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Alanine aminotransferase 2 (ALT2) (EC 2.6.1.2) (Glutamate pyruvate transaminase 2) (GPT 2) (Glutamic--alanine transaminase 2) (Glutamic--pyruvic transaminase 2)

 ALAT2_HUMAN             Reviewed;         523 AA.
Q8TD30; Q8N9E2;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
28-MAR-2018, entry version 127.
RecName: Full=Alanine aminotransferase 2;
Short=ALT2;
EC=2.6.1.2;
AltName: Full=Glutamate pyruvate transaminase 2;
Short=GPT 2;
AltName: Full=Glutamic--alanine transaminase 2;
AltName: Full=Glutamic--pyruvic transaminase 2;
Name=GPT2; Synonyms=AAT2, ALT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND TISSUE SPECIFICITY.
TISSUE=Adipose tissue;
PubMed=11863375; DOI=10.1006/geno.2002.6722;
Yang R.-Z., Blaileanu G., Hansen B.C., Shuldiner A.R., Gong D.-W.;
"cDNA cloning, genomic structure, chromosomal mapping, and functional
expression of a novel human alanine aminotransferase.";
Genomics 79:445-450(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
INVOLVEMENT IN MRT49, VARIANT MRT49 ARG-153, AND CHARACTERIZATION OF
VARIANT MRT49 ARG-153.
PubMed=25758935; DOI=10.1007/s10545-015-9824-x;
Celis K., Shuldiner S., Haverfield E.V., Cappell J., Yang R.,
Gong D.W., Chung W.K.;
"Loss of function mutation in glutamic pyruvate transaminase 2 (GPT2)
causes developmental encephalopathy.";
J. Inherit. Metab. Dis. 38:941-948(2015).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 49-523 IN COMPLEX WITH
PYRIDOXAL PHOSPHATE, AND COFACTOR.
Structural genomics consortium (SGC);
"Human glutamate pyruvate transaminase 2.";
Submitted (AUG-2009) to the PDB data bank.
-!- FUNCTION: Catalyzes the reversible transamination between alanine
and 2-oxoglutarate to form pyruvate and glutamate.
{ECO:0000269|PubMed:11863375}.
-!- CATALYTIC ACTIVITY: L-alanine + 2-oxoglutarate = pyruvate + L-
glutamate. {ECO:0000269|PubMed:11863375}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|Ref.7};
-!- PATHWAY: Amino-acid degradation; L-alanine degradation via
transaminase pathway; pyruvate from L-alanine: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TD30-1; Sequence=Displayed;
Name=2;
IsoId=Q8TD30-2; Sequence=VSP_020008;
-!- TISSUE SPECIFICITY: Expressed at high levels in muscle, adipose
tissue, kidney and brain and at lower levels in the liver and
breast. {ECO:0000269|PubMed:11863375}.
-!- DISEASE: Mental retardation, autosomal recessive 49 (MRT49)
[MIM:616281]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRT49 patients show a
developmental encephalopathy characterized by rapid onset of
failure to thrive and microcephaly, as well as profoundly delayed
development. {ECO:0000269|PubMed:25758935}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. Alanine aminotransferase subfamily.
{ECO:0000305}.
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EMBL; AY029173; AAK31794.2; -; mRNA.
EMBL; AK094971; BAC04465.1; -; mRNA.
EMBL; AC018845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC062555; AAH62555.1; -; mRNA.
CCDS; CCDS10725.1; -. [Q8TD30-1]
CCDS; CCDS45478.1; -. [Q8TD30-2]
RefSeq; NP_001135938.1; NM_001142466.2. [Q8TD30-2]
RefSeq; NP_597700.1; NM_133443.3. [Q8TD30-1]
UniGene; Hs.460693; -.
PDB; 3IHJ; X-ray; 2.30 A; A=49-523.
PDBsum; 3IHJ; -.
ProteinModelPortal; Q8TD30; -.
SMR; Q8TD30; -.
BioGrid; 124217; 19.
IntAct; Q8TD30; 3.
STRING; 9606.ENSP00000345282; -.
DrugBank; DB00160; L-Alanine.
DrugBank; DB00142; L-Glutamic Acid.
DrugBank; DB00780; Phenelzine.
DrugBank; DB00114; Pyridoxal Phosphate.
iPTMnet; Q8TD30; -.
PhosphoSitePlus; Q8TD30; -.
BioMuta; GPT2; -.
DMDM; 74730602; -.
EPD; Q8TD30; -.
MaxQB; Q8TD30; -.
PaxDb; Q8TD30; -.
PeptideAtlas; Q8TD30; -.
PRIDE; Q8TD30; -.
Ensembl; ENST00000340124; ENSP00000345282; ENSG00000166123. [Q8TD30-1]
Ensembl; ENST00000440783; ENSP00000413804; ENSG00000166123. [Q8TD30-2]
GeneID; 84706; -.
KEGG; hsa:84706; -.
UCSC; uc002eel.4; human. [Q8TD30-1]
CTD; 84706; -.
DisGeNET; 84706; -.
EuPathDB; HostDB:ENSG00000166123.13; -.
GeneCards; GPT2; -.
HGNC; HGNC:18062; GPT2.
HPA; HPA051514; -.
MalaCards; GPT2; -.
MIM; 138210; gene.
MIM; 616281; phenotype.
neXtProt; NX_Q8TD30; -.
OpenTargets; ENSG00000166123; -.
PharmGKB; PA28948; -.
eggNOG; KOG0258; Eukaryota.
eggNOG; COG0436; LUCA.
GeneTree; ENSGT00650000093331; -.
HOGENOM; HOG000215020; -.
HOVERGEN; HBG026148; -.
InParanoid; Q8TD30; -.
KO; K00814; -.
OMA; APGTEWV; -.
OrthoDB; EOG091G0PY3; -.
PhylomeDB; Q8TD30; -.
TreeFam; TF300839; -.
BioCyc; MetaCyc:HS09332-MONOMER; -.
Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
UniPathway; UPA00528; UER00586.
ChiTaRS; GPT2; human.
EvolutionaryTrace; Q8TD30; -.
GenomeRNAi; 84706; -.
PRO; PR:Q8TD30; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000166123; -.
CleanEx; HS_GPT2; -.
ExpressionAtlas; Q8TD30; baseline and differential.
Genevisible; Q8TD30; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0042851; P:L-alanine metabolic process; IDA:UniProtKB.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Aminotransferase;
Complete proteome; Disease mutation; Mental retardation;
Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 523 Alanine aminotransferase 2.
/FTId=PRO_0000247532.
MOD_RES 341 341 N6-(pyridoxal phosphate)lysine.
MOD_RES 415 415 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BGT5}.
MOD_RES 505 505 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BGT5}.
MOD_RES 512 512 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BGT5}.
VAR_SEQ 1 100 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_020008.
VARIANT 153 153 S -> R (in MRT49; loss of function
mutation; dbSNP:rs786203999).
{ECO:0000269|PubMed:25758935}.
/FTId=VAR_073379.
CONFLICT 284 284 D -> G (in Ref. 4; BAC04465).
{ECO:0000305}.
STRAND 49 52 {ECO:0000244|PDB:3IHJ}.
TURN 53 56 {ECO:0000244|PDB:3IHJ}.
STRAND 57 64 {ECO:0000244|PDB:3IHJ}.
HELIX 67 80 {ECO:0000244|PDB:3IHJ}.
STRAND 86 89 {ECO:0000244|PDB:3IHJ}.
HELIX 107 117 {ECO:0000244|PDB:3IHJ}.
HELIX 119 123 {ECO:0000244|PDB:3IHJ}.
STRAND 125 127 {ECO:0000244|PDB:3IHJ}.
HELIX 129 141 {ECO:0000244|PDB:3IHJ}.
HELIX 157 170 {ECO:0000244|PDB:3IHJ}.
TURN 171 173 {ECO:0000244|PDB:3IHJ}.
HELIX 178 180 {ECO:0000244|PDB:3IHJ}.
STRAND 181 186 {ECO:0000244|PDB:3IHJ}.
HELIX 187 198 {ECO:0000244|PDB:3IHJ}.
HELIX 203 205 {ECO:0000244|PDB:3IHJ}.
STRAND 206 214 {ECO:0000244|PDB:3IHJ}.
HELIX 218 225 {ECO:0000244|PDB:3IHJ}.
STRAND 229 234 {ECO:0000244|PDB:3IHJ}.
HELIX 237 239 {ECO:0000244|PDB:3IHJ}.
HELIX 245 255 {ECO:0000244|PDB:3IHJ}.
TURN 256 258 {ECO:0000244|PDB:3IHJ}.
STRAND 259 269 {ECO:0000244|PDB:3IHJ}.
TURN 271 273 {ECO:0000244|PDB:3IHJ}.
HELIX 279 292 {ECO:0000244|PDB:3IHJ}.
STRAND 295 299 {ECO:0000244|PDB:3IHJ}.
TURN 301 304 {ECO:0000244|PDB:3IHJ}.
HELIX 316 322 {ECO:0000244|PDB:3IHJ}.
HELIX 325 328 {ECO:0000244|PDB:3IHJ}.
STRAND 333 342 {ECO:0000244|PDB:3IHJ}.
STRAND 347 349 {ECO:0000244|PDB:3IHJ}.
STRAND 352 358 {ECO:0000244|PDB:3IHJ}.
HELIX 361 373 {ECO:0000244|PDB:3IHJ}.
HELIX 379 388 {ECO:0000244|PDB:3IHJ}.
HELIX 399 425 {ECO:0000244|PDB:3IHJ}.
STRAND 437 441 {ECO:0000244|PDB:3IHJ}.
HELIX 449 457 {ECO:0000244|PDB:3IHJ}.
HELIX 462 474 {ECO:0000244|PDB:3IHJ}.
HELIX 481 483 {ECO:0000244|PDB:3IHJ}.
STRAND 492 496 {ECO:0000244|PDB:3IHJ}.
HELIX 501 521 {ECO:0000244|PDB:3IHJ}.
SEQUENCE 523 AA; 57904 MW; 4DD87814C62C7DEA CRC64;
MQRAAALVRR GCGPRTPSSW GRSQSSAAAE ASAVLKVRPE RSRRERILTL ESMNPQVKAV
EYAVRGPIVL KAGEIELELQ RGIKKPFTEV IRANIGDAQA MGQQPITFLR QVMALCTYPN
LLDSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAYITRR DGGVPADPDN
IYLTTGASDG ISTILKILVS GGGKSRTGVM IPIPQYPLYS AVISELDAIQ VNYYLDEENC
WALNVNELRR AVQEAKDHCD PKVLCIINPG NPTGQVQSRK CIEDVIHFAW EEKLFLLADE
VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS KGYMGECGYR GGYMEVINLH
PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE QFSREKESVL GNLAKKAKLT
EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK AVEAAQAHQM APDMFYCMKL LEETGICVVP
GSGFGQREGT YHFRMTILPP VEKLKTVLQK VKDFHINFLE KYA


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