CRYL1_RABIT
ID CRYL1_RABIT Reviewed; 319 AA.
AC P14755; A7VMV1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Lambda-crystallin;
DE EC=1.1.1.45 {ECO:0000269|PubMed:15809331};
DE AltName: Full=L-gulonate 3-dehydrogenase;
DE Short=Gul3DH;
GN Name=CRYL1; Synonyms=GUL3DH;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACETYLATION AT ALA-2, AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Lens;
RX PubMed=3170592; DOI=10.1016/s0021-9258(19)37611-2;
RA Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H.,
RA de Jong W.W.;
RT "Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-
RT coenzyme A dehydrogenases.";
RL J. Biol. Chem. 263:15462-15466(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ASP-36; SER-124; HIS-145; GLU-157 AND ASN-196, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=15809331; DOI=10.1093/jb/mvi033;
RA Ishikura S., Usami N., Araki M., Hara A.;
RT "Structural and functional characterization of rabbit and human L-gulonate
RT 3-dehydrogenase.";
RL J. Biochem. 137:303-314(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NAD.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the rabbit L-gulonate 3-dehydrogenase.";
RL Submitted (NOV-2006) to the PDB data bank.
CC -!- FUNCTION: Functions as crystallin in the rabbit eye lens. Has high L-
CC gulonate 3-dehydrogenase activity. It also exhibits low dehydrogenase
CC activity toward L-3-hydroxybutyrate (HBA) and L-threonate.
CC {ECO:0000269|PubMed:15809331}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH;
CC Xref=Rhea:RHEA:12889, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945; EC=1.1.1.45;
CC Evidence={ECO:0000269|PubMed:15809331};
CC -!- ACTIVITY REGULATION: Inhibited by malonate and by inorganic phosphate.
CC {ECO:0000269|PubMed:15809331}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.011 mM for NAD {ECO:0000269|PubMed:15809331};
CC KM=0.0005 mM for NADH {ECO:0000269|PubMed:15809331};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15809331, ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15809331}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens, kidney, liver, heart, lung,
CC brain and testis. {ECO:0000269|PubMed:15809331}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M22743; AAA31207.1; -; mRNA.
DR EMBL; AB359905; BAF76380.1; -; mRNA.
DR PIR; A31992; A31992.
DR RefSeq; NP_001075747.1; NM_001082278.1.
DR PDB; 3ADO; X-ray; 1.70 A; A=1-319.
DR PDB; 3ADP; X-ray; 1.85 A; A=1-319.
DR PDBsum; 3ADO; -.
DR PDBsum; 3ADP; -.
DR AlphaFoldDB; P14755; -.
DR SMR; P14755; -.
DR STRING; 9986.ENSOCUP00000011580; -.
DR MoonProt; P14755; -.
DR iPTMnet; P14755; -.
DR GeneID; 100009108; -.
DR KEGG; ocu:100009108; -.
DR CTD; 51084; -.
DR eggNOG; KOG2305; Eukaryota.
DR InParanoid; P14755; -.
DR OrthoDB; 840631at2759; -.
DR BRENDA; 1.1.1.45; 1749.
DR SABIO-RK; P14755; -.
DR EvolutionaryTrace; P14755; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Eye lens protein; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..319
FT /note="Lambda-crystallin"
FT /id="PRO_0000109322"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305|PubMed:3170592"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811X6"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2S2"
FT MUTAGEN 36
FT /note="D->R: Reduces enzyme activity and alters
FT specificity, so that NADP can be used as cosubstrate."
FT /evidence="ECO:0000269|PubMed:15809331"
FT MUTAGEN 124
FT /note="S->A: Reduces enzyme activity 500-fold."
FT /evidence="ECO:0000269|PubMed:15809331"
FT MUTAGEN 145
FT /note="H->Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:15809331"
FT MUTAGEN 157
FT /note="E->Q: No major effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:15809331"
FT MUTAGEN 196
FT /note="N->D,Q: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:15809331"
FT CONFLICT 252
FT /note="C -> S (in Ref. 1; AAA31207)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="V -> G (in Ref. 1; AAA31207)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="R -> RE (in Ref. 1; AAA31207)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3ADO"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 128..132
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3ADO"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3ADO"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3ADO"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:3ADO"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:3ADO"
FT HELIX 292..315
FT /evidence="ECO:0007829|PDB:3ADO"
SQ SEQUENCE 319 AA; 35202 MW; C6F66B558BA422F6 CRC64;
MASPAAGDVL IVGSGLVGRS WAMLFASGGF RVKLYDIEPR QITGALENIR KEMKSLQQSG
SLKGSLSAEE QLSLISSCTN LAEAVEGVVH IQECVPENLD LKRKIFAQLD SIVDDRVVLS
SSSSCLLPSK LFTGLAHVKQ CIVAHPVNPP YYIPLVELVP HPETSPATVD RTHALMRKIG
QSPVRVLKEI DGFVLNRLQY AIISEAWRLV EEGIVSPSDL DLVMSDGLGM RYAFIGPLET
MHLNAEGMLS YCDRYSEGMK RVLKSFGSIP EFSGATVEKV NQAMCKKVPA DPEHLAARRE
WRDECLKRLA KLKRQMQPQ
