ARLY_HUMAN
ID ARLY_HUMAN Reviewed; 464 AA.
AC P04424; E7EMI0; E9PE48; Q6LDS5; Q96HS2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Argininosuccinate lyase {ECO:0000303|PubMed:3391281};
DE Short=ASAL;
DE EC=4.3.2.1 {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:9045711};
DE AltName: Full=Arginosuccinase;
GN Name=ASL;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3391281; DOI=10.1016/0014-5793(88)80124-8;
RA Matuo S., Tatsuno M., Kobayashi K., Saheki T., Miyata T.;
RT "Isolation of cDNA clones of human argininosuccinate lyase and corrected
RT amino acid sequence.";
RL FEBS Lett. 234:395-399(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3463959; DOI=10.1073/pnas.83.19.7211;
RA O'Brien W.E., McInnes R., Kalumuck K., Adcock M.;
RT "Cloning and sequence analysis of cDNA for human argininosuccinate lyase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7211-7215(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2644168; DOI=10.1016/0888-7543(89)90314-5;
RA Todd S., McGill J.R., McCombs J.L., Moore C.M., Weider I., Naylor S.L.;
RT "cDNA sequence, interspecies comparison, and gene mapping analysis of
RT argininosuccinate lyase.";
RL Genomics 4:53-59(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Matuo S.;
RT "Cloning and sequence analysis of cDNA for human argininosuccinate lyase.";
RL Kagoshima Daigaku Igaku Zasshi 40:147-160(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Linnebank M., Tschiedel E., Koch H.G.;
RT "Complete sequence of the human ASL gene.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Cervix;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-97 (ISOFORM 1/2/3).
RX PubMed=3368457; DOI=10.1073/pnas.85.10.3479;
RA Piatigorsky J., O'Brien W.E., Norman B.L., Kalumuck K., Wistow G.J.,
RA Borras T., Nickerson J.M., Wawrousek E.F.;
RT "Gene sharing by delta-crystallin and argininosuccinate lyase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3479-3483(1988).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP PATHWAY, VARIANTS ARGINSA GLY-87; ARG-286; THR-360 AND ASP-398, AND
RP CHARACTERIZATION OF VARIANTS ARGINSA GLY-87; ARG-286; THR-360 AND ASP-398.
RX PubMed=11747433; DOI=10.1021/bi011526e;
RA Yu B., Thompson G.D., Yip P., Howell P.L., Davidson A.R.;
RT "Mechanisms for intragenic complementation at the human argininosuccinate
RT lyase locus.";
RL Biochemistry 40:15581-15590(2001).
RN [10]
RP ACETYLATION AT LYS-69 AND LYS-288, ACTIVITY REGULATION, MUTAGENESIS OF
RP LYS-288, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20167786; DOI=10.1126/science.1179689;
RA Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L.,
RA Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L., Chin J.,
RA Yang P., Chen X., Lei Q., Xiong Y., Guan K.L.;
RT "Regulation of cellular metabolism by protein lysine acetylation.";
RL Science 327:1000-1004(2010).
RN [11]
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., Buerckstuemmer 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 [12]
RP FUNCTION, VARIANTS ARGINSA GLN-113 AND TRP-236, AND CHARACTERIZATION OF
RP VARIANTS ARGINSA GLN-113 AND TRP-236.
RX PubMed=22081021; DOI=10.1038/nm.2544;
RA Erez A., Nagamani S.C., Shchelochkov O.A., Premkumar M.H., Campeau P.M.,
RA Chen Y., Garg H.K., Li L., Mian A., Bertin T.K., Black J.O., Zeng H.,
RA Tang Y., Reddy A.K., Summar M., O'Brien W.E., Harrison D.G., Mitch W.E.,
RA Marini J.C., Aschner J.L., Bryan N.S., Lee B.;
RT "Requirement of argininosuccinate lyase for systemic nitric oxide
RT production.";
RL Nat. Med. 17:1619-1626(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [14]
RP X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS).
RC TISSUE=Liver;
RX PubMed=9256435; DOI=10.1073/pnas.94.17.9063;
RA Turner M.A., Simpson A., McInnes R.R., Howell P.L.;
RT "Human argininosuccinate lyase: a structural basis for intragenic
RT complementation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9063-9068(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF VARIANT ARGINSA ARG-286,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION OF VARIANTS ARGINSA GLN-12 AND ARG-286.
RX PubMed=11747432; DOI=10.1021/bi011525m;
RA Sampaleanu L.M., Vallee F., Thompson G.D., Howell P.L.;
RT "Three-dimensional structure of the argininosuccinate lyase frequently
RT complementing allele Q286R.";
RL Biochemistry 40:15570-15580(2001).
RN [16]
RP VARIANT ARGINSA CYS-95, CHARACTERIZATION OF VARIANT ARGINSA CYS-95,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2263616; DOI=10.1073/pnas.87.24.9625;
RA Walker D.C., McCloskey D.A., Simard L.R., McInnes R.R.;
RT "Molecular analysis of human argininosuccinate lyase: mutant
RT characterization and alternative splicing of the coding region.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9625-9629(1990).
RN [17]
RP VARIANTS ARGINSA TRP-111; GLN-193 AND ARG-286, AND MUTAGENESIS OF LYS-51
RP AND HIS-89.
RX PubMed=1705937; DOI=10.1016/s0021-9258(19)67785-9;
RA Barbosa P., Cialkowski M., O'Brien W.E.;
RT "Analysis of naturally occurring and site-directed mutations in the
RT argininosuccinate lyase gene.";
RL J. Biol. Chem. 266:5286-5290(1991).
RN [18]
RP VARIANTS ARGINSA GLY-87; ARG-286 AND ASP-398, CHARACTERIZATION OF VARIANTS
RP ARGINSA GLY-87 AND ARG-286, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9045711; DOI=10.1074/jbc.272.10.6777;
RA Walker D.C., Christodoulou J., Craig H.J., Simard L.R., Ploder L.,
RA Howell P.L., McInnes R.R.;
RT "Intragenic complementation at the human argininosuccinate lyase locus.
RT Identification of the major complementing alleles.";
RL J. Biol. Chem. 272:6777-6783(1997).
RN [19]
RP VARIANTS ARGINSA MET-178; CYS-379 AND CYS-385.
RX PubMed=12408190; DOI=10.1023/a:1020108002877;
RA Kleijer W.J., Garritsen V.H., Linnebank M., Mooyer P., Huijmans J.G.M.,
RA Mustonen A., Simola K.O.J., Arslan-Kirchner M., Battini R., Briones P.,
RA Cardo E., Mandel H., Tschiedel E., Wanders R.J.A., Koch H.G.;
RT "Clinical, enzymatic, and molecular genetic characterization of a
RT biochemical variant type of argininosuccinic aciduria: prenatal and
RT postnatal diagnosis in five unrelated families.";
RL J. Inherit. Metab. Dis. 25:399-410(2002).
RN [20]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-181 AND VAL-200.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [21]
RP VARIANTS ARGINSA ASN-31; GLN-113; MET-178; GLN-186; TRP-236; ARG-286;
RP LEU-335; ARG-382 AND TRP-456.
RX PubMed=17326097; DOI=10.1002/humu.20498;
RA Trevisson E., Salviati L., Baldoin M.C., Toldo I., Casarin A., Sacconi S.,
RA Cesaro L., Basso G., Burlina A.B.;
RT "Argininosuccinate lyase deficiency: mutational spectrum in Italian
RT patients and identification of a novel ASL pseudogene.";
RL Hum. Mutat. 28:694-702(2007).
RN [22]
RP VARIANTS ARGINSA ASN-31; LYS-73; GLN-113; MET-178; GLN-182; GLN-186;
RP TRP-236; ARG-286; GLN-297; LEU-335; ARG-382 AND TRP-456, AND
RP CHARACTERIZATION OF VARIANTS ARGINSA ASN-31; LYS-73; GLN-113; MET-178;
RP GLN-182; GLN-186; TRP-236; ARG-286; GLN-297; LEU-335; ARG-382 AND TRP-456.
RX PubMed=19703900; DOI=10.1074/jbc.m109.050195;
RA Trevisson E., Burlina A., Doimo M., Pertegato V., Casarin A., Cesaro L.,
RA Navas P., Basso G., Sartori G., Salviati L.;
RT "Functional complementation in yeast allows molecular characterization of
RT missense argininosuccinate lyase mutations.";
RL J. Biol. Chem. 284:28926-28934(2009).
RN [23]
RP VARIANTS ARGINSA ALA-70; CYS-94; HIS-94; HIS-95; VAL-104; GLU-120; HIS-121;
RP TRP-126; TRP-146; ARG-156; ASN-160; HIS-166; HIS-168; ASN-170; ARG-180;
RP GLN-182; TRP-191; TRP-193; VAL-205; GLN-213; PRO-227; ARG-229; THR-229;
RP GLU-231; ASN-237; THR-256; PRO-262; PRO-295; ARG-301; TRP-306; ALA-324;
RP LEU-326; PHE-343; PRO-343; VAL-368; GLU-380; HIS-385; LEU-385; GLN-388;
RP ARG-433; LEU-434; ASN-447 AND GLN-456.
RX PubMed=24166829; DOI=10.1002/humu.22469;
RA Balmer C., Pandey A.V., Rufenacht V., Nuoffer J.M., Fang P., Wong L.J.,
RA Haberle J.;
RT "Mutations and polymorphisms in the human argininosuccinate lyase (ASL)
RT gene.";
RL Hum. Mutat. 35:27-35(2014).
CC -!- FUNCTION: Catalyzes the reversible cleavage of L-argininosuccinate to
CC fumarate and L-arginine, an intermediate step reaction in the urea
CC cycle mostly providing for hepatic nitrogen detoxification into
CC excretable urea as well as de novo L-arginine synthesis in nonhepatic
CC tissues (PubMed:11747433, PubMed:11747432, PubMed:9045711,
CC PubMed:22081021, PubMed:2263616). Essential regulator of intracellular
CC and extracellular L-arginine pools. As part of citrulline-nitric oxide
CC cycle, forms tissue-specific multiprotein complexes with
CC argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric
CC oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-
CC arginine synthesis while channeling extracellular L-arginine to nitric
CC oxide synthesis pathway (PubMed:22081021).
CC {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433,
CC ECO:0000269|PubMed:22081021, ECO:0000269|PubMed:9045711}.
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; Evidence={ECO:0000269|PubMed:11747432,
CC ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:2263616,
CC ECO:0000269|PubMed:9045711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24021;
CC Evidence={ECO:0000305|PubMed:11747432, ECO:0000305|PubMed:11747433};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24022;
CC Evidence={ECO:0000305|PubMed:11747433, ECO:0000305|PubMed:9045711};
CC -!- ACTIVITY REGULATION: Enzyme activity is regulated by acetylation.
CC {ECO:0000269|PubMed:20167786}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for 2-(N(omega)-L-arginino)succinate
CC {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433};
CC Vmax=10.36 umol/min/mg enzyme toward 2-(N(omega)-L-arginino)succinate
CC {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC {ECO:0000305|PubMed:11747433}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from
CC (N(omega)-L-arginino)succinate: step 1/1.
CC {ECO:0000305|PubMed:11747433}.
CC -!- SUBUNIT: Homotetramer (PubMed:11747433). Forms tissue-specific
CC complexes with ASS1, SLC7A1, HSP90AA1 and nitric oxide synthase NOS1,
CC NOS2 or NOS3; the complex maintenance is independent of ASL catalytic
CC function (By similarity). {ECO:0000250|UniProtKB:Q91YI0,
CC ECO:0000269|PubMed:11747433}.
CC -!- INTERACTION:
CC P04424; P04424: ASL; NbExp=7; IntAct=EBI-750131, EBI-750131;
CC P04424; Q9BTE3-2: MCMBP; NbExp=6; IntAct=EBI-750131, EBI-9384556;
CC P04424; Q96HA8: NTAQ1; NbExp=7; IntAct=EBI-750131, EBI-741158;
CC P04424; O75382: TRIM3; NbExp=3; IntAct=EBI-750131, EBI-2129889;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P04424-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04424-2; Sequence=VSP_047256;
CC Name=3;
CC IsoId=P04424-3; Sequence=VSP_047255;
CC -!- PTM: Acetylation modifies enzyme activity in response to alterations of
CC extracellular nutrient availability. Acetylation increased with
CC trichostin A (TSA) or with nicotinamide (NAM). Glucose increases
CC acetylation by about a factor of 3 with decreasing enzyme activity.
CC Acetylation on Lys-288 is decreased on the addition of extra amino
CC acids resulting in activation of enzyme activity.
CC {ECO:0000269|PubMed:20167786}.
CC -!- DISEASE: Argininosuccinic aciduria (ARGINSA) [MIM:207900]: An autosomal
CC recessive disorder of the urea cycle. The disease is characterized by
CC mental and physical retardation, liver enlargement, skin lesions, dry
CC and brittle hair showing trichorrhexis nodosa microscopically and
CC fluorescing red, convulsions, and episodic unconsciousness.
CC {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433,
CC ECO:0000269|PubMed:12408190, ECO:0000269|PubMed:1705937,
CC ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:19703900,
CC ECO:0000269|PubMed:22081021, ECO:0000269|PubMed:2263616,
CC ECO:0000269|PubMed:24166829, ECO:0000269|PubMed:9045711}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. The phenotype heterogeneity among patients is associated with
CC interallelic complementation resulting in either complete loss of
CC activity or partial regeneration of functional active sites in the
CC heterotetrameric mutant protein. {ECO:0000269|PubMed:11747433}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51786.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y00753; CAA68722.1; -; mRNA.
DR EMBL; M14218; AAA51786.1; ALT_FRAME; mRNA.
DR EMBL; J03058; AAA51787.1; -; mRNA.
DR EMBL; M57638; AAA51788.1; -; mRNA.
DR EMBL; AF376770; AAL57276.1; -; Genomic_DNA.
DR EMBL; AC068533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008195; AAH08195.1; -; mRNA.
DR EMBL; BC033146; AAH33146.1; -; mRNA.
DR EMBL; M21007; AAA35566.1; -; Genomic_DNA.
DR EMBL; M21006; AAA35566.1; JOINED; Genomic_DNA.
DR CCDS; CCDS47597.1; -. [P04424-2]
DR CCDS; CCDS47598.1; -. [P04424-3]
DR CCDS; CCDS5531.1; -. [P04424-1]
DR PIR; A31658; WZHURS.
DR RefSeq; NP_000039.2; NM_000048.3. [P04424-1]
DR RefSeq; NP_001020114.1; NM_001024943.1. [P04424-1]
DR RefSeq; NP_001020115.1; NM_001024944.1. [P04424-2]
DR PDB; 1AOS; X-ray; 4.20 A; A/B=1-464.
DR PDB; 1K62; X-ray; 2.65 A; A/B=1-464.
DR PDBsum; 1AOS; -.
DR PDBsum; 1K62; -.
DR AlphaFoldDB; P04424; -.
DR SMR; P04424; -.
DR BioGRID; 106927; 20.
DR IntAct; P04424; 8.
DR STRING; 9606.ENSP00000307188; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB02267; Argininosuccinate.
DR iPTMnet; P04424; -.
DR MetOSite; P04424; -.
DR PhosphoSitePlus; P04424; -.
DR BioMuta; ASL; -.
DR EPD; P04424; -.
DR jPOST; P04424; -.
DR MassIVE; P04424; -.
DR MaxQB; P04424; -.
DR PaxDb; P04424; -.
DR PeptideAtlas; P04424; -.
DR PRIDE; P04424; -.
DR ProteomicsDB; 16946; -.
DR ProteomicsDB; 19811; -.
DR ProteomicsDB; 51704; -. [P04424-1]
DR Antibodypedia; 1530; 317 antibodies from 30 providers.
DR DNASU; 435; -.
DR Ensembl; ENST00000304874.14; ENSP00000307188.9; ENSG00000126522.17. [P04424-1]
DR Ensembl; ENST00000380839.9; ENSP00000370219.4; ENSG00000126522.17. [P04424-3]
DR Ensembl; ENST00000395331.4; ENSP00000378740.3; ENSG00000126522.17. [P04424-2]
DR Ensembl; ENST00000395332.8; ENSP00000378741.3; ENSG00000126522.17. [P04424-1]
DR Ensembl; ENST00000673518.1; ENSP00000499889.1; ENSG00000126522.17. [P04424-3]
DR GeneID; 435; -.
DR KEGG; hsa:435; -.
DR MANE-Select; ENST00000304874.14; ENSP00000307188.9; NM_000048.4; NP_000039.2.
DR UCSC; uc003tuo.4; human. [P04424-1]
DR CTD; 435; -.
DR DisGeNET; 435; -.
DR GeneCards; ASL; -.
DR GeneReviews; ASL; -.
DR HGNC; HGNC:746; ASL.
DR HPA; ENSG00000126522; Tissue enriched (liver).
DR MalaCards; ASL; -.
DR MIM; 207900; phenotype.
DR MIM; 608310; gene.
DR neXtProt; NX_P04424; -.
DR OpenTargets; ENSG00000126522; -.
DR Orphanet; 23; Argininosuccinic aciduria.
DR PharmGKB; PA25046; -.
DR VEuPathDB; HostDB:ENSG00000126522; -.
DR eggNOG; KOG1316; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR HOGENOM; CLU_027272_2_1_1; -.
DR InParanoid; P04424; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; P04424; -.
DR TreeFam; TF300656; -.
DR BioCyc; MetaCyc:HS10034-MON; -.
DR BRENDA; 4.3.2.1; 2681.
DR PathwayCommons; P04424; -.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; P04424; -.
DR SignaLink; P04424; -.
DR UniPathway; UPA00068; UER00114.
DR UniPathway; UPA00158; UER00273.
DR BioGRID-ORCS; 435; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; ASL; human.
DR EvolutionaryTrace; P04424; -.
DR GenomeRNAi; 435; -.
DR Pharos; P04424; Tbio.
DR PRO; PR:P04424; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P04424; protein.
DR Bgee; ENSG00000126522; Expressed in right lobe of liver and 97 other tissues.
DR ExpressionAtlas; P04424; baseline and differential.
DR Genevisible; P04424; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019676; P:ammonia assimilation cycle; IEA:Ensembl.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 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 PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis;
KW Arginine biosynthesis; Disease variant; Lyase; Reference proteome;
KW Urea cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q91YI0"
FT CHAIN 2..464
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137712"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 27
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 114
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 159
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain C"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 289
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 321
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 326
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 329
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT SITE 294
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q91YI0"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YI0"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20167786"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:20167786"
FT VAR_SEQ 176..201
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047255"
FT VAR_SEQ 307..326
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047256"
FT VARIANT 12
FT /note="R -> Q (in ARGINSA; 18-fold reduction in catalytic
FT efficiency toward argininosuccinate; dbSNP:rs145138923)"
FT /evidence="ECO:0000269|PubMed:11747432"
FT /id="VAR_085825"
FT VARIANT 31
FT /note="D -> N (in ARGINSA; reduction of argininosuccinate
FT lyase activity; no effect on protein expression;
FT dbSNP:rs754995756)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900"
FT /id="VAR_043106"
FT VARIANT 70
FT /note="V -> A (in ARGINSA; dbSNP:rs1027739421)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072186"
FT VARIANT 73
FT /note="E -> K (in ARGINSA; complete loss of
FT argininosuccinate lyase activity; abolishes protein
FT expression)"
FT /evidence="ECO:0000269|PubMed:19703900"
FT /id="VAR_075551"
FT VARIANT 87
FT /note="D -> G (in ARGINSA; loss of argininosuccinate lyase
FT activity; dbSNP:rs752100894)"
FT /evidence="ECO:0000269|PubMed:11747433,
FT ECO:0000269|PubMed:9045711"
FT /id="VAR_085826"
FT VARIANT 94
FT /note="R -> C (in ARGINSA; severe; dbSNP:rs374304304)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072187"
FT VARIANT 94
FT /note="R -> H (in ARGINSA; dbSNP:rs777437569)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072188"
FT VARIANT 95
FT /note="R -> C (in ARGINSA; loss of argininosuccinate lyase
FT activity; dbSNP:rs28940585)"
FT /evidence="ECO:0000269|PubMed:2263616"
FT /id="VAR_000676"
FT VARIANT 95
FT /note="R -> H (in ARGINSA; dbSNP:rs150244667)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072189"
FT VARIANT 104
FT /note="A -> V (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072190"
FT VARIANT 111
FT /note="R -> W (in ARGINSA; dbSNP:rs138310841)"
FT /evidence="ECO:0000269|PubMed:1705937"
FT /id="VAR_000677"
FT VARIANT 113
FT /note="R -> Q (in ARGINSA; complete loss of
FT argininosuccinate lyase activity; no effect on protein
FT expression; no effect on nitric oxide production;
FT dbSNP:rs752783461)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900, ECO:0000269|PubMed:22081021"
FT /id="VAR_043107"
FT VARIANT 120
FT /note="D -> E (in ARGINSA; severe)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072191"
FT VARIANT 121
FT /note="L -> H (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072192"
FT VARIANT 126
FT /note="R -> W (in ARGINSA; dbSNP:rs201962738)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072193"
FT VARIANT 146
FT /note="R -> W (in ARGINSA; dbSNP:rs199938613)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072194"
FT VARIANT 156
FT /note="P -> R (in ARGINSA; dbSNP:rs769017508)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072195"
FT VARIANT 160
FT /note="H -> N (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072196"
FT VARIANT 166
FT /note="P -> H (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072197"
FT VARIANT 168
FT /note="R -> H (in ARGINSA; dbSNP:rs727503811)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072198"
FT VARIANT 170
FT /note="S -> N (in ARGINSA; dbSNP:rs1180650883)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072199"
FT VARIANT 178
FT /note="V -> M (in ARGINSA; reduction of argininosuccinate
FT lyase activity; no effect on protein expression;
FT dbSNP:rs28941473)"
FT /evidence="ECO:0000269|PubMed:12408190,
FT ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:19703900"
FT /id="VAR_017572"
FT VARIANT 180
FT /note="L -> R (in ARGINSA; dbSNP:rs1057141162)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072200"
FT VARIANT 181
FT /note="T -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036281"
FT VARIANT 182
FT /note="R -> Q (in ARGINSA; reduction of argininosuccinate
FT lyase activity; reduces protein expression;
FT dbSNP:rs751590073)"
FT /evidence="ECO:0000269|PubMed:19703900,
FT ECO:0000269|PubMed:24166829"
FT /id="VAR_072201"
FT VARIANT 186
FT /note="R -> Q (in ARGINSA; reduction of argininosuccinate
FT lyase activity; reduces protein expression;
FT dbSNP:rs752397242)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900"
FT /id="VAR_043108"
FT VARIANT 191
FT /note="R -> W (in ARGINSA; dbSNP:rs143508372)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072202"
FT VARIANT 193
FT /note="R -> Q (in ARGINSA; dbSNP:rs373697663)"
FT /evidence="ECO:0000269|PubMed:1705937"
FT /id="VAR_000678"
FT VARIANT 193
FT /note="R -> W (in ARGINSA; dbSNP:rs1428029508)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072203"
FT VARIANT 200
FT /note="G -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036282"
FT VARIANT 205
FT /note="A -> V (in ARGINSA; dbSNP:rs796051925)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072204"
FT VARIANT 213
FT /note="R -> Q (in ARGINSA; dbSNP:rs1449589636)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072205"
FT VARIANT 227
FT /note="L -> P (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072206"
FT VARIANT 229
FT /note="S -> R (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072207"
FT VARIANT 229
FT /note="S -> T (in ARGINSA; dbSNP:rs1554327272)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072208"
FT VARIANT 231
FT /note="D -> E (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072209"
FT VARIANT 236
FT /note="R -> W (in ARGINSA; complete loss of
FT argininosuccinate lyase activity; no effect on protein
FT expression; no effect on NOS complex formation;
FT dbSNP:rs761268464)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900, ECO:0000269|PubMed:22081021"
FT /id="VAR_043109"
FT VARIANT 237
FT /note="D -> N (in ARGINSA; severe; dbSNP:rs552951774)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072210"
FT VARIANT 256
FT /note="M -> T (in ARGINSA; dbSNP:rs149057077)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072211"
FT VARIANT 262
FT /note="L -> P (in ARGINSA; dbSNP:rs1554327586)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072212"
FT VARIANT 286
FT /note="Q -> R (in ARGINSA; complete loss of
FT argininosuccinate lyase activity; no effect on protein
FT expression; dbSNP:rs28941472)"
FT /evidence="ECO:0000269|PubMed:11747432,
FT ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:1705937,
FT ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:19703900,
FT ECO:0000269|PubMed:9045711"
FT /id="VAR_000679"
FT VARIANT 295
FT /note="L -> P (in ARGINSA; dbSNP:rs1369337876)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072213"
FT VARIANT 297
FT /note="R -> Q (in ARGINSA; reduction of argininosuccinate
FT lyase activity; no effect on protein expression;
FT dbSNP:rs750431938)"
FT /evidence="ECO:0000269|PubMed:19703900"
FT /id="VAR_075552"
FT VARIANT 301
FT /note="G -> R (in ARGINSA; dbSNP:rs1161412459)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072214"
FT VARIANT 306
FT /note="R -> W (in ARGINSA; severe; dbSNP:rs868834862)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072215"
FT VARIANT 324
FT /note="D -> A (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072216"
FT VARIANT 326
FT /note="Q -> L (in ARGINSA; severe)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072217"
FT VARIANT 335
FT /note="V -> L (in ARGINSA; reduction of argininosuccinate
FT lyase activity; no effect on protein expression)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900"
FT /id="VAR_043110"
FT VARIANT 343
FT /note="L -> F (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072218"
FT VARIANT 343
FT /note="L -> P (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072219"
FT VARIANT 360
FT /note="M -> T (in ARGINSA; loss of argininosuccinate lyase
FT activity; may cause protein misfolding; dbSNP:rs875989948)"
FT /evidence="ECO:0000269|PubMed:11747433"
FT /id="VAR_085827"
FT VARIANT 368
FT /note="M -> V (in ARGINSA; dbSNP:rs1554328202)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072220"
FT VARIANT 379
FT /note="R -> C (in ARGINSA; dbSNP:rs28940287)"
FT /evidence="ECO:0000269|PubMed:12408190"
FT /id="VAR_017573"
FT VARIANT 380
FT /note="K -> E (in ARGINSA)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072221"
FT VARIANT 382
FT /note="M -> R (in ARGINSA; reduction of argininosuccinate
FT lyase activity; reduces protein expression)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900"
FT /id="VAR_043111"
FT VARIANT 385
FT /note="R -> C (in ARGINSA; dbSNP:rs28940286)"
FT /evidence="ECO:0000269|PubMed:12408190"
FT /id="VAR_017574"
FT VARIANT 385
FT /note="R -> H (in ARGINSA; dbSNP:rs746120802)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072222"
FT VARIANT 385
FT /note="R -> L (in ARGINSA; severe)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072223"
FT VARIANT 388
FT /note="H -> Q (in ARGINSA; severe)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072224"
FT VARIANT 398
FT /note="A -> D (in ARGINSA; impairs tetramer formation
FT likely due to protein misfolding; loss of argininosuccinate
FT lyase activity)"
FT /evidence="ECO:0000269|PubMed:11747433,
FT ECO:0000269|PubMed:9045711"
FT /id="VAR_085828"
FT VARIANT 433
FT /note="S -> R (in ARGINSA; dbSNP:rs796051928)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072225"
FT VARIANT 434
FT /note="V -> L (in ARGINSA; dbSNP:rs773071023)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072226"
FT VARIANT 447
FT /note="S -> N (in ARGINSA; dbSNP:rs373519615)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072227"
FT VARIANT 456
FT /note="R -> Q (in ARGINSA; dbSNP:rs767271619)"
FT /evidence="ECO:0000269|PubMed:24166829"
FT /id="VAR_072228"
FT VARIANT 456
FT /note="R -> W (in ARGINSA; reduction of argininosuccinate
FT lyase activity; reduces protein expression;
FT dbSNP:rs759396688)"
FT /evidence="ECO:0000269|PubMed:17326097,
FT ECO:0000269|PubMed:19703900"
FT /id="VAR_043112"
FT MUTAGEN 51
FT /note="K->N: 2-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:1705937"
FT MUTAGEN 89
FT /note="H->Q: 10-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:1705937"
FT MUTAGEN 288
FT /note="K->R: Refractory to inhibition by TSA and NAM and by
FT addition of extra amino acids. No effect on protein
FT structure."
FT /evidence="ECO:0000269|PubMed:20167786"
FT CONFLICT 246
FT /note="A -> R (in Ref. 1; CAA68722, 2; AAA51786, 3;
FT AAA51787, 4; AAA51788 and 5; AAL57276)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="G -> R (in Ref. 1; CAA68722)"
FT /evidence="ECO:0000305"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 57..76
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:1K62"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 113..150
FT /evidence="ECO:0007829|PDB:1K62"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1K62"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 169..194
FT /evidence="ECO:0007829|PDB:1K62"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1K62"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1K62"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 237..264
FT /evidence="ECO:0007829|PDB:1K62"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 291..314
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 328..352
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 384..400
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:1K62"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1K62"
FT HELIX 445..463
FT /evidence="ECO:0007829|PDB:1K62"
SQ SEQUENCE 464 AA; 51658 MW; F751625C1A581883 CRC64;
MASESGKLWG GRFVGAVDPI MEKFNASIAY DRHLWEVDVQ GSKAYSRGLE KAGLLTKAEM
DQILHGLDKV AEEWAQGTFK LNSNDEDIHT ANERRLKELI GATAGKLHTG RSRNDQVVTD
LRLWMRQTCS TLSGLLWELI RTMVDRAEAE RDVLFPGYTH LQRAQPIRWS HWILSHAVAL
TRDSERLLEV RKRINVLPLG SGAIAGNPLG VDRELLRAEL NFGAITLNSM DATSERDFVA
EFLFWASLCM THLSRMAEDL ILYCTKEFSF VQLSDAYSTG SSLMPQKKNP DSLELIRSKA
GRVFGRCAGL LMTLKGLPST YNKDLQEDKE AVFEVSDTMS AVLQVATGVI STLQIHQENM
GQALSPDMLA TDLAYYLVRK GMPFRQAHEA SGKAVFMAET KGVALNQLSL QELQTISPLF
SGDVICVWDY GHSVEQYGAL GGTARSSVDW QIRQVRALLQ AQQA
