P05083 (ARLY2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Argininosuccinate lyase
Short name=ASAL
EC=4.3.2.1

Alternative name(s):
Arginosuccinase
Delta crystallin II
Delta-2 crystallin

Gene names

Name:

ASL2

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein may also function as an enzymatically active argininosuccinate lyase.
Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subunit structure	Homotetramer.
Tissue specificity	Eye lens.
Miscellaneous	It is uncertain if this gene is expressed.
Sequence similarities	Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Molecular function	Eye lens protein Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process via ornithine Inferred from electronic annotation. Source: InterPro
Molecular function	argininosuccinate lyase activity Inferred from electronic annotation. Source: EC structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 466	466	Argininosuccinate lyase		PRO_0000137720
Regions
	Region	112 – 114	3	Substrate binding By similarity
Sites
	Active site	160	1	Proton acceptor; shared with tetrameric partner 2 By similarity
	Active site	281	1	Proton acceptor; shared with tetrameric partner 1 By similarity
	Active site	294	1	Charge relay system; shared with tetrameric partner 1 By similarity
	Binding site	27	1	Substrate By similarity
	Binding site	89	1	Substrate By similarity
	Binding site	159	1	Substrate; shared with tetrameric partner 2 By similarity
	Binding site	287	1	Substrate; shared with tetrameric partner 1 By similarity
	Binding site	321	1	Substrate By similarity
	Binding site	326	1	Substrate By similarity
	Binding site	329	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P05083 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 4EC67B371D4BBCB8	FASTA	466	51,044
	10 20 30 40 50 60 MASEGDKLWG GRFSGSTDPI MEMLNSSIAC DQRLSEVDIQ GSMAYAKALE KAGILTKTEL 70 80 90 100 110 120 EKILSGLEKI SEEWSKGVFV VKQSDEDIHT ANERRLKELI GDIAGKLHTG RSRNDQVVTD 130 140 150 160 170 180 LKLLLKSSIS VISTHLLQLI KTLVERAATE IDVIMPGYTH LQKALPIRWS QFLLSHAVAL 190 200 210 220 230 240 IRDSERLGEV KKRMSVLPLG SGALAGNPLE IDRELLRSEL DFASISLNSM DAISERDFVV 250 260 270 280 290 300 ELLSVATLLM IHLSKLAEDL IIFSTTEFGF VTLSDAYSTG SSLLPQKKNP DSLELIRSKA 310 320 330 340 350 360 GRVFGRLAAV LMVLKGLPST YNKDLQEDKE AVFDVVDTLT AVLQVATGVI STLQVNKENM 370 380 390 400 410 420 EKALTPELLS TDLALYLVRK GMPFRQAHVA SGKAVHLAET KGIAINKLTL EDLKSISPLF 430 440 450 460 ASDVSQVFNI VNSVEQYTAV GGTAKSSVTA QIEQLRELLK KQKEQA

References

[1]	"Sequence of the chicken delta 2 crystallin gene and its intergenic spacer. Extreme homology with the delta 1 crystallin gene." Nickerson J.M., Wawrousek E.F., Borras T., Hawkins J.W., Norman B.L., Filpula D.R., Nagle J.W., Ally A.H., Piatigorsky J. J. Biol. Chem. 261:552-557(1986) [PubMed: 3941090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural and functional evidence for differential promoter activity of the two linked delta-crystallin genes in the chicken." Borras T., Nickerson J.M., Chepelinsky A.B., Piatigorsky J. EMBO J. 4:445-452(1985) [PubMed: 4018032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M10806 Genomic DNA. Translation: AAA48727.1. X02188 Genomic DNA. Translation: CAA26129.1.
IPI	IPI00579936.
PIR	CYCHD2. A25622.
RefSeq	NP_001025885.1. NM_001030714.1.
UniGene	Gga.17624.
3D structure databases
ProteinModelPortal	P05083.
SMR	P05083. Positions 18-462.
ModBase	Search...
Protein-protein interaction databases
STRING	P05083.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	417545.
KEGG	gga:417545.
Organism-specific databases
CTD	417545.
Phylogenomic databases
eggNOG	veNOG06663.
HOVERGEN	HBG004281.
PhylomeDB	P05083.
Family and domain databases
InterPro	IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR000362. Fumarate_lyase. IPR008948. L-Aspartase-like. IPR022761. Lyase1_N. [Graphical view]
KO	K01755.
PANTHER	PTHR11444:SF3. argH. 1 hit.
Pfam	PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00838. ArgH. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARLY2_CHICK

Accession

Primary (citable) accession number: P05083

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 16, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program