ID   CRYL1_BOVIN             Reviewed;         321 AA.
AC   Q8SPX7;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 108.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
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).
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}.
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DR   EMBL; AF480862; AAL88550.1; -; mRNA.
DR   RefSeq; NP_776718.1; NM_174293.2.
DR   AlphaFoldDB; Q8SPX7; -.
DR   SMR; Q8SPX7; -.
DR   STRING; 9913.ENSBTAP00000015575; -.
DR   PaxDb; Q8SPX7; -.
DR   PRIDE; Q8SPX7; -.
DR   Ensembl; ENSBTAT00000015575; ENSBTAP00000015575; ENSBTAG00000011726.
DR   GeneID; 281725; -.
DR   KEGG; bta:281725; -.
DR   CTD; 51084; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011726; -.
DR   VGNC; VGNC:27744; CRYL1.
DR   eggNOG; KOG2305; Eukaryota.
DR   GeneTree; ENSGT00390000007182; -.
DR   HOGENOM; CLU_009834_0_0_1; -.
DR   InParanoid; Q8SPX7; -.
DR   OMA; RDNCLTH; -.
DR   OrthoDB; 840631at2759; -.
DR   TreeFam; TF313501; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000011726; Expressed in rumen papilla and 104 other tissues.
DR   ExpressionAtlas; Q8SPX7; baseline and differential.
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: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   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..321
FT                   /note="Lambda-crystallin homolog"
FT                   /id="PRO_0000232505"
FT   BINDING         19..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q811X6"
SQ   SEQUENCE   321 AA;  35072 MW;  0BA232C7130F028C CRC64;
     MASPGSSAPG GVAVVGSGLI GRSWAMLFAS AGFRVKLFDI EPRQVTDALV SLRKEMKMLE
     LSGYLKGELG AEEQLSLISG CSDLREAVEG ALHVQECVPE NLELKRKLFA QLDKIADDHV
     ILSSSSSCLL PSKLFAGLAH VKQCLVAHPV NPPYYVPLVE LVPHPETAPA TVDRTYALMR
     RVGQSPVRLL REIDGFALNR LQYAVIAEAW RLVEEGVVSP GDLDLVMSDG LGLRYAFIGP
     LETMHLNAEG MLSYCDRYGE GMKRVLKTFG PVPEFSGATA EKVHQAMCVK VPDDAEHLAA
     RRAWRDGCLM RLAQLKHQLP Q