer
JOURNAL Front Oncol 12, 1056572 (2022)
PUBMED 36531074
REMARK Publication Status: Online-Only
REFERENCE 3 (residues 1 to 585)
AUTHORS Bedi S, Richardson TM, Jia B, Saab H, Brinkman FSL and Westley M.
TITLE Similarities between bacterial GAD and human GAD65: Implications in
gut mediated autoimmune type 1 diabetes
JOURNAL PLoS One 17 (2), e0261103 (2022)
PUBMED 35196314
REMARK GeneRIF: Similarities between bacterial GAD and human GAD65:
Implications in gut mediated autoimmune type 1 diabetes.
Publication Status: Online-Only
REFERENCE 4 (residues 1 to 585)
AUTHORS Vazifekhah,S., Barfi,S., Soleimany,F., Aliakbar,A., Zavvari,F. and
Karimzadeh,F.
TITLE The plasma level of glutamic acid decarboxylase 65 (GAD65)
increased in severely autistic Iranian children
JOURNAL Bratisl Lek Listy 123 (5), 347-351 (2022)
PUBMED 35420879
REMARK GeneRIF: The plasma level of glutamic acid decarboxylase 65 (GAD65)
increased in severely autistic Iranian children.
REFERENCE 5 (residues 1 to 585)
AUTHORS Dade M, Berzero G, Izquierdo C, Giry M, Benazra M, Delattre JY,
Psimaras D and Alentorn A.
TITLE Neurological Syndromes Associated with Anti-GAD Antibodies
JOURNAL Int J Mol Sci 21 (10), 3701 (2020)
PUBMED 32456344
REMARK GeneRIF: Neurological Syndromes Associated with Anti-GAD
Antibodies.
Review article
Publication Status: Online-Only
REFERENCE 6 (residues 1 to 585)
AUTHORS Dirkx R Jr, Thomas A, Li L, Lernmark A, Sherwin RS, De Camilli P
and Solimena M.
TITLE Targeting of the 67-kDa isoform of glutamic acid decarboxylase to
intracellular organelles is mediated by its interaction with the
NH2-terminal region of the 65-kDa isoform of glutamic acid
decarboxylase
JOURNAL J Biol Chem 270 (5), 2241-2246 (1995)
PUBMED 7836456
REFERENCE 7 (residues 1 to 585)
AUTHORS Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B and Northemann
W.
TITLE Characterization of a linear epitope within the human pancreatic
64-kDa glutamic acid decarboxylase and its autoimmune recognition
by sera from insulin-dependent diabetes mellitus patients
JOURNAL Eur J Biochem 212 (2), 597-603 (1993)
PUBMED 7680313
REFERENCE 8 (residues 1 to 585)
AUTHORS Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL,
Wagner-McPherson CB, Evans GA and Tobin AJ.
TITLE Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are
each encoded by a single gene
JOURNAL Proc Natl Acad Sci U S A 89 (6), 2115-2119 (1992)
PUBMED 1549570
REFERENCE 9 (residues 1 to 585)
AUTHORS Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA,
Barmeier H, Mathewes S, Grant FJ, Foster D and Lernmark A.
TITLE Cloning and primary structure of a human islet isoform of glutamic
acid decarboxylase from chromosome 10
JOURNAL Proc Natl Acad Sci U S A 88 (19), 8337-8341 (1991)
PUBMED 1924293
REFERENCE 10 (residues 1 to 585)
AUTHORS Cram DS, Barnett LD, Joseph JL and Harrison LC.
TITLE Cloning and partial nucleotide sequence of human glutamic acid
decarboxylase cDNA from brain and pancreatic islets
JOURNAL Biochem Biophys Res Commun 176 (3), 1239-1244 (1991)
PUBMED 2039509
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from BI438818.1, M74826.1 and
BP392604.1.
Summary: This gene encodes one of several forms of glutamic acid
decarboxylase, identified as a major autoantigen in
insulin-dependent diabetes. The enzyme encoded is responsible for
catalyzing the production of gamma-aminobutyric acid from
L-glutamic acid. A pathogenic role for this enzyme has been
identified in the human pancreas since it has been identified as an
autoantibody and an autoreactive T cell target in insulin-dependent
diabetes. This gene may also play a role in the stiff man syndrome.
Alternative splicing results in multiple transcript variants that
encode the same protein. [provided by RefSeq, Oct 2008].
Transcript Variant: This variant (1) represents the longer
transcript.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: M74826.1, BC126329.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMEA2145743, SAMEA2157437
[ECO:0000348]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..585
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="10"
/map="10p12.1"
Protein 1..585
/product="glutamate decarboxylase 2"
/EC_number="4.1.1.15"
/note="Glutamate decarboxylase-2 (pancreas); GAD-65; 65
kDa glutamic acid decarboxylase; glutamate decarboxylase 2
(pancreatic islets and brain, 65kDa)"
/calculated_mol_wt=65280
Region 1..24
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q05329.1)"
Site 3
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:8999827; propagated from
UniProtKB/Swiss-Prot (Q05329.1)"
Site 6
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:8999827; propagated from
UniProtKB/Swiss-Prot (Q05329.1)"
Site 10
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:8999827; propagated from
UniProtKB/Swiss-Prot (Q05329.1)"
Site 13
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000269|PubMed:8999827; propagated from
UniProtKB/Swiss-Prot (Q05329.1)"
Region 138..509
/region_name="Pyridoxal_deC"
/note="Pyridoxal-dependent decarboxylase conserved domain;
pfam00282"
/db_xref="CDD:395219"
Site order(243..244,247,335,364,367,393,396)
/site_type="other"
/note="pyridoxal 5'-phosphate binding site [chemical
binding]"
/db_xref="CDD:99743"
Site 396
/site_type="active"
/note="catalytic residue [active]"
/db_xref="CDD:99743"
CDS 1..585
/gene="GAD2"
/gene_synonym="GAD65"
/coded_by="NM_000818.3:439..2196"
/db_xref="CCDS:CCDS7149.1"
/db_xref="GeneID:2572"
/db_xref="HGNC:HGNC:4093"
/db_xref="MIM:138275"
ORIGIN
1 maspgsgfws fgsedgsgds enpgtarawc qvaqkftggi gnklcallyg daekpaesgg
61 sqppraaark aacacdqkpc scskvdvnya flhatdllpa cdgerptlaf lqdvmnillq
121 yvvksfdrst kvidfhypne llqeynwela dqpqnleeil mhcqttlkya iktghpryfn
181 qlstgldmvg laadwltsta ntnmftyeia pvfvlleyvt lkkmreiigw pggsgdgifs
241 pggaisnmya mmiarfkmfp evkekgmaal prliaftseh shfslkkgaa algigtdsvi
301 likcdergkm ipsdlerril eakqkgfvpf lvsatagttv ygafdpllav adickkykiw
361 mhvdaawggg llmsrkhkwk lsgveransv twnphkmmgv plqcsallvr eeglmqncnq
421 mhasylfqqd khydlsydtg dkalqcgrhv dvfklwlmwr akgttgfeah vdkclelaey
481 lyniiknreg yemvfdgkpq htnvcfwyip pslrtledne ermsrlskva pvikarmmey
541 gttmvsyqpl gdkvnffrmv isnpaathqd idflieeier lgqdl
//
