ARLY2_CHICK
ID ARLY2_CHICK Reviewed; 466 AA.
AC P05083;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
DE AltName: Full=Delta crystallin II;
DE AltName: Full=Delta-2 crystallin;
GN Name=ASL2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3941090; DOI=10.1016/s0021-9258(17)36127-6;
RA Nickerson J.M., Wawrousek E.F., Borras T., Hawkins J.W., Norman B.L.,
RA Filpula D.R., Nagle J.W., Ally A.H., Piatigorsky J.;
RT "Sequence of the chicken delta 2 crystallin gene and its intergenic spacer.
RT Extreme homology with the delta 1 crystallin gene.";
RL J. Biol. Chem. 261:552-557(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RX PubMed=4018032; DOI=10.1002/j.1460-2075.1985.tb03649.x;
RA Borras T., Nickerson J.M., Chepelinsky A.B., Piatigorsky J.;
RT "Structural and functional evidence for differential promoter activity of
RT the two linked delta-crystallin genes in the chicken.";
RL EMBO J. 4:445-452(1985).
CC -!- FUNCTION: Delta crystallin, the principal crystallin in embryonic lens,
CC is found only in birds and reptiles. This protein may also function as
CC an enzymatically active argininosuccinate lyase.
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC -!- SUBUNIT: Homotetramer.
CC -!- TISSUE SPECIFICITY: Eye lens.
CC -!- MISCELLANEOUS: It is uncertain if this gene is expressed.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; M10806; AAA48727.1; -; Genomic_DNA.
DR EMBL; X02188; CAA26129.1; -; Genomic_DNA.
DR PIR; A25622; CYCHD2.
DR RefSeq; NP_001025885.1; NM_001030714.1.
DR AlphaFoldDB; P05083; -.
DR SMR; P05083; -.
DR STRING; 9031.ENSGALP00000004034; -.
DR PaxDb; P05083; -.
DR Ensembl; ENSGALT00000080158; ENSGALP00000057554; ENSGALG00000002576.
DR GeneID; 417545; -.
DR KEGG; gga:417545; -.
DR CTD; 435; -.
DR VEuPathDB; HostDB:geneid_417545; -.
DR eggNOG; KOG1316; Eukaryota.
DR GeneTree; ENSGT00950000183122; -.
DR InParanoid; P05083; -.
DR OrthoDB; 1074729at2759; -.
DR PhylomeDB; P05083; -.
DR Reactome; R-GGA-187630; Arginine metabolism.
DR UniPathway; UPA00068; UER00114.
DR PRO; PR:P05083; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000002576; Expressed in ovary and 12 other tissues.
DR ExpressionAtlas; P05083; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0006525; P:arginine metabolic process; TAS:Reactome.
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; 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.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Eye lens protein; Lyase;
KW Reference proteome.
FT CHAIN 1..466
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137720"
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"
SQ SEQUENCE 466 AA; 51044 MW; 4EC67B371D4BBCB8 CRC64;
MASEGDKLWG GRFSGSTDPI MEMLNSSIAC DQRLSEVDIQ GSMAYAKALE KAGILTKTEL
EKILSGLEKI SEEWSKGVFV VKQSDEDIHT ANERRLKELI GDIAGKLHTG RSRNDQVVTD
LKLLLKSSIS VISTHLLQLI KTLVERAATE IDVIMPGYTH LQKALPIRWS QFLLSHAVAL
IRDSERLGEV KKRMSVLPLG SGALAGNPLE IDRELLRSEL DFASISLNSM DAISERDFVV
ELLSVATLLM IHLSKLAEDL IIFSTTEFGF VTLSDAYSTG SSLLPQKKNP DSLELIRSKA
GRVFGRLAAV LMVLKGLPST YNKDLQEDKE AVFDVVDTLT AVLQVATGVI STLQVNKENM
EKALTPELLS TDLALYLVRK GMPFRQAHVA SGKAVHLAET KGIAINKLTL EDLKSISPLF
ASDVSQVFNI VNSVEQYTAV GGTAKSSVTA QIEQLRELLK KQKEQA
