ID   CRYL1_PIG               Reviewed;         322 AA.
AC   Q8SQ26;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 83.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
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; AF351608; AAM13397.1; -; mRNA.
DR   RefSeq; NP_999046.1; NM_213881.1.
DR   AlphaFoldDB; Q8SQ26; -.
DR   SMR; Q8SQ26; -.
DR   STRING; 9823.ENSSSCP00000009883; -.
DR   PaxDb; Q8SQ26; -.
DR   PeptideAtlas; Q8SQ26; -.
DR   GeneID; 396914; -.
DR   KEGG; ssc:396914; -.
DR   CTD; 51084; -.
DR   eggNOG; KOG2305; Eukaryota.
DR   InParanoid; Q8SQ26; -.
DR   OrthoDB; 840631at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..322
FT                   /note="Lambda-crystallin homolog"
FT                   /id="PRO_0000232506"
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   322 AA;  35128 MW;  13574ABCA10945DC CRC64;
     MASSASSTAD GVAVVGSGLI GRSWAMLFAS GGFRVKLYDI EQQQVTGALD TIRKEMKLLE
     QSGALKGSLG AEEQLALISG CSDLREAVEG TVHIQECVPE NLELKQQLFA QLDQIVDGNV
     VLSSSSSCLL PSKLFAGLVH VRQCLVAHPV NPPYHVPLVE LVPHPETAPA TMARTYALMR
     QIGQSPVRIL KEVDGFALNR LQYALIGEAW RLVEARIVSP GDLDLVMSDG LGLRYAFIGP
     LETMHLNAEG MLSYCDRYRE GMKRVLKTFG PIPEFSGAVA EKVHQAMCVK VPDDPEHLSA
     RREWRDGCLM RLAKLKGQVQ PP