ARLY1_ANAPL
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 25-MAY-2022, entry version 113.
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}.
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DR EMBL; M35133; AAC31659.1; -; mRNA.
DR PIR; JU0452; CYDKD1.
DR RefSeq; NP_001297344.1; NM_001310415.1.
DR RefSeq; XP_012963492.1; XM_013108038.1.
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 PDBsum; 1HY0; -.
DR PDBsum; 1U15; -.
DR PDBsum; 1U16; -.
DR AlphaFoldDB; P24057; -.
DR SMR; P24057; -.
DR Ensembl; ENSAPLT00020025514; ENSAPLP00020023645; ENSAPLG00020016403.
DR GeneID; 101796068; -.
DR KEGG; apla:101796068; -.
DR CTD; 435; -.
DR OrthoDB; 1074729at2759; -.
DR SABIO-RK; P24057; -.
DR EvolutionaryTrace; P24057; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005212; F:structural constituent of eye lens; TAS:UniProtKB.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
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; IPR020557; Fumarate_lyase_CS.
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.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
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
