ID ARLY1_ANAPL Reviewed; 466 AA. AC P24057; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 02-SEP-2026, entry version 126. DE RecName: Full=Delta-1 crystallin; DE AltName: Full=Delta crystallin I; GN Name=ASL1; OS Anas platyrhynchos (Mallard) (Anas boschas). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anatinae; Anas. OX NCBI_TaxID=8839; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Lens; RX PubMed=2269436; DOI=10.1016/0378-1119(90)90262-p; RA Wistow G.J., Piatigorsky J.; RT "Gene conversion and splice-site slippage in the argininosuccinate RT lyases/delta-crystallins of the duck lens: members of an enzyme RT superfamily."; RL Gene 96:263-270(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-54. RX PubMed=2822941; DOI=10.1007/bf02603115; RA Piatigorsky J., Norman B., Jones R.E.; RT "Conservation of delta-crystallin gene structure between ducks and RT chickens."; RL J. Mol. Evol. 25:308-317(1987). RN [3] RP PROTEIN SEQUENCE OF 8-21, AND FUNCTION. RC TISSUE=Lens; RX PubMed=7944404; DOI=10.1006/abbi.1994.1408; RA Lee H.J., Lin C.C., Chiou S.-H., Chang G.G.; RT "Characterization of the multiple forms of duck lens delta-crystallin with RT endogenous argininosuccinate lyase activity."; RL Arch. Biochem. Biophys. 314:31-38(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. RX PubMed=11258884; DOI=10.1021/bi002272k; RA Sampaleanu L.M., Vallee F., Slingsby C., Howell P.L.; RT "Structural studies of duck delta 1 and delta 2 crystallin suggest RT conformational changes occur during catalysis."; RL Biochemistry 40:2732-2742(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. RX PubMed=15362851; DOI=10.1021/bi0489006; RA Tsai M., Sampaleanu L.M., Greene C., Creagh L., Haynes C., Howell P.L.; RT "A duck delta1 crystallin double loop mutant provides insight into residues RT important for argininosuccinate lyase activity."; RL Biochemistry 43:11672-11682(2004). CC -!- FUNCTION: Delta crystallin, the principal crystallin in embryonic lens, CC is found only in birds and reptiles. Despite possessing the necessary CC catalytic residues, this protein does not function as an enzymatically CC active argininosuccinate lyase. {ECO:0000269|PubMed:7944404}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11258884, CC ECO:0000269|PubMed:15362851}. CC -!- TISSUE SPECIFICITY: Eye lens. {ECO:0000269|PubMed:2269436}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35133; AAC31659.1; -; mRNA. DR PIR; JU0452; CYDKD1. DR RefSeq; NP_001297344.1; NM_001310415.2. DR PDB; 1HY0; X-ray; 2.20 A; A/B=1-466. DR PDB; 1U15; X-ray; 2.50 A; A/B/C/D=1-466. DR PDB; 1U16; X-ray; 2.20 A; A=1-466. DR AlphaFoldDB; P24057; -. DR SMR; P24057; -. DR Ensembl; ENSAPLT00020025514; ENSAPLP00020023645; ENSAPLG00020016403. DR GeneID; 101796068; -. DR KEGG; apla:101796068; -. DR CTD; 435; -. DR OrthoDB; 2561043at2759; -. DR SABIO-RK; P24057; -. DR EvolutionaryTrace; P24057; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005212; F:structural constituent of eye lens; TAS:UniProtKB. DR CDD; cd01359; Argininosuccinate_lyase; 1. DR FunFam; 1.10.275.10:FF:000002; Argininosuccinate lyase; 1. DR FunFam; 1.10.40.30:FF:000001; Argininosuccinate lyase; 1. DR FunFam; 1.20.200.10:FF:000002; Argininosuccinate lyase; 1. DR FunFam; 1.20.200.10:FF:000015; argininosuccinate lyase isoform X2; 1. DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1. DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1. DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1. DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1. DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1. DR Pfam; PF14698; ASL_C2; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00145; ARGSUCLYASE. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; L-aspartase-like; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. DR PDBsum; 1HY0; -. DR PDBsum; 1U15; -. DR PDBsum; 1U16; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Eye lens protein. FT CHAIN 1..466 FT /note="Delta-1 crystallin" FT /id="PRO_0000137716" FT CONFLICT 11 FT /note="G -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 19..23 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 28..33 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 35..51 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 57..75 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 88..100 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 101..108 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 113..149 FT /evidence="ECO:0007829|PDB:1HY0" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 154..159 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 169..194 FT /evidence="ECO:0007829|PDB:1HY0" FT TURN 202..205 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 213..220 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 229..234 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 237..263 FT /evidence="ECO:0007829|PDB:1HY0" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 291..314 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:1U15" FT HELIX 323..327 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 328..352 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 357..363 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 366..369 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 370..379 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 384..401 FT /evidence="ECO:0007829|PDB:1HY0" FT TURN 405..407 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 410..414 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 422..427 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 430..435 FT /evidence="ECO:0007829|PDB:1HY0" FT STRAND 442..444 FT /evidence="ECO:0007829|PDB:1HY0" FT HELIX 445..463 FT /evidence="ECO:0007829|PDB:1HY0" SQ SEQUENCE 466 AA; 51136 MW; 4663F87DED299879 CRC64; MASEGDKLMG GRFVGSTDPI MQMLSTSIST EQRLSEVDIQ ASIAYAKALE KAGILTKTEL EKILSGLEKI SEELSKGVIV VTQSDEDIQT ANERRLKELI GDIAGKLHTG RSRNEQVVTD LKLFMKNSLS IISTHLLQLI KTLVERAAIE IDVILPGYTH LQKAQPIRWS QFLLSHAVAL TRDSERLGEV KKRINVLPLG SGALAGNPLD IDREMLRSEL EFASISLNSM DAISERDFVV EFLSVATLLL IHLSKMAEDL IIYSTSEFGF LTLSDAFSTG SSLMPQKKNP DSLELIRSKA GRVFGRLASI LMVLKGLPST YNKDLQEDKE AVIDVVDTLT AVLQVATGVI STLQISKENM EKALTPEMLA TDLALYLVRK GMPFRQAHTA SGKAVHLAET KGIAINNLTL EDLKSISPLF SSDVSQVFNF VNSVEQYTAL GGTAKSSVTT QIEQLRELMK KQKEQA //