ALAT2_DANRE
ID ALAT2_DANRE Reviewed; 549 AA.
AC Q6NYL5; A2BII0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Alanine aminotransferase 2-like;
DE Short=ALT2;
DE EC=2.6.1.2;
DE AltName: Full=Glutamate pyruvate transaminase 2;
DE Short=GPT 2;
DE AltName: Full=Glutamic--alanine transaminase 2;
DE AltName: Full=Glutamic--pyruvic transaminase 2;
GN Name=gpt2l; Synonyms=gpt2; ORFNames=im:6791811, si:ch211-261f3.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible transamination between alanine and
CC 2-oxoglutarate to form pyruvate and glutamate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC pathway; pyruvate from L-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NYL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NYL5-2; Sequence=VSP_029840;
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. Alanine aminotransferase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM14165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX928742; CAM14165.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC061955; AAH61955.1; -; mRNA.
DR EMBL; BC066543; AAH66543.1; -; mRNA.
DR RefSeq; XP_017213488.1; XM_017357999.1. [Q6NYL5-1]
DR AlphaFoldDB; Q6NYL5; -.
DR SMR; Q6NYL5; -.
DR STRING; 7955.ENSDARP00000121415; -.
DR PaxDb; Q6NYL5; -.
DR GeneID; 403086; -.
DR CTD; 2875; -.
DR ZFIN; ZDB-GENE-050302-11; gpt.
DR eggNOG; KOG0258; Eukaryota.
DR InParanoid; Q6NYL5; -.
DR OrthoDB; 477122at2759; -.
DR PhylomeDB; Q6NYL5; -.
DR Reactome; R-DRE-8964540; Alanine metabolism.
DR UniPathway; UPA00528; UER00586.
DR PRO; PR:Q6NYL5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042851; P:L-alanine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR045088; ALAT1/2-like.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11751; PTHR11751; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminotransferase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..549
FT /note="Alanine aminotransferase 2-like"
FT /id="PRO_0000247534"
FT MOD_RES 367
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..44
FT /note="MLSKRSLRVLKWGRCEAAYAAAYPKVPDWVLNFSPLPSLSSPHR -> ADLS
FT LLSVVSATEEAPLLHFW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_029840"
FT CONFLICT 57
FT /note="M -> L (in Ref. 2; AAH66543/AAH61955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 61092 MW; 633DDE9C6F3305D9 CRC64;
MLSKRSLRVL KWGRCEAAYA AAYPKVPDWV LNFSPLPSLS SPHRDFSAFP AAQSEHMQQK
MSENGAIPRQ GKVLTVDTMN ANVKKVDYAV RGPIVQRAVQ IEKELKEGVK KPFDEVIKAN
IGDAHAMGQR PITFFRQVMA LCTYPQLLDD NKFPEDAKNR ARRILQSCGG NSIGAYTTSQ
GIDCVRQDVA KYIERRDGGI PSDPDNIYLT TGASDGIVTI LKLLTAGEGL TRTGVMISIP
QYPLYSASIA ELGAVQINYY LNEEKCWSLD ISELQRSLQA ARKHCNPRVL CIINPGNPTG
QVQSRQCIED VIQFAAKENL FLMADEVYQD NVYAKGCEFH SFKKVLFEMG PEYSKKVELA
SFHSTSKCYM GECGFRGGYM EVINMDADVK AQLTKLVSVR LCPPAPGQAL MDLVVNPPQP
GEPSHQTFMQ ERTAVLSALA EKAKLTEQIL NTVPGISCNP VQGAMYSFPR ITLPERAISE
AKAKGQAPDM FYCMKLLEET GICLVPGSGF GQREGTYHFR MTILPPTDKL KLMLNKLKDF
HQRFTQQYS
