CRYL1_RAT
ID CRYL1_RAT Reviewed; 319 AA.
AC Q811X6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Lambda-crystallin homolog;
DE EC=1.1.1.45 {ECO:0000250|UniProtKB:Q9Y2S2};
DE AltName: Full=L-gulonate 3-dehydrogenase;
DE Short=Gul3DH;
GN Name=Cryl1; Synonyms=Cry;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12527201; DOI=10.1016/s0378-1119(02)01095-8;
RA Chen J., Yu L., Li D., Gao Q., Wang J., Huang X., Bi G., Wu H., Zhao S.;
RT "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and kidney
RT and downregulated in 58% of liver cancer tissues from 60 Chinese patients,
RT and four new homologs from other mammalians.";
RL Gene 302:103-113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Has high L-gulonate 3-dehydrogenase activity. It also
CC exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA)
CC and L-threonate. {ECO:0000250|UniProtKB:Q9Y2S2}.
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:0000250|UniProtKB:Q9Y2S2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12890;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2S2};
CC -!- ACTIVITY REGULATION: Inhibited by malonate.
CC {ECO:0000250|UniProtKB:Q9Y2S2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9Y2S2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14755}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {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; AY040223; AAK72608.1; -; mRNA.
DR EMBL; BC078685; AAH78685.1; -; mRNA.
DR RefSeq; NP_786933.1; NM_175757.2.
DR AlphaFoldDB; Q811X6; -.
DR SMR; Q811X6; -.
DR STRING; 10116.ENSRNOP00000012093; -.
DR iPTMnet; Q811X6; -.
DR PhosphoSitePlus; Q811X6; -.
DR PaxDb; Q811X6; -.
DR PRIDE; Q811X6; -.
DR Ensembl; ENSRNOT00000012093; ENSRNOP00000012093; ENSRNOG00000008989.
DR GeneID; 290277; -.
DR KEGG; rno:290277; -.
DR UCSC; RGD:631427; rat.
DR CTD; 51084; -.
DR RGD; 631427; Cryl1.
DR eggNOG; KOG2305; Eukaryota.
DR GeneTree; ENSGT00390000007182; -.
DR HOGENOM; CLU_009834_0_0_1; -.
DR InParanoid; Q811X6; -.
DR OMA; RDNCLTH; -.
DR OrthoDB; 840631at2759; -.
DR PhylomeDB; Q811X6; -.
DR TreeFam; TF313501; -.
DR Reactome; R-RNO-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:Q811X6; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000008989; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q811X6; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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 Acetylation; Cytoplasm; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P14755"
FT CHAIN 2..319
FT /note="Lambda-crystallin homolog"
FT /id="PRO_0000232508"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P14755"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 319 AA; 35341 MW; AA53EFBD64C98505 CRC64;
MASPAAGGVV IIGSGLIGRS WAMLFASGGF KVKLYDIEQQ QITNALESIR KEMKSLEQSG
SLKGSLGAEQ QLSLISGCGN LAEAVEGAMH IQECVPENLE LKKKIFAQLD RIVDDQVILS
SSSSCLLPSK LFTGLAHVKQ CIVAHPVNPP YYVPLVELVP HPETAPATMD RTYALMKKIR
QTPVRVLKEI DGFVLNRLQY AIISEAWRLV EEGIVSPNDL DLVMSDGLGM RYAFIGPLET
MHLNAEGMVS YCDRYSEGMK RVLKTFGPVP EFSGDTVEKV NQDMCMKVPD DPEHLAARRH
WRDDCLMQLS KLKHQMQPQ
