Full text data of CRYZ
CRYZ
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Quinone oxidoreductase; 1.6.5.5 (NADPH:quinone reductase; Zeta-crystallin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Quinone oxidoreductase; 1.6.5.5 (NADPH:quinone reductase; Zeta-crystallin)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q08257
ID QOR_HUMAN Reviewed; 329 AA.
AC Q08257; A6NN60; D3DQ76; Q53FT0; Q59EU7; Q5HYE7; Q6NSK9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1994, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Quinone oxidoreductase;
DE EC=1.6.5.5;
DE AltName: Full=NADPH:quinone reductase;
DE AltName: Full=Zeta-crystallin;
GN Name=CRYZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8466529; DOI=10.1006/bbrc.1993.1302;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Molecular cloning and sequencing of zeta-crystallin/quinone reductase
RT cDNA from human liver.";
RL Biochem. Biophys. Res. Commun. 191:902-907(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8088825; DOI=10.1006/geno.1994.1272;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Organization of the human zeta-crystallin/quinone reductase gene
RT (CRYZ).";
RL Genomics 21:317-324(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-176.
RC TISSUE=Brain, Kidney proximal tubule, and Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-66.
RC TISSUE=Testis;
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).
RN [9]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=17497241; DOI=10.1007/s00018-007-7091-1;
RA Fernandez M.R., Porte S., Crosas E., Barbera N., Farres J.,
RA Biosca J.A., Pares X.;
RT "Human and yeast zeta-crystallins bind AU-rich elements in RNA.";
RL Cell. Mol. Life Sci. 64:1419-1427(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=20103721; DOI=10.1096/fj.09-140459;
RA Lapucci A., Lulli M., Amedei A., Papucci L., Witort E.,
RA Di Gesualdo F., Bertolini F., Brewer G., Nicolin A., Bevilacqua A.,
RA Schiavone N., Morello D., Donnini M., Capaccioli S.;
RT "{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2
RT overexpression in T-cell acute lymphocytic leukemia.";
RL FASEB J. 24:1852-1865(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human zeta-crystallin at 1.85 A.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP
CC and acts through a one-electron transfer process. Orthoquinones,
CC such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the
CC best substrates (in vitro). May act in the detoxification of
CC xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR
CC of target mRNA species. Enhances the stability of mRNA coding for
CC BCL2. NADPH binding interferes with mRNA binding.
CC -!- CATALYTIC ACTIVITY: NADPH + 2 quinone = NADP(+) + 2 semiquinone.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08257-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08257-2; Sequence=VSP_042927, VSP_042928;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q08257-3; Sequence=VSP_046425;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Only very low amounts in the lens.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
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DR EMBL; L13278; AAA36536.1; -; mRNA.
DR EMBL; L31526; AAK40311.1; -; Genomic_DNA.
DR EMBL; L31521; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31522; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31523; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31524; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31525; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; AB209714; BAD92951.1; -; mRNA.
DR EMBL; AK223150; BAD96870.1; -; mRNA.
DR EMBL; AK223201; BAD96921.1; -; mRNA.
DR EMBL; BX647883; CAI46072.1; -; mRNA.
DR EMBL; AK314813; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC091611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06409.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06410.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06411.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06412.1; -; Genomic_DNA.
DR EMBL; BC039578; AAH39578.1; -; mRNA.
DR EMBL; BC070058; AAH70058.1; -; mRNA.
DR PIR; PN0448; PN0448.
DR RefSeq; NP_001123514.1; NM_001130042.1.
DR RefSeq; NP_001123515.1; NM_001130043.1.
DR RefSeq; NP_001128231.1; NM_001134759.1.
DR RefSeq; NP_001880.2; NM_001889.3.
DR RefSeq; XP_005270548.1; XM_005270491.1.
DR UniGene; Hs.83114; -.
DR PDB; 1YB5; X-ray; 1.85 A; A/B=1-329.
DR PDBsum; 1YB5; -.
DR ProteinModelPortal; Q08257; -.
DR SMR; Q08257; 6-329.
DR IntAct; Q08257; 1.
DR MINT; MINT-5002754; -.
DR STRING; 9606.ENSP00000339399; -.
DR ChEMBL; CHEMBL6118; -.
DR DrugBank; DB00266; Dicumarol.
DR PhosphoSite; Q08257; -.
DR DMDM; 585013; -.
DR REPRODUCTION-2DPAGE; IPI00000792; -.
DR PaxDb; Q08257; -.
DR PRIDE; Q08257; -.
DR Ensembl; ENST00000340866; ENSP00000339399; ENSG00000116791.
DR Ensembl; ENST00000370871; ENSP00000359908; ENSG00000116791.
DR Ensembl; ENST00000370872; ENSP00000359909; ENSG00000116791.
DR Ensembl; ENST00000417775; ENSP00000399805; ENSG00000116791.
DR GeneID; 1429; -.
DR KEGG; hsa:1429; -.
DR UCSC; uc001dgl.3; human.
DR CTD; 1429; -.
DR GeneCards; GC01M075171; -.
DR HGNC; HGNC:2419; CRYZ.
DR HPA; HPA021921; -.
DR HPA; HPA023290; -.
DR MIM; 123691; gene.
DR neXtProt; NX_Q08257; -.
DR PharmGKB; PA26925; -.
DR eggNOG; COG0604; -.
DR HOGENOM; HOG000294672; -.
DR HOVERGEN; HBG002466; -.
DR InParanoid; Q08257; -.
DR KO; K00344; -.
DR OMA; IPYFTAC; -.
DR OrthoDB; EOG7BGHM8; -.
DR PhylomeDB; Q08257; -.
DR EvolutionaryTrace; Q08257; -.
DR GeneWiki; CRYZ; -.
DR GenomeRNAi; 1429; -.
DR NextBio; 5829; -.
DR PRO; PR:Q08257; -.
DR ArrayExpress; Q08257; -.
DR Bgee; Q08257; -.
DR CleanEx; HS_CRYZ; -.
DR Genevestigator; Q08257; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.180.10; -; 1.
DR InterPro; IPR013149; ADH_C.
DR InterPro; IPR013154; ADH_GroES-like.
DR InterPro; IPR002085; ADH_SF_Zn-type.
DR InterPro; IPR011032; GroES-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR11695; PTHR11695; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 329 Quinone oxidoreductase.
FT /FTId=PRO_0000160906.
FT NP_BIND 158 161 NADP.
FT NP_BIND 246 249 NADP.
FT NP_BIND 269 271 NADP.
FT BINDING 53 53 NADP.
FT BINDING 181 181 NADP; via amide nitrogen.
FT BINDING 200 200 NADP.
FT BINDING 229 229 NADP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 23 23 N6-acetyllysine.
FT MOD_RES 248 248 Phosphoserine.
FT VAR_SEQ 1 5 MATGQ -> MHLLS (in isoform 2).
FT /FTId=VSP_042927.
FT VAR_SEQ 6 142 Missing (in isoform 2).
FT /FTId=VSP_042928.
FT VAR_SEQ 211 244 Missing (in isoform 3).
FT /FTId=VSP_046425.
FT VARIANT 66 66 P -> S (in dbSNP:rs11551729).
FT /FTId=VAR_022913.
FT VARIANT 176 176 I -> V (in dbSNP:rs3819946).
FT /FTId=VAR_022914.
FT VARIANT 183 183 E -> K (in dbSNP:rs17095822).
FT /FTId=VAR_048200.
FT CONFLICT 105 105 E -> G (in Ref. 3; AK314813).
FT STRAND 7 15
FT HELIX 19 21
FT STRAND 22 29
FT STRAND 37 46
FT HELIX 49 55
FT STRAND 65 67
FT STRAND 73 80
FT STRAND 92 96
FT STRAND 102 110
FT HELIX 111 113
FT STRAND 114 116
FT HELIX 123 126
FT TURN 127 129
FT HELIX 130 141
FT STRAND 151 156
FT HELIX 160 171
FT STRAND 175 182
FT HELIX 183 191
FT STRAND 195 199
FT HELIX 205 213
FT STRAND 218 224
FT HELIX 226 236
FT STRAND 237 245
FT STRAND 252 254
FT HELIX 257 260
FT TURN 261 263
FT STRAND 265 268
FT HELIX 271 273
FT HELIX 276 292
FT STRAND 299 304
FT HELIX 305 307
FT HELIX 308 317
FT STRAND 322 328
SQ SEQUENCE 329 AA; 35207 MW; 68C1828911486D4E CRC64;
MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS
RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK
LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG
GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG
SQYPLEKVAE AHENIIHGSG ATGKMILLL
//
ID QOR_HUMAN Reviewed; 329 AA.
AC Q08257; A6NN60; D3DQ76; Q53FT0; Q59EU7; Q5HYE7; Q6NSK9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1994, sequence version 1.
DT 22-JAN-2014, entry version 130.
DE RecName: Full=Quinone oxidoreductase;
DE EC=1.6.5.5;
DE AltName: Full=NADPH:quinone reductase;
DE AltName: Full=Zeta-crystallin;
GN Name=CRYZ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8466529; DOI=10.1006/bbrc.1993.1302;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Molecular cloning and sequencing of zeta-crystallin/quinone reductase
RT cDNA from human liver.";
RL Biochem. Biophys. Res. Commun. 191:902-907(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8088825; DOI=10.1006/geno.1994.1272;
RA Gonzalez P., Rao P.V., Zigler J.S. Jr.;
RT "Organization of the human zeta-crystallin/quinone reductase gene
RT (CRYZ).";
RL Genomics 21:317-324(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-176.
RC TISSUE=Brain, Kidney proximal tubule, and Lung;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP SER-66.
RC TISSUE=Testis;
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).
RN [9]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=17497241; DOI=10.1007/s00018-007-7091-1;
RA Fernandez M.R., Porte S., Crosas E., Barbera N., Farres J.,
RA Biosca J.A., Pares X.;
RT "Human and yeast zeta-crystallins bind AU-rich elements in RNA.";
RL Cell. Mol. Life Sci. 64:1419-1427(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX PubMed=20103721; DOI=10.1096/fj.09-140459;
RA Lapucci A., Lulli M., Amedei A., Papucci L., Witort E.,
RA Di Gesualdo F., Bertolini F., Brewer G., Nicolin A., Bevilacqua A.,
RA Schiavone N., Morello D., Donnini M., Capaccioli S.;
RT "{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2
RT overexpression in T-cell acute lymphocytic leukemia.";
RL FASEB J. 24:1852-1865(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human zeta-crystallin at 1.85 A.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Does not have alcohol dehydrogenase activity. Binds NADP
CC and acts through a one-electron transfer process. Orthoquinones,
CC such as 1,2-naphthoquinone or 9,10-phenanthrenequinone, are the
CC best substrates (in vitro). May act in the detoxification of
CC xenobiotics. Interacts with (AU)-rich elements (ARE) in the 3'-UTR
CC of target mRNA species. Enhances the stability of mRNA coding for
CC BCL2. NADPH binding interferes with mRNA binding.
CC -!- CATALYTIC ACTIVITY: NADPH + 2 quinone = NADP(+) + 2 semiquinone.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08257-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08257-2; Sequence=VSP_042927, VSP_042928;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q08257-3; Sequence=VSP_046425;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Only very low amounts in the lens.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily.
CC -----------------------------------------------------------------------
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DR EMBL; L13278; AAA36536.1; -; mRNA.
DR EMBL; L31526; AAK40311.1; -; Genomic_DNA.
DR EMBL; L31521; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31522; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31523; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31524; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; L31525; AAK40311.1; JOINED; Genomic_DNA.
DR EMBL; AB209714; BAD92951.1; -; mRNA.
DR EMBL; AK223150; BAD96870.1; -; mRNA.
DR EMBL; AK223201; BAD96921.1; -; mRNA.
DR EMBL; BX647883; CAI46072.1; -; mRNA.
DR EMBL; AK314813; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC091611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06409.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06410.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06411.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06412.1; -; Genomic_DNA.
DR EMBL; BC039578; AAH39578.1; -; mRNA.
DR EMBL; BC070058; AAH70058.1; -; mRNA.
DR PIR; PN0448; PN0448.
DR RefSeq; NP_001123514.1; NM_001130042.1.
DR RefSeq; NP_001123515.1; NM_001130043.1.
DR RefSeq; NP_001128231.1; NM_001134759.1.
DR RefSeq; NP_001880.2; NM_001889.3.
DR RefSeq; XP_005270548.1; XM_005270491.1.
DR UniGene; Hs.83114; -.
DR PDB; 1YB5; X-ray; 1.85 A; A/B=1-329.
DR PDBsum; 1YB5; -.
DR ProteinModelPortal; Q08257; -.
DR SMR; Q08257; 6-329.
DR IntAct; Q08257; 1.
DR MINT; MINT-5002754; -.
DR STRING; 9606.ENSP00000339399; -.
DR ChEMBL; CHEMBL6118; -.
DR DrugBank; DB00266; Dicumarol.
DR PhosphoSite; Q08257; -.
DR DMDM; 585013; -.
DR REPRODUCTION-2DPAGE; IPI00000792; -.
DR PaxDb; Q08257; -.
DR PRIDE; Q08257; -.
DR Ensembl; ENST00000340866; ENSP00000339399; ENSG00000116791.
DR Ensembl; ENST00000370871; ENSP00000359908; ENSG00000116791.
DR Ensembl; ENST00000370872; ENSP00000359909; ENSG00000116791.
DR Ensembl; ENST00000417775; ENSP00000399805; ENSG00000116791.
DR GeneID; 1429; -.
DR KEGG; hsa:1429; -.
DR UCSC; uc001dgl.3; human.
DR CTD; 1429; -.
DR GeneCards; GC01M075171; -.
DR HGNC; HGNC:2419; CRYZ.
DR HPA; HPA021921; -.
DR HPA; HPA023290; -.
DR MIM; 123691; gene.
DR neXtProt; NX_Q08257; -.
DR PharmGKB; PA26925; -.
DR eggNOG; COG0604; -.
DR HOGENOM; HOG000294672; -.
DR HOVERGEN; HBG002466; -.
DR InParanoid; Q08257; -.
DR KO; K00344; -.
DR OMA; IPYFTAC; -.
DR OrthoDB; EOG7BGHM8; -.
DR PhylomeDB; Q08257; -.
DR EvolutionaryTrace; Q08257; -.
DR GeneWiki; CRYZ; -.
DR GenomeRNAi; 1429; -.
DR NextBio; 5829; -.
DR PRO; PR:Q08257; -.
DR ArrayExpress; Q08257; -.
DR Bgee; Q08257; -.
DR CleanEx; HS_CRYZ; -.
DR Genevestigator; Q08257; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.180.10; -; 1.
DR InterPro; IPR013149; ADH_C.
DR InterPro; IPR013154; ADH_GroES-like.
DR InterPro; IPR002085; ADH_SF_Zn-type.
DR InterPro; IPR011032; GroES-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR11695; PTHR11695; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 329 Quinone oxidoreductase.
FT /FTId=PRO_0000160906.
FT NP_BIND 158 161 NADP.
FT NP_BIND 246 249 NADP.
FT NP_BIND 269 271 NADP.
FT BINDING 53 53 NADP.
FT BINDING 181 181 NADP; via amide nitrogen.
FT BINDING 200 200 NADP.
FT BINDING 229 229 NADP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 23 23 N6-acetyllysine.
FT MOD_RES 248 248 Phosphoserine.
FT VAR_SEQ 1 5 MATGQ -> MHLLS (in isoform 2).
FT /FTId=VSP_042927.
FT VAR_SEQ 6 142 Missing (in isoform 2).
FT /FTId=VSP_042928.
FT VAR_SEQ 211 244 Missing (in isoform 3).
FT /FTId=VSP_046425.
FT VARIANT 66 66 P -> S (in dbSNP:rs11551729).
FT /FTId=VAR_022913.
FT VARIANT 176 176 I -> V (in dbSNP:rs3819946).
FT /FTId=VAR_022914.
FT VARIANT 183 183 E -> K (in dbSNP:rs17095822).
FT /FTId=VAR_048200.
FT CONFLICT 105 105 E -> G (in Ref. 3; AK314813).
FT STRAND 7 15
FT HELIX 19 21
FT STRAND 22 29
FT STRAND 37 46
FT HELIX 49 55
FT STRAND 65 67
FT STRAND 73 80
FT STRAND 92 96
FT STRAND 102 110
FT HELIX 111 113
FT STRAND 114 116
FT HELIX 123 126
FT TURN 127 129
FT HELIX 130 141
FT STRAND 151 156
FT HELIX 160 171
FT STRAND 175 182
FT HELIX 183 191
FT STRAND 195 199
FT HELIX 205 213
FT STRAND 218 224
FT HELIX 226 236
FT STRAND 237 245
FT STRAND 252 254
FT HELIX 257 260
FT TURN 261 263
FT STRAND 265 268
FT HELIX 271 273
FT HELIX 276 292
FT STRAND 299 304
FT HELIX 305 307
FT HELIX 308 317
FT STRAND 322 328
SQ SEQUENCE 329 AA; 35207 MW; 68C1828911486D4E CRC64;
MATGQKLMRA VRVFEFGGPE VLKLRSDIAV PIPKDHQVLI KVHACGVNPV ETYIRSGTYS
RKPLLPYTPG SDVAGVIEAV GDNASAFKKG DRVFTSSTIS GGYAEYALAA DHTVYKLPEK
LDFKQGAAIG IPYFTAYRAL IHSACVKAGE SVLVHGASGG VGLAACQIAR AYGLKILGTA
GTEEGQKIVL QNGAHEVFNH REVNYIDKIK KYVGEKGIDI IIEMLANVNL SKDLSLLSHG
GRVIVVGSRG TIEINPRDTM AKESSIIGVT LFSSTKEEFQ QYAAALQAGM EIGWLKPVIG
SQYPLEKVAE AHENIIHGSG ATGKMILLL
//
MIM
123691
*RECORD*
*FIELD* NO
123691
*FIELD* TI
*123691 CRYSTALLIN, ZETA; CRYZ
;;QUINONE OXIDOREDUCTASE
*FIELD* TX
CLONING
Gonzalez et al. (1994) isolated and characterized the human
read morezeta-crystallin gene and its processed pseudogene. The 5-prime flanking
region of the gene is rich in G and C (58%) and lacks TATA and CAAT
boxes. Previous analysis of the guinea pig gene revealed the presence of
2 different promoters, one responsible for the high lens-specific
expression and the other for expression at the enzymatic level in
numerous tissues. A comparative analysis with the guinea pig gene showed
that a region of approximately 2.5 kb that includes the promoter
responsible for the high expression in the lens in the guinea pig is not
present in the human gene.
GENE STRUCTURE
Gonzalez et al. (1994) determined that the human CRYZ gene is composed
of 9 exons and spans about 20 kb.
MAPPING
By Southern analysis of human/mouse somatic cell hybrids, Heinzmann et
al. (1994) assigned the CRYZ gene to human chromosome 1 and regionalized
the assignment to 1p31-p22 by fluorescence in situ hybridization. They
also identified 5 RFLPs.
GENE FAMILY
In addition to the alpha (see 123580), beta (see 123630), and gamma (see
123660) crystallin families, which are present in the ocular lenses of
all vertebrates, a number of other crystallins have been found to be
present in high amounts in lenses from phylogenetically restricted
groups. Most of these 'taxon-specific' crystallins are pyridine
nucleotide-dependent oxidoreductases that are also present at enzymatic
levels in nonlenticular tissues. The acquisition of this new function as
a lens crystallin generally occurs without gene duplication and
apparently without affecting the catalytic role of the enzyme.
Zeta-crystallin/quinone reductase was initially described as a major
protein in the lens of the guinea pig (Huang et al., 1987), in which a
mutation in the gene is associated with hereditary cataracts (Rodriguez
et al., 1992). It was later found to be also present in high amounts in
the lens of camels (Garland et al., 1991) and at enzymatic levels in a
number of nonlenticular tissues of various species. In the lens of
guinea pigs and camels, it comprises about 10% of the total soluble
protein (summary by Gonzalez et al., 1994).
*FIELD* RF
1. Garland, D.; Rao, P. V.; Del Corso, A.; Mura, U.; Zigler, J. S.,
Jr.: Zeta-crystallin is a major protein in the lens of Camelus dromedarius. Arch.
Biochem. Biophys. 285: 134-136, 1991.
2. Gonzalez, P.; Rao, P. V.; Zigler, J. S., Jr.: Organization of
the human zeta-crystallin/quinone reductase gene (CRYZ). Genomics 21:
317-324, 1994.
3. Heinzmann, C.; Kojis, T. L.; Gonzalez, P.; Rao, P. V.; Zigler,
J. S., Jr.; Polymeropoulos, M. H.; Klisak, I.; Sparkes, R. S.; Mohandas,
T.; Bateman, J. B.: Assignment of the zeta-crystallin gene (CRYZ)
to human chromosome 1p22-p31 and identification of restriction fragment
length polymorphisms. Genomics 23: 403-407, 1994.
4. Huang, Q.-L.; Russell, P.; Stone, S. H.; Zigler, J. S., Jr.: Zeta-crystallin,
a novel lens protein from the guinea pig. Curr. Eye Res. 6: 725-732,
1987.
5. Rodriguez, I. R.; Gonzalez, P.; Zigler, J. S., Jr.; Borras, T.
: A guinea-pig hereditary cataract contains a splice site deletion
in a crystallin gene. Biochim. Biophys. Acta 1180: 44-52, 1992.
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
alopez: 09/13/2012
carol: 11/30/1994
jason: 6/17/1994
*RECORD*
*FIELD* NO
123691
*FIELD* TI
*123691 CRYSTALLIN, ZETA; CRYZ
;;QUINONE OXIDOREDUCTASE
*FIELD* TX
CLONING
Gonzalez et al. (1994) isolated and characterized the human
read morezeta-crystallin gene and its processed pseudogene. The 5-prime flanking
region of the gene is rich in G and C (58%) and lacks TATA and CAAT
boxes. Previous analysis of the guinea pig gene revealed the presence of
2 different promoters, one responsible for the high lens-specific
expression and the other for expression at the enzymatic level in
numerous tissues. A comparative analysis with the guinea pig gene showed
that a region of approximately 2.5 kb that includes the promoter
responsible for the high expression in the lens in the guinea pig is not
present in the human gene.
GENE STRUCTURE
Gonzalez et al. (1994) determined that the human CRYZ gene is composed
of 9 exons and spans about 20 kb.
MAPPING
By Southern analysis of human/mouse somatic cell hybrids, Heinzmann et
al. (1994) assigned the CRYZ gene to human chromosome 1 and regionalized
the assignment to 1p31-p22 by fluorescence in situ hybridization. They
also identified 5 RFLPs.
GENE FAMILY
In addition to the alpha (see 123580), beta (see 123630), and gamma (see
123660) crystallin families, which are present in the ocular lenses of
all vertebrates, a number of other crystallins have been found to be
present in high amounts in lenses from phylogenetically restricted
groups. Most of these 'taxon-specific' crystallins are pyridine
nucleotide-dependent oxidoreductases that are also present at enzymatic
levels in nonlenticular tissues. The acquisition of this new function as
a lens crystallin generally occurs without gene duplication and
apparently without affecting the catalytic role of the enzyme.
Zeta-crystallin/quinone reductase was initially described as a major
protein in the lens of the guinea pig (Huang et al., 1987), in which a
mutation in the gene is associated with hereditary cataracts (Rodriguez
et al., 1992). It was later found to be also present in high amounts in
the lens of camels (Garland et al., 1991) and at enzymatic levels in a
number of nonlenticular tissues of various species. In the lens of
guinea pigs and camels, it comprises about 10% of the total soluble
protein (summary by Gonzalez et al., 1994).
*FIELD* RF
1. Garland, D.; Rao, P. V.; Del Corso, A.; Mura, U.; Zigler, J. S.,
Jr.: Zeta-crystallin is a major protein in the lens of Camelus dromedarius. Arch.
Biochem. Biophys. 285: 134-136, 1991.
2. Gonzalez, P.; Rao, P. V.; Zigler, J. S., Jr.: Organization of
the human zeta-crystallin/quinone reductase gene (CRYZ). Genomics 21:
317-324, 1994.
3. Heinzmann, C.; Kojis, T. L.; Gonzalez, P.; Rao, P. V.; Zigler,
J. S., Jr.; Polymeropoulos, M. H.; Klisak, I.; Sparkes, R. S.; Mohandas,
T.; Bateman, J. B.: Assignment of the zeta-crystallin gene (CRYZ)
to human chromosome 1p22-p31 and identification of restriction fragment
length polymorphisms. Genomics 23: 403-407, 1994.
4. Huang, Q.-L.; Russell, P.; Stone, S. H.; Zigler, J. S., Jr.: Zeta-crystallin,
a novel lens protein from the guinea pig. Curr. Eye Res. 6: 725-732,
1987.
5. Rodriguez, I. R.; Gonzalez, P.; Zigler, J. S., Jr.; Borras, T.
: A guinea-pig hereditary cataract contains a splice site deletion
in a crystallin gene. Biochim. Biophys. Acta 1180: 44-52, 1992.
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
alopez: 09/13/2012
carol: 11/30/1994
jason: 6/17/1994