P24057 (ARLY1_ANAPL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Delta-1 crystallin

Alternative name(s):
Delta crystallin I

Gene names

Name:

ASL1

Organism

Anas platyrhynchos (Domestic duck) (Anas boschas)

Taxonomic identifier

8839 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Anseriformes › Anatidae › Anas

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. Despite possessing the necessary catalytic residues, this protein does not function as an enzymatically active argininosuccinate lyase. Ref.3
Subunit structure	Homotetramer. Ref.4 Ref.5
Tissue specificity	Eye lens. Ref.1
Sequence similarities	Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.

Ontologies

Keywords
Molecular function	Eye lens protein
Technical term	3D-structure Direct protein sequencing
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: InterPro structural constituent of eye lens Traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 466

466

Delta-1 crystallin

PRO_0000137716

Experimental info

Sequence conflict

11

1

G → Q AA sequence Ref.3

Secondary structure

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466

Helix Strand Turn

Details...

Helix

19 – 23

5

Helix

28 – 33

6

Helix

35 – 51

17

Helix

57 – 75

19

Beta strand

85 – 87

3

Helix

88 – 100

13

Helix

101 – 108

8

Helix

113 – 149

37

Turn

150 – 152

3

Beta strand

154 – 159

6

Beta strand

162 – 168

7

Helix

169 – 194

26

Turn

202 – 205

4

Helix

213 – 220

8

Beta strand

223 – 225

3

Helix

229 – 234

6

Helix

237 – 263

27

Turn

266 – 268

3

Beta strand

270 – 272

3

Helix

275 – 277

3

Helix

291 – 314

24

Helix

323 – 327

5

Helix

328 – 352

25

Helix

357 – 363

7

Helix

366 – 369

4

Helix

370 – 379

10

Helix

384 – 401

18

Turn

405 – 407

3

Helix

410 – 414

5

Helix

422 – 427

6

Helix

430 – 435

6

Beta strand

442 – 444

3

Helix

445 – 463

19

Sequences

	Sequence		Length	Mass (Da)
	P24057 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 4663F87DED299879	FASTA	466	51,136
	10 20 30 40 50 60 MASEGDKLMG GRFVGSTDPI MQMLSTSIST EQRLSEVDIQ ASIAYAKALE KAGILTKTEL 70 80 90 100 110 120 EKILSGLEKI SEELSKGVIV VTQSDEDIQT ANERRLKELI GDIAGKLHTG RSRNEQVVTD 130 140 150 160 170 180 LKLFMKNSLS IISTHLLQLI KTLVERAAIE IDVILPGYTH LQKAQPIRWS QFLLSHAVAL 190 200 210 220 230 240 TRDSERLGEV KKRINVLPLG SGALAGNPLD IDREMLRSEL EFASISLNSM DAISERDFVV 250 260 270 280 290 300 EFLSVATLLL IHLSKMAEDL IIYSTSEFGF LTLSDAFSTG SSLMPQKKNP DSLELIRSKA 310 320 330 340 350 360 GRVFGRLASI LMVLKGLPST YNKDLQEDKE AVIDVVDTLT AVLQVATGVI STLQISKENM 370 380 390 400 410 420 EKALTPEMLA TDLALYLVRK GMPFRQAHTA SGKAVHLAET KGIAINNLTL EDLKSISPLF 430 440 450 460 SSDVSQVFNF VNSVEQYTAL GGTAKSSVTT QIEQLRELMK KQKEQA

References

[1]	"Gene conversion and splice-site slippage in the argininosuccinate lyases/delta-crystallins of the duck lens: members of an enzyme superfamily." Wistow G.J., Piatigorsky J. Gene 96:263-270(1990) [PubMed: 2269436] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Lens.
[2]	"Conservation of delta-crystallin gene structure between ducks and chickens." Piatigorsky J., Norman B., Jones R.E. J. Mol. Evol. 25:308-317(1987) [PubMed: 2822941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-54.
[3]	"Characterization of the multiple forms of duck lens delta-crystallin with endogenous argininosuccinate lyase activity." Lee H.J., Lin C.C., Chiou S.-H., Chang G.G. Arch. Biochem. Biophys. 314:31-38(1994) [PubMed: 7944404] [Abstract] Cited for: PROTEIN SEQUENCE OF 8-21, FUNCTION. Tissue: Lens.
[4]	"Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis." Sampaleanu L.M., Vallee F., Slingsby C., Howell P.L. Biochemistry 40:2732-2742(2001) [PubMed: 11258884] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT.
[5]	"A duck delta1 crystallin double loop mutant provides insight into residues important for argininosuccinate lyase activity." Tsai M., Sampaleanu L.M., Greene C., Creagh L., Haynes C., Howell P.L. Biochemistry 43:11672-11682(2004) [PubMed: 15362851] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35133 mRNA. Translation: AAC31659.1.

PIR

CYDKD1. JU0452.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HY0	X-ray	2.20	A/B	1-466	[»]
1U15	X-ray	2.50	A/B/C/D	1-466	[»]
1U16	X-ray	2.20	A	1-466	[»]

ProteinModelPortal

P24057.

SMR

P24057. Positions 18-465.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG004281.

Family and domain databases

InterPro

IPR009049. Argininosuccinate_lyase.
IPR003031. D_crystallin.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR022761. Lyase1_N.
[Graphical view]

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. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARLY1_ANAPL

Accession

Primary (citable) accession number: P24057

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 31, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program