Q01592 (ARLY_COLLI) 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

Gene names

Name:	ASL
Synonyms:	DELTAP

Organism

Columba livia (Domestic pigeon)

Taxonomic identifier

8932 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Columbiformes › Columbidae › Columba

Protein attributes

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

General annotation (Comments)

Function	Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein also functions as an enzymatically active argininosuccinate lyase, but it has a low activity.
Catalytic activity	2-(N(omega)-L-arginino)succinate = fumarate + L-arginine. Ref.2
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3.
Subunit structure	Homotetramer. Ref.2
Tissue specificity	Eye lens. Ref.1 Ref.2
Post-translational modification	The N-terminus is blocked.
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
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_0000137721
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)
	Q01592 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 86EBBD1E19D9627E	FASTA	466	51,086
	10 20 30 40 50 60 MASEGDKMLG GRFVGSTDPV MEMLSASITI DQRLAEVDIQ GSMAYAKALE KAGILSKSEL 70 80 90 100 110 120 EKTLSGLEKI SEEWSKGVFV VTPTDEDIHT ANERRLKELI GDIAGKLHTG RSRNDQVVTD 130 140 150 160 170 180 LKLFMKNSLS VISTHLLQLI KTLVERAAIE VDVILPGYTH LQKTQPIRWS QFLLSHAVAL 190 200 210 220 230 240 TRDSERLGEI KKRINILPLG SGALAGNPLE IDRELLRSEL DFASISLNSM DAVRQRDSVV 250 260 270 280 290 300 EFLSVAALLM IHLSKMAEDL IIYSTSEFGF LTLSDTYCTG SSVMPQKKNP DSLELIRSKA 310 320 330 340 350 360 GRVFGRLAAI LMVLKGLPST YNKDLQEDKE AVFDVVDTLN AVLQVATGVI STLQINKENM 370 380 390 400 410 420 EKALSPEILS SDLALYLVHK GMPFRQAHVA SGKAVHLAES KGITLNNLSL DDLKSISPLF 430 440 450 460 GSDVSQVFNV VNSVEQYTAL GGTAKSSVTA QIEQLRELLK RHKEQA

References

[1]	"Sequence analysis of pigeon delta-crystallin gene and its deduced primary structure. Comparison of avian delta-crystallins with and without endogenous argininosuccinate lyase activity." Lin C.-W., Chiou S.-H. FEBS Lett. 311:276-280(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Lens.
[2]	"Biochemical characterization of crystallins from pigeon lenses: structural and sequence analysis of pigeon delta-crystallin." Chiou S.-H., Hung C.-C., Lin C.-W. Biochim. Biophys. Acta 1160:317-324(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-100, CATALYTIC ACTIVITY, SUBUNIT, BLOCKAGE OF N-TERMINUS, TISSUE SPECIFICITY. Tissue: Lens.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X66404 mRNA. Translation: CAA47031.1.
PIR	S29247.
3D structure databases
ProteinModelPortal	Q01592.
SMR	Q01592. Positions 16-465.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG004281.
Enzyme and pathway databases
UniPathway	UPA00068; UER00114.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
InterPro	IPR009049. Argininosuccinate_lyase. IPR003031. D_crystallin. IPR024083. Fumarase/histidase_N. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view]
PANTHER	PTHR11444:SF3. PTHR11444:SF3. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARLY_COLLI

Accession

Primary (citable) accession number: Q01592

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program