CRYL1_MOUSE
ID CRYL1_MOUSE Reviewed; 319 AA.
AC Q99KP3; Q542R9; Q8R4W7;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in liver.
CC Undetectable in skeletal muscle. {ECO:0000269|PubMed:12527201}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM13398.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF351609; AAM13398.1; ALT_FRAME; mRNA.
DR EMBL; AK043569; BAC31583.1; -; mRNA.
DR EMBL; AK080625; BAC37964.1; -; mRNA.
DR EMBL; AK135834; BAE22682.1; -; mRNA.
DR EMBL; BC004074; AAH04074.1; -; mRNA.
DR EMBL; BC027064; AAH27064.1; -; mRNA.
DR CCDS; CCDS27155.1; -.
DR RefSeq; NP_084280.2; NM_030004.3.
DR AlphaFoldDB; Q99KP3; -.
DR SMR; Q99KP3; -.
DR STRING; 10090.ENSMUSP00000022517; -.
DR iPTMnet; Q99KP3; -.
DR PhosphoSitePlus; Q99KP3; -.
DR REPRODUCTION-2DPAGE; Q99KP3; -.
DR jPOST; Q99KP3; -.
DR MaxQB; Q99KP3; -.
DR PaxDb; Q99KP3; -.
DR PRIDE; Q99KP3; -.
DR ProteomicsDB; 285316; -.
DR Antibodypedia; 49573; 72 antibodies from 14 providers.
DR DNASU; 68631; -.
DR Ensembl; ENSMUST00000022517; ENSMUSP00000022517; ENSMUSG00000021947.
DR GeneID; 68631; -.
DR KEGG; mmu:68631; -.
DR UCSC; uc007ucz.1; mouse.
DR CTD; 51084; -.
DR MGI; MGI:1915881; Cryl1.
DR VEuPathDB; HostDB:ENSMUSG00000021947; -.
DR eggNOG; KOG2305; Eukaryota.
DR GeneTree; ENSGT00390000007182; -.
DR HOGENOM; CLU_009834_0_0_1; -.
DR InParanoid; Q99KP3; -.
DR OMA; RDNCLTH; -.
DR OrthoDB; 840631at2759; -.
DR PhylomeDB; Q99KP3; -.
DR TreeFam; TF313501; -.
DR Reactome; R-MMU-5661270; Formation of xylulose-5-phosphate.
DR BioGRID-ORCS; 68631; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cryl1; mouse.
DR PRO; PR:Q99KP3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99KP3; protein.
DR Bgee; ENSMUSG00000021947; Expressed in right kidney and 242 other tissues.
DR ExpressionAtlas; Q99KP3; baseline and differential.
DR Genevisible; Q99KP3; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
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:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IDA:MGI.
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_0000109321"
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:0000250|UniProtKB:Q811X6"
SQ SEQUENCE 319 AA; 35209 MW; 590EC278F5C83A9D CRC64;
MASPAAGGVV IVGSGLIGRS WAMLFASGGF KVKLYDIEQQ QITDALENIR KEMKSLEQSG
SLKGSLSAER QLSLISGCGN LAEAVEGAVH IQECVPENLE LKKKIFAQLD RIVDDRVILS
SSSSCLLPSK LFSGLAHVKQ CIVAHPVNPP YYVPLVELVP HPETAPATMD RTYALMKKIG
QSPVRVLKEI DGFVLNRLQY AVISEAWRLV EEEIVSPSDL DLVMSDGLGM RYAFIGPLET
MHLNAEGVIS YCERYSEGMK HVLSTFGPVP EFSGATVERV SEDMCMKVPD DPEHLAARRQ
WRDDCLMKLS ILKYQMQPK
