ID F8W943_HUMAN Unreviewed; 399 AA.
AC F8W943;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00019698};
GN Name=ASL {ECO:0000313|Ensembl:ENSP00000354710.6};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000354710.6, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000354710.6, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [3] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [4] {ECO:0000313|Ensembl:ENSP00000354710.6}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00033644};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24021;
CC Evidence={ECO:0000256|ARBA:ARBA00033644};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24022;
CC Evidence={ECO:0000256|ARBA:ARBA00033644};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004730}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from
CC (N(omega)-L-arginino)succinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005214}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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; AC068533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F8W943; -.
DR SMR; F8W943; -.
DR IntAct; F8W943; 1.
DR MINT; F8W943; -.
DR MassIVE; F8W943; -.
DR MaxQB; F8W943; -.
DR PeptideAtlas; F8W943; -.
DR ProteomicsDB; 30257; -.
DR Antibodypedia; 1530; 351 antibodies from 30 providers.
DR Ensembl; ENST00000362000.10; ENSP00000354710.6; ENSG00000126522.17.
DR UCSC; uc064dzj.1; human.
DR HGNC; HGNC:746; ASL.
DR VEuPathDB; HostDB:ENSG00000126522; -.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_027272_0_0_1; -.
DR UniPathway; UPA00068; -.
DR UniPathway; UPA00158; UER00273.
DR ChiTaRS; ASL; human.
DR Proteomes; UP000005640; Chromosome 7.
DR Bgee; ENSG00000126522; Expressed in right lobe of liver and 98 other cell types or tissues.
DR ExpressionAtlas; F8W943; baseline and differential.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:F8W943,
KW ECO:0007829|MaxQB:F8W943};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Urea cycle {ECO:0000256|ARBA:ARBA00022436}.
FT DOMAIN 2..240
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 303..370
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 399 AA; 44471 MW; 04B347A485A8BDCC CRC64;
MASEVAEEWA QGTFKLNSND EDIHTANERR LKELIGATAG KLHTGRSRND QVVTDLRLWM
RQTCSTLSGL LWELIRTMVD RAEAERDVLF PGYTHLQRAQ PIRWSHWILS HAVALTRDSE
RLLEVRKRIN VLPLGSGAIA GNPLGVDREL LRAELNFGAI TLNSMDATSE RDFVAEFLFW
ASLCMTHLSR MAEDLILYCT KEFSFVQLSD AYSTGSSLMP QKKNPDSLEL IRSKAGRVFG
RCAGLLMTLK GLPSTYNKDL QEDKEAVFEV SDTMSAVLQV ATGVISTLQI HQENMGQALS
PDMLATDLAY YLVRKGMPFR QAHEASGKAV FMAETKGVAL NQLSLQELQT ISPLFSGDVI
CVWDYGHSVE QYGALGGTAR SSVDWQIRQV RALLQAQQA
//
