ASSY_BOVIN
ID ASSY_BOVIN Reviewed; 412 AA.
AC P14568; Q3T0A7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Argininosuccinate synthase {ECO:0000305};
DE EC=6.3.4.5 {ECO:0000250|UniProtKB:P00966};
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=ASS1 {ECO:0000250|UniProtKB:P00966};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN CITRULLINEMIA.
RX PubMed=2813370; DOI=10.1073/pnas.86.20.7947;
RA Dennis J.A., Healy P.J., Beaudet A.L., O'Brien W.E.;
RT "Molecular definition of bovine argininosuccinate synthetase deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7947-7951(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the enzymes of the urea cycle, the metabolic pathway
CC transforming neurotoxic amonia produced by protein catabolism into
CC inocuous urea in the liver of ureotelic animals. Catalyzes the
CC formation of arginosuccinate from aspartate, citrulline and ATP and
CC together with ASL it is responsible for the biosynthesis of arginine in
CC most body tissues. {ECO:0000250|UniProtKB:P00966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:456215; EC=6.3.4.5;
CC Evidence={ECO:0000250|UniProtKB:P00966};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 2/3.
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; (N(omega)-L-
CC arginino)succinate from L-aspartate and L-citrulline: step 1/1.
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- SUBUNIT: Homotetramer. Interacts with NMRAL1. Interacts with CLOCK; in
CC a circadian manner (By similarity). Forms tissue-specific complexes
CC with ASL, SLC7A1, HSP90AA1 and nitric oxide synthase NOS1, NOS2 or
CC NOS3; the complex regulates cell-autonomous L-arginine synthesis and
CC citrulline recycling while channeling extracellular L-arginine to
CC nitric oxide synthesis pathway (By similarity).
CC {ECO:0000250|UniProtKB:P00966, ECO:0000250|UniProtKB:P16460}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- PTM: Acetylated by CLOCK in a circadian manner which negatively
CC regulates its enzyme activity. Deacetylated by histone deacetylases.
CC {ECO:0000250|UniProtKB:P00966}.
CC -!- DISEASE: Note=Defects in ASS1 are the cause of a bovine form of
CC citrullinemia. {ECO:0000269|PubMed:2813370}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; M26198; AAA30388.1; -; mRNA.
DR EMBL; BC102474; AAI02475.1; -; mRNA.
DR PIR; A33986; AJBORS.
DR RefSeq; NP_776317.1; NM_173892.4.
DR AlphaFoldDB; P14568; -.
DR SMR; P14568; -.
DR STRING; 9913.ENSBTAP00000027649; -.
DR iPTMnet; P14568; -.
DR PaxDb; P14568; -.
DR PeptideAtlas; P14568; -.
DR PRIDE; P14568; -.
DR Ensembl; ENSBTAT00000027649; ENSBTAP00000027649; ENSBTAG00000020747.
DR Ensembl; ENSBTAT00000071866; ENSBTAP00000074521; ENSBTAG00000020747.
DR GeneID; 280726; -.
DR KEGG; bta:280726; -.
DR CTD; 445; -.
DR VEuPathDB; HostDB:ENSBTAG00000020747; -.
DR VGNC; VGNC:26224; ASS1.
DR eggNOG; KOG1706; Eukaryota.
DR GeneTree; ENSGT00390000004524; -.
DR HOGENOM; CLU_032784_4_2_1; -.
DR InParanoid; P14568; -.
DR OrthoDB; 1459745at2759; -.
DR TreeFam; TF300736; -.
DR SABIO-RK; P14568; -.
DR UniPathway; UPA00068; UER00113.
DR UniPathway; UPA00158; UER00272.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000020747; Expressed in cortex of kidney and 105 other tissues.
DR ExpressionAtlas; P14568; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004055; F:argininosuccinate synthase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0000050; P:urea cycle; ISS:UniProtKB.
DR CDD; cd01999; Argininosuccinate_Synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR InterPro; IPR001518; Arginosuc_synth.
DR InterPro; IPR018223; Arginosuc_synth_CS.
DR InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR InterPro; IPR024074; AS_cat/multimer_dom_body.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11587; PTHR11587; 1.
DR Pfam; PF00764; Arginosuc_synth; 1.
DR SUPFAM; SSF69864; SSF69864; 1.
DR TIGRFAMs; TIGR00032; argG; 1.
DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Urea cycle.
FT CHAIN 1..412
FT /note="Argininosuccinate synthase"
FT /id="PRO_0000148553"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 87
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 92
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 115..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 119
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 123
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 127
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 180
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 189
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 270
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT BINDING 282
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT MOD_RES 87
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09034"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16460"
FT MOD_RES 113
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT MOD_RES 165
FT /note="N6-acetyllysine; by CLOCK"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT MOD_RES 176
FT /note="N6-acetyllysine; by CLOCK"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00966"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16460"
SQ SEQUENCE 412 AA; 46417 MW; 6F74C7F445EE0D86 CRC64;
MSGKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF
IEDISKEFVE EFIWPAIQSS ALYEDRYLLG TSLARPCIAR KQVEIAQREG AKYVSHGATG
KGNDQIRFEL TCYSLAPQIK VIAPWRMPEF YNRFQGRNDL MEYAKQHGIP VPVTPKNPWS
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNSP DMLEIEFKKG VPVKVTNVGD
GTTHSTALEL FLYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIAK SQERVEGKVQ VSVFKGQVYI
LGRESPLSLY NEELVSMNVQ GDYEPVDATG FININSLRLK EYHRLQNKVT AK
