BUP1_MOUSE
ID BUP1_MOUSE Reviewed; 393 AA.
AC Q8VC97; Q8R1K8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Beta-ureidopropionase;
DE EC=3.5.1.6;
DE AltName: Full=Beta-alanine synthase;
DE AltName: Full=N-carbamoyl-beta-alanine amidohydrolase;
GN Name=Upb1;
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=FVB/N; TISSUE=Kidney, and Liver;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 a late step in pyrimidine degradation. Converts N-
CC carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia
CC and carbon dioxide. Likewise, converts N-carbamoyl-beta-
CC aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate,
CC ammonia and carbon dioxide. {ECO:0000250|UniProtKB:Q9UBR1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(carbamoylamino)propanoate + 2 H(+) + H2O = beta-alanine +
CC CO2 + NH4(+); Xref=Rhea:RHEA:11184, ChEBI:CHEBI:11892,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57966; EC=3.5.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q9UBR1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(carbamoylamino)-2-methylpropanoate + 2 H(+) + H2O = (R)-3-
CC amino-2-methylpropanoate + CO2 + NH4(+); Xref=Rhea:RHEA:37339,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57731, ChEBI:CHEBI:74414; EC=3.5.1.6;
CC Evidence={ECO:0000250|UniProtKB:Q9UBR1};
CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC {ECO:0000250|UniProtKB:Q9UBR1}.
CC -!- SUBUNIT: Homodimer, homotetramer, homooctamer; can also form higher
CC homooligomers. {ECO:0000250|UniProtKB:Q9UBR1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BUP
CC family. {ECO:0000305}.
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DR EMBL; BC021388; AAH21388.1; -; mRNA.
DR EMBL; BC024447; AAH24447.1; -; mRNA.
DR CCDS; CCDS23925.1; -.
DR RefSeq; NP_598756.1; NM_133995.4.
DR AlphaFoldDB; Q8VC97; -.
DR SMR; Q8VC97; -.
DR STRING; 10090.ENSMUSP00000049342; -.
DR iPTMnet; Q8VC97; -.
DR PhosphoSitePlus; Q8VC97; -.
DR SwissPalm; Q8VC97; -.
DR jPOST; Q8VC97; -.
DR MaxQB; Q8VC97; -.
DR PaxDb; Q8VC97; -.
DR PRIDE; Q8VC97; -.
DR ProteomicsDB; 273718; -.
DR Antibodypedia; 252; 93 antibodies from 24 providers.
DR DNASU; 103149; -.
DR Ensembl; ENSMUST00000039925; ENSMUSP00000049342; ENSMUSG00000033427.
DR GeneID; 103149; -.
DR KEGG; mmu:103149; -.
DR UCSC; uc007fqj.2; mouse.
DR CTD; 51733; -.
DR MGI; MGI:2143535; Upb1.
DR VEuPathDB; HostDB:ENSMUSG00000033427; -.
DR eggNOG; KOG0808; Eukaryota.
DR GeneTree; ENSGT00390000004906; -.
DR HOGENOM; CLU_030130_4_1_1; -.
DR InParanoid; Q8VC97; -.
DR OMA; AVKPNYS; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; Q8VC97; -.
DR TreeFam; TF313402; -.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR UniPathway; UPA00131; -.
DR BioGRID-ORCS; 103149; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Upb1; mouse.
DR PRO; PR:Q8VC97; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VC97; protein.
DR Bgee; ENSMUSG00000033427; Expressed in left lobe of liver and 72 other tissues.
DR ExpressionAtlas; Q8VC97; baseline and differential.
DR Genevisible; Q8VC97; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0003837; F:beta-ureidopropionase activity; IDA:MGI.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0033396; P:beta-alanine biosynthetic process via 3-ureidopropionate; ISS:UniProtKB.
DR GO; GO:0019482; P:beta-alanine metabolic process; ISO:MGI.
DR GO; GO:0006248; P:CMP catabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; IDA:MGI.
DR GO; GO:0046074; P:dTMP catabolic process; ISO:MGI.
DR GO; GO:0046079; P:dUMP catabolic process; IDA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0046135; P:pyrimidine nucleoside catabolic process; ISS:UniProtKB.
DR GO; GO:0046050; P:UMP catabolic process; IDA:MGI.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..393
FT /note="Beta-ureidopropionase"
FT /id="PRO_0000204052"
FT DOMAIN 72..344
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03248"
SQ SEQUENCE 393 AA; 43937 MW; 442A33470A54BEBA CRC64;
MAGPEWQSLE QCLEKHLPPD DLAQVKRILY GKQTRNLDLP REALKAASER NFELKGYAFG
AAKEQQRCPQ IVRVGLVQNR IPLPTSAPVA EQVSALHKSI EEIAEVAAMC GVNIICFQEA
WNMPFAFCTR EKLPWTEFAE SAEDGLTTRF CQKLAKKHNM VVVSPILERD REHGGVLWNT
AVVISNSGLV MGKTRKNHIP RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL
NWLMYSINGA EIIFNPSATI GELSESLWPI EARNAAIANH CFTCALNRVG QEHFPNEFTS
GDGKKAHHDL GYFYGSSYVA APDGSRTPGL SRNQDGLLVT ELNLNLCQQI NDFWTFKMTG
RLEMYARELA EAVKPNYSPN IVKEDLVLAP SSG
