ARLY1_MELGA
ID ARLY1_MELGA Reviewed; 466 AA.
AC Q7SIE0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Delta-1 crystallin;
DE AltName: Full=Delta crystallin I;
GN Name=ASL1;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1] {ECO:0000312|PDB:1I0A}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), SUBUNIT, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Delta crystallin, the principal crystallin in embryonic lens,
CC is found only in birds and reptiles. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11258884}.
CC -!- TISSUE SPECIFICITY: Eye lens. {ECO:0000269|PubMed:11258884}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000250|UniProtKB:P24057}.
CC -!- CAUTION: Despite possessing the necessary catalytic residues, this
CC protein does not function as an enzymatically active argininosuccinate
CC lyase. {ECO:0000305}.
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DR PDB; 1I0A; X-ray; 2.50 A; A/B/C/D=1-466.
DR PDBsum; 1I0A; -.
DR AlphaFoldDB; Q7SIE0; -.
DR SMR; Q7SIE0; -.
DR InParanoid; Q7SIE0; -.
DR EvolutionaryTrace; Q7SIE0; -.
DR Proteomes; UP000001645; Unplaced.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Eye lens protein; Reference proteome.
FT CHAIN 1..466
FT /note="Delta-1 crystallin"
FT /id="PRO_0000233914"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 113..149
FT /evidence="ECO:0007829|PDB:1I0A"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1I0A"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1I0A"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 169..194
FT /evidence="ECO:0007829|PDB:1I0A"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:1I0A"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 237..263
FT /evidence="ECO:0007829|PDB:1I0A"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1I0A"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 291..314
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 328..352
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 384..400
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 410..414
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 430..434
FT /evidence="ECO:0007829|PDB:1I0A"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1I0A"
FT HELIX 445..460
FT /evidence="ECO:0007829|PDB:1I0A"
SQ SEQUENCE 466 AA; 50836 MW; 9E357C227B0C2815 CRC64;
MATEGDKLLG GRFVGSVDPI MEILSSSIST EQRLTEVDIQ ASMAYAKALE KASILTKTEL
EKILSGLEKI SEESSKGVLV MTQSDEDIQT AIERRLKELI GDIAGKLQTG RSRNEQVVTD
LKLLLKSSIS VISTHLLQLI KTLVERAAIE IDIIMPGYTH LQKALPIRWS QFLLSHAVAL
TRDSERLGEV KKRITVLPLG SGVLAGNPLE IDRELLRSEL DMTSITLNSI DAISERDFVV
ELISVATLLM IHLSKLAEDL IIFSTTEFGF VTLSDAYSTG SSLLPQKKNP DSLELIRSKA
GRVFGRLAAI LMVLKGIPST FSKDLQEDKE AVLDVVDTLT AVLQVATGVI STLQINKENM
EKALTPELLS TDLALYLVRK GMPIRQAQTA SGKAVHLAET KGITINNLTL EDLKSISPLF
ASDVSQVFSV VNSVEQYTAV GGTAKSSVTA QIEQLRELLK KQKEQA
