AT2L2_MOUSE
ID AT2L2_MOUSE Reviewed; 467 AA.
AC Q8R1K4; Q3TUU9; Q8BG04;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=5-phosphohydroxy-L-lysine phospho-lyase;
DE EC=4.2.3.134 {ECO:0000250|UniProtKB:Q8IUZ5};
DE AltName: Full=Alanine--glyoxylate aminotransferase 2-like 2;
GN Name=Phykpl; Synonyms=Agxt2l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Heart, Ovary, and Testis;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-
CC phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate
CC and 2-aminoadipate semialdehyde. {ECO:0000250|UniProtKB:Q8IUZ5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5-phosphooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate
CC + NH4(+) + phosphate; Xref=Rhea:RHEA:34091, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:57882,
CC ChEBI:CHEBI:58321; EC=4.2.3.134;
CC Evidence={ECO:0000250|UniProtKB:Q8IUZ5};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q8IUZ5};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P22256}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8IUZ5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R1K4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1K4-2; Sequence=VSP_025588;
CC Name=3;
CC IsoId=Q8R1K4-3; Sequence=VSP_025586, VSP_025587;
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Does not seem to possess aminotransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUZ5}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK085984; BAC39584.1; -; mRNA.
DR EMBL; AK087703; BAC39972.1; -; mRNA.
DR EMBL; AK133235; BAE21570.1; -; mRNA.
DR EMBL; AK160557; BAE35872.1; -; mRNA.
DR EMBL; AL645602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024461; AAH24461.1; -; mRNA.
DR CCDS; CCDS24653.1; -. [Q8R1K4-1]
DR RefSeq; NP_082674.1; NM_028398.2. [Q8R1K4-1]
DR AlphaFoldDB; Q8R1K4; -.
DR SMR; Q8R1K4; -.
DR STRING; 10090.ENSMUSP00000132190; -.
DR iPTMnet; Q8R1K4; -.
DR PhosphoSitePlus; Q8R1K4; -.
DR EPD; Q8R1K4; -.
DR MaxQB; Q8R1K4; -.
DR PaxDb; Q8R1K4; -.
DR PeptideAtlas; Q8R1K4; -.
DR PRIDE; Q8R1K4; -.
DR ProteomicsDB; 277266; -. [Q8R1K4-1]
DR ProteomicsDB; 277267; -. [Q8R1K4-2]
DR ProteomicsDB; 277268; -. [Q8R1K4-3]
DR Antibodypedia; 29429; 156 antibodies from 26 providers.
DR DNASU; 72947; -.
DR Ensembl; ENSMUST00000020625; ENSMUSP00000020625; ENSMUSG00000020359. [Q8R1K4-2]
DR Ensembl; ENSMUST00000167797; ENSMUSP00000132190; ENSMUSG00000020359. [Q8R1K4-1]
DR GeneID; 72947; -.
DR KEGG; mmu:72947; -.
DR UCSC; uc007itw.1; mouse. [Q8R1K4-3]
DR UCSC; uc007itx.1; mouse. [Q8R1K4-2]
DR UCSC; uc007ity.1; mouse. [Q8R1K4-1]
DR CTD; 85007; -.
DR MGI; MGI:1920197; Phykpl.
DR VEuPathDB; HostDB:ENSMUSG00000020359; -.
DR eggNOG; KOG1403; Eukaryota.
DR GeneTree; ENSGT00940000159222; -.
DR HOGENOM; CLU_016922_8_0_1; -.
DR InParanoid; Q8R1K4; -.
DR OMA; TSGQMSC; -.
DR OrthoDB; 145181at2759; -.
DR PhylomeDB; Q8R1K4; -.
DR TreeFam; TF320468; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR BioGRID-ORCS; 72947; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Phykpl; mouse.
DR PRO; PR:Q8R1K4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R1K4; protein.
DR Bgee; ENSMUSG00000020359; Expressed in embryonic post-anal tail and 252 other tissues.
DR ExpressionAtlas; Q8R1K4; baseline and differential.
DR Genevisible; Q8R1K4; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lyase; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..467
FT /note="5-phosphohydroxy-L-lysine phospho-lyase"
FT /id="PRO_0000287668"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P22256"
FT VAR_SEQ 168..184
FT /note="APLPDTYRGPYREDHPN -> VCIPTISNRSVSIPKPG (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025586"
FT VAR_SEQ 185..467
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025587"
FT VAR_SEQ 453..467
FT /note="EDTHPTQILLTRQQD -> GSTGPGCRAATGNRPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025588"
SQ SEQUENCE 467 AA; 51966 MW; 85DE6A02090E6758 CRC64;
MAADTRAKAV TLDLRRRLLS SSCRLFFPED PVKIIRGQGQ YLYDEQGREY LDCINNVAHV
GHCHPTVVQA AHEQNLVLNT NSRYLHDNIV DYAQRLSETL PEQLSVFYFL NSGSEANDLA
LRLARQYTGH QDVVVLDHAY HGHLSSLIDI SPYKFRNLGG QKEWVHVAPL PDTYRGPYRE
DHPNPAEAYA NEVKHVISSA QQKGRKIAAF FAESLPSVSG QIIPPAGYFS QVAEHIHRAG
GLFVADEIQV GFGRIGKHFW AFQLEGEDFV PDIVTMGKSI GNGHPVACMA TTQAVSRAFE
ATGVEYFNTF GGNPVSCAVG LAVLDVLKTE QLQAHATNVG SFLLEHLTQQ KAKHPIIGDV
RGTGLFIGVD LIKDETLRTP ATEEAEYLVS RLKENYILLS IDGPGKNILK FKPPMCFNVD
NAQHVVAKLD DILTDMEEKV RSCETLRIKH PPEDTHPTQI LLTRQQD
