ID GADL1_MOUSE Reviewed; 550 AA.
AC Q80WP8; Q9CTD2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-APR-2013, entry version 68.
DE RecName: Full=Glutamate decarboxylase-like protein 1;
DE EC=4.1.1.-;
GN Name=Gadl1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-550 (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 341-550 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80WP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WP8-2; Sequence=VSP_029752;
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
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DR EMBL; AC133169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052327; AAH52327.1; -; mRNA.
DR EMBL; AK003937; BAB23083.1; -; mRNA.
DR IPI; IPI00316617; -.
DR IPI; IPI00911123; -.
DR RefSeq; NP_082914.1; NM_028638.1.
DR UniGene; Mm.485018; -.
DR ProteinModelPortal; Q80WP8; -.
DR SMR; Q80WP8; 70-550.
DR IntAct; Q80WP8; 1.
DR STRING; 10090.ENSMUSP00000081902; -.
DR PhosphoSite; Q80WP8; -.
DR PaxDb; Q80WP8; -.
DR PRIDE; Q80WP8; -.
DR GeneID; 73748; -.
DR KEGG; mmu:73748; -.
DR UCSC; uc009ryr.2; mouse.
DR CTD; 339896; -.
DR MGI; MGI:1920998; Gadl1.
DR eggNOG; COG0076; -.
DR HOGENOM; HOG000005382; -.
DR HOVERGEN; HBG004980; -.
DR OrthoDB; EOG4MKNG7; -.
DR NextBio; 338981; -.
DR ArrayExpress; Q80WP8; -.
DR Bgee; Q80WP8; -.
DR CleanEx; MM_GADL1; -.
DR Genevestigator; Q80WP8; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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_major_sub2.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Decarboxylase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1 550 Glutamate decarboxylase-like protein 1.
FT /FTId=PRO_0000312225.
FT MOD_RES 362 362 N6-(pyridoxal phosphate)lysine (By
FT similarity).
FT VAR_SEQ 494 550 VAPAIKEKMMKKGSLMLGYQPHRGKVNFFRQVVISPQVSRE
FT DMDFLLDEIDSLGRDM -> RTVQFICRGFLLERNADSHFA
FT LRNWKTFPSVLA (in isoform 2).
FT /FTId=VSP_029752.
FT CONFLICT 341 341 R -> K (in Ref. 3; BAB23083).
SQ SEQUENCE 550 AA; 62519 MW; 7CEFEAC6428E65BF CRC64;
MSHARDDHQG ASQGSQWLSQ ARTLVQEGTL FNFIRCLLLF QGDSGQKEMT PGKKIPIFVD
GVVLNGPQTD VKAGEKFVEE ACRLIMEEVV LKATDVNEKV CEWQPPEQLR QLLDLEMRDT
GESQDKLLKL CQDVIHFSVK TNHPRFFNQL YAGLDYYSLA ARIITEALNP SIYTYEVSPV
FLLVEEAVLK KMIECVGWKE GDGIFNPGGS VSNMCAMNLA RYRHCPDIKE KGLSGLPRLI
LFTSAECHYS MKKAASFLGI GTQNVYFVET DGRGKMIPED LEKQIWQARQ EGAVPFLVCA
TSGTTVLGAF DPLDEIAEVC ERHGLWLHVD ASWGGSALVS RKHRRLLHGI HRADSVAWNP
HKMLMAGIQC SALLVKDKSD LLKKCYSAKA TYLFQQDKFY DVSYDTGDKS IQCSRRPDAF
KFWMTWKALG TSGLEERVNR AFALSRYLVD EIKKREGFKL LMEPEYTNVC FWYIPPSLRE
MEEGPEFWRK LSLVAPAIKE KMMKKGSLML GYQPHRGKVN FFRQVVISPQ VSREDMDFLL
DEIDSLGRDM
//
