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-APR-2013, entry version 96.
DE RecName: Full=Lambda-crystallin homolog;
DE EC=1.1.1.45;
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Zhao S.;
RT "Human CRYL1, a novel enzyme-crystallin overexpressed in liver and
RT kidney and downregulated in 58% of liver cancer tissues from 60
RT Chinese patients, 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- CATALYTIC ACTIVITY: L-gulonate + NAD(+) = 3-dehydro-L-gulonate +
CC NADH.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
CC liver. Undetectable in skeletal muscle.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM13398.1; Type=Frameshift; Positions=227;
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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 IPI; IPI00409345; -.
DR RefSeq; NP_084280.2; NM_030004.3.
DR UniGene; Mm.25539; -.
DR ProteinModelPortal; Q99KP3; -.
DR SMR; Q99KP3; 7-316.
DR PhosphoSite; Q99KP3; -.
DR REPRODUCTION-2DPAGE; Q99KP3; -.
DR PaxDb; Q99KP3; -.
DR PRIDE; Q99KP3; -.
DR Ensembl; ENSMUST00000022517; ENSMUSP00000022517; ENSMUSG00000021947.
DR GeneID; 68631; -.
DR KEGG; mmu:68631; -.
DR CTD; 51084; -.
DR MGI; MGI:1915881; Cryl1.
DR eggNOG; COG1250; -.
DR GeneTree; ENSGT00390000007182; -.
DR HOGENOM; HOG000141499; -.
DR HOVERGEN; HBG051126; -.
DR InParanoid; Q99KP3; -.
DR KO; K13247; -.
DR OMA; RSWAMVF; -.
DR OrthoDB; EOG4DBTF7; -.
DR NextBio; 327590; -.
DR ArrayExpress; Q99KP3; -.
DR Bgee; Q99KP3; -.
DR CleanEx; MM_CRYL1; -.
DR Genevestigator; Q99KP3; -.
DR GermOnline; ENSMUSG00000021947; Mus musculus.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050104; F:L-gulonate 3-dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR Gene3D; 3.40.50.720; -; 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_C-like.
DR InterPro; IPR013328; DH_multihelical.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6DGDH_C_like; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 319 Lambda-crystallin homolog.
FT /FTId=PRO_0000109321.
FT NP_BIND 16 17 NAD (By similarity).
FT BINDING 36 36 NAD (By similarity).
FT BINDING 97 97 NAD (By similarity).
FT BINDING 102 102 NAD (By similarity).
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
//
