THNS2_MOUSE
ID THNS2_MOUSE Reviewed; 483 AA.
AC Q80W22; Q8R135;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Threonine synthase-like 2;
DE Short=TSH2;
DE Short=mTSH2;
DE EC=4.2.3.-;
GN Name=Thnsl2;
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].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=17034760; DOI=10.1016/j.bbrc.2006.09.112;
RA Donini S., Percudani R., Credali A., Montanini B., Sartori A., Peracchi A.;
RT "A threonine synthase homolog from a mammalian genome.";
RL Biochem. Biophys. Res. Commun. 350:922-928(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Acts as a catabolic phospho-lyase on both gamma- and beta-
CC phosphorylated substrates. Degrades O-phospho-threonine (PThr) to
CC alpha-ketobutyrate, ammonia and phosphate. Also degrades O-phospho-
CC homoserine (PHS), but this is not its physiological substrate.
CC {ECO:0000269|PubMed:17034760}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17034760};
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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; AK165463; BAE38200.1; -; mRNA.
DR EMBL; BC025604; AAH25604.1; -; mRNA.
DR EMBL; BC051244; AAH51244.1; -; mRNA.
DR CCDS; CCDS20225.1; -.
DR RefSeq; NP_001029101.1; NM_001033929.2.
DR RefSeq; NP_848500.3; NM_178413.5.
DR AlphaFoldDB; Q80W22; -.
DR SMR; Q80W22; -.
DR BioGRID; 231215; 10.
DR STRING; 10090.ENSMUSP00000124423; -.
DR iPTMnet; Q80W22; -.
DR PhosphoSitePlus; Q80W22; -.
DR EPD; Q80W22; -.
DR jPOST; Q80W22; -.
DR MaxQB; Q80W22; -.
DR PaxDb; Q80W22; -.
DR PeptideAtlas; Q80W22; -.
DR PRIDE; Q80W22; -.
DR ProteomicsDB; 262776; -.
DR Antibodypedia; 32227; 139 antibodies from 28 providers.
DR DNASU; 232078; -.
DR Ensembl; ENSMUST00000074241; ENSMUSP00000073861; ENSMUSG00000054474.
DR Ensembl; ENSMUST00000160918; ENSMUSP00000124423; ENSMUSG00000054474.
DR GeneID; 232078; -.
DR KEGG; mmu:232078; -.
DR UCSC; uc009cgf.2; mouse.
DR CTD; 55258; -.
DR MGI; MGI:3041254; Thnsl2.
DR VEuPathDB; HostDB:ENSMUSG00000054474; -.
DR eggNOG; KOG2616; Eukaryota.
DR GeneTree; ENSGT00940000158503; -.
DR HOGENOM; CLU_015170_1_1_1; -.
DR InParanoid; Q80W22; -.
DR OMA; FGRIAFQ; -.
DR OrthoDB; 1361511at2759; -.
DR PhylomeDB; Q80W22; -.
DR TreeFam; TF329641; -.
DR BioGRID-ORCS; 232078; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Thnsl2; mouse.
DR PRO; PR:Q80W22; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80W22; protein.
DR Bgee; ENSMUSG00000054474; Expressed in right kidney and 131 other tissues.
DR ExpressionAtlas; Q80W22; baseline and differential.
DR Genevisible; Q80W22; MM.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:MGI.
DR GO; GO:0070905; F:serine binding; IDA:BHF-UCL.
DR GO; GO:0046360; P:2-oxobutyrate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0016311; P:dephosphorylation; IDA:BHF-UCL.
DR GO; GO:0009071; P:serine family amino acid catabolic process; IDA:BHF-UCL.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; -; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
PE 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..483
FT /note="Threonine synthase-like 2"
FT /id="PRO_0000306408"
FT MOD_RES 113
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 408
FT /note="Q -> P (in Ref. 1; AAH25604)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> K (in Ref. 1; AAH25604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 54188 MW; C13B20F9173D2C5E CRC64;
MWYTSTRGMA PRVNFEGALF SGYAPDGGLY MPEELPRLDE ETLRHWSTLS YRSLVKELCA
LFIGLELIPR HDLNDLIDRA FSRFRHRNVV HLCKLKNGLN ILELWHGVTY AFKDLSLSCT
AQFLQYFLEK KKKHVTIVVG TSGDTGSAAI ESVQGSKNVD IIVLLPKGHC SKIQELQMTT
VLKENVHVFE VEGNSDELDE PIKAVFADVA FVQRHNVMSL NSINWSRVLV QMAHHFFAYF
QCTPSLDTHP LPTVEVVVPT GAGGNLAAGC IAQKMGLPIC LVVAVNRNDI IHRTVQKGDF
SLCEVLRTTL ASAMDIQVPY NMERIFWLLS GSDSQTTRAL MEQFERTQSL QLPKDLHNKL
SEAVTSESVT DEAITQTMAR CWEENQYLLC PHSATAVNYH YQQTDSGQSS IRCCLASASA
VKFPEAVQAA GLTPETPAEI LALEHKETRC IPMRRGDDWT QMLRVTIEGL SQRWKDCVVN
PSE
