ID CRYM_HUMAN Reviewed; 314 AA. AC Q14894; D5MNX0; Q5HYB7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 24-JAN-2024, entry version 196. DE RecName: Full=Ketimine reductase mu-crystallin; DE EC=1.5.1.25; DE AltName: Full=NADP-regulated thyroid-hormone-binding protein; GN Name=CRYM; Synonyms=THBP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RX PubMed=9285773; RA Segovia L., Horwitz J., Gasser R., Wistow G.; RT "Two roles for mu-crystallin: a lens structural protein in diurnal RT marsupials and a possible enzyme in mammalian retinas."; RL Mol. Vis. 3:9-9(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9328354; DOI=10.1210/mend.11.11.9915; RA Vie M.-P., Evrard C., Osty J., Breton-Gilet A., Blanchet P., Pomerance M., RA Rouget P., Francon J., Blondeau J.-P.; RT "Purification, molecular cloning, and functional expression of the human RT nicotinamide-adenine dinucleotide phosphate-regulated thyroid hormone- RT binding protein."; RL Mol. Endocrinol. 11:1728-1736(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Sperbeck S.J., Segovia L., Wistow G.J.; RT "Human and mouse Mu-crystallin."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10493829; DOI=10.1006/geno.1999.5927; RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., RA Adams M.D.; RT "Genome duplications and other features in 12 Mb of DNA sequence from human RT chromosome 16p and 16q."; RL Genomics 60:295-308(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterine endothelium; 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [10] RP PROTEIN SEQUENCE OF 4-18; 57-83; 177-186; 243-277 AND 292-314, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [11] RP NUCLEOTIDE SEQUENCE OF 37-314. RC TISSUE=Retina; RX PubMed=1384048; DOI=10.1073/pnas.89.19.9292; RA Kim R.Y., Gasser R., Wistow G.J.; RT "Mu-crystallin is a mammalian homologue of Agrobacterium ornithine RT cyclodeaminase and is expressed in human retina."; RL Proc. Natl. Acad. Sci. U.S.A. 89:9292-9296(1992). RN [12] RP INVOLVEMENT IN DFNA40, AND VARIANTS DFNA40 THR-314 AND RP TYR-ASN-LYS-GLY-THR-314 EXT. RX PubMed=12471561; DOI=10.1086/345398; RA Abe S., Katagiri T., Saito-Hisaminato A., Usami S., Inoue Y., Tsunoda T., RA Nakamura Y.; RT "Identification of CRYM as a candidate responsible for nonsyndromic RT deafness, through cDNA microarray analysis of human cochlear and vestibular RT tissues."; RL Am. J. Hum. Genet. 72:73-82(2003). RN [13] RP FUNCTION AS A KETIMINE REDUCTASE, CATALYTIC ACTIVITY, KINETIC PARAMETERS, RP AND PH DEPENDENCE. RX PubMed=21332720; DOI=10.1111/j.1471-4159.2011.07220.x; RA Hallen A., Cooper A.J., Jamie J.F., Haynes P.A., Willows R.D.; RT "Mammalian forebrain ketimine reductase identified as mu-crystallin; RT potential regulation by thyroid hormones."; RL J. Neurochem. 118:379-387(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2-313 IN COMPLEX WITH NADPH, RP SUBUNIT, AND NADP-BINDING SITES. RX PubMed=17242435; DOI=10.1110/ps.062556907; RA Cheng Z., Sun L., He J., Gong W.; RT "Crystal structure of human micro-crystallin complexed with NADPH."; RL Protein Sci. 16:329-335(2007). CC -!- FUNCTION: Specifically catalyzes the reduction of imine bonds in brain CC substrates that may include cystathionine ketimine (CysK) and CC lanthionine ketimine (LK). Binds thyroid hormone which is a strong CC reversible inhibitor. Presumably involved in the regulation of the free CC intracellular concentration of triiodothyronine and access to its CC nuclear receptors. {ECO:0000269|PubMed:21332720}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4- CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH; CC Xref=Rhea:RHEA:12504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873; CC EC=1.5.1.25; Evidence={ECO:0000269|PubMed:21332720}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NADP(+) = 3,4- CC dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADPH; CC Xref=Rhea:RHEA:12500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873; CC EC=1.5.1.25; Evidence={ECO:0000269|PubMed:21332720}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=47 uM for 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and CC 37 degrees Celsius) {ECO:0000269|PubMed:21332720}; CC KM=3.6 uM for NADH (at pH 5.0 and 37 degrees Celsius) CC {ECO:0000269|PubMed:21332720}; CC Vmax=9.6 umol/min/mg enzyme with CC 3,4-dehydro-thiomorpholine-3-carboxylate as substrate (at pH 5.0 and CC 37 degrees Celsius) {ECO:0000269|PubMed:21332720}; CC pH dependence: CC Optimum pH is 4.5. {ECO:0000269|PubMed:21332720}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17242435}. CC -!- INTERACTION: CC Q14894; Q96CV9: OPTN; NbExp=3; IntAct=EBI-7107048, EBI-748974; CC Q14894; P54274: TERF1; NbExp=2; IntAct=EBI-7107048, EBI-710997; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in neural tissue, muscle and kidney. CC -!- DISEASE: Deafness, autosomal dominant, 40 (DFNA40) [MIM:616357]: A form CC of non-syndromic sensorineural hearing loss. Sensorineural deafness CC results from damage to the neural receptors of the inner ear, the nerve CC pathways to the brain, or the area of the brain that receives sound CC information. {ECO:0000269|PubMed:12471561}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L02950; AAC16914.1; -; mRNA. DR EMBL; U85772; AAB81564.1; -; mRNA. DR EMBL; AF039397; AAB94938.1; -; Genomic_DNA. DR EMBL; AF039392; AAB94938.1; JOINED; Genomic_DNA. DR EMBL; AF039393; AAB94938.1; JOINED; Genomic_DNA. DR EMBL; AF039394; AAB94938.1; JOINED; Genomic_DNA. DR EMBL; AF039395; AAB94938.1; JOINED; Genomic_DNA. DR EMBL; AF039396; AAB94938.1; JOINED; Genomic_DNA. DR EMBL; AK290852; BAF83541.1; -; mRNA. DR EMBL; BX648477; CAI46030.1; -; mRNA. DR EMBL; AF001550; AAB67600.1; -; Genomic_DNA. DR EMBL; CH471228; EAW66863.1; -; Genomic_DNA. DR EMBL; BC018061; AAH18061.1; -; mRNA. DR CCDS; CCDS10597.1; -. DR PIR; B46290; B46290. DR RefSeq; NP_001879.1; NM_001888.4. DR PDB; 2I99; X-ray; 2.60 A; A/B=2-313. DR PDBsum; 2I99; -. DR AlphaFoldDB; Q14894; -. DR SMR; Q14894; -. DR BioGRID; 107815; 9. DR IntAct; Q14894; 8. DR MINT; Q14894; -. DR STRING; 9606.ENSP00000219599; -. DR DrugBank; DB05235; NRP409. DR GlyCosmos; Q14894; 1 site, 1 glycan. DR GlyGen; Q14894; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q14894; -. DR PhosphoSitePlus; Q14894; -. DR BioMuta; CRYM; -. DR DMDM; 2498259; -. DR EPD; Q14894; -. DR jPOST; Q14894; -. DR MassIVE; Q14894; -. DR PaxDb; 9606-ENSP00000219599; -. DR PeptideAtlas; Q14894; -. DR ProteomicsDB; 60215; -. DR Pumba; Q14894; -. DR Antibodypedia; 12355; 365 antibodies from 28 providers. DR DNASU; 1428; -. DR Ensembl; ENST00000219599.8; ENSP00000219599.3; ENSG00000103316.12. DR Ensembl; ENST00000543948.5; ENSP00000440227.1; ENSG00000103316.12. DR Ensembl; ENST00000572914.2; ENSP00000461904.2; ENSG00000103316.12. DR GeneID; 1428; -. DR KEGG; hsa:1428; -. DR MANE-Select; ENST00000572914.2; ENSP00000461904.2; NM_001376256.1; NP_001363185.1. DR UCSC; uc002dim.4; human. DR AGR; HGNC:2418; -. DR CTD; 1428; -. DR DisGeNET; 1428; -. DR GeneCards; CRYM; -. DR HGNC; HGNC:2418; CRYM. DR HPA; ENSG00000103316; Tissue enhanced (brain, heart muscle). DR MalaCards; CRYM; -. DR MIM; 123740; gene. DR MIM; 616357; phenotype. DR neXtProt; NX_Q14894; -. DR OpenTargets; ENSG00000103316; -. DR Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA. DR PharmGKB; PA26924; -. DR VEuPathDB; HostDB:ENSG00000103316; -. DR eggNOG; KOG3007; Eukaryota. DR GeneTree; ENSGT00390000000237; -. DR InParanoid; Q14894; -. DR OMA; AVKAFTY; -. DR OrthoDB; 2501268at2759; -. DR PhylomeDB; Q14894; -. DR TreeFam; TF105309; -. DR BioCyc; MetaCyc:ENSG00000103316-MONOMER; -. DR BRENDA; 1.5.1.21; 2681. DR BRENDA; 1.5.1.25; 2681. DR PathwayCommons; Q14894; -. DR Reactome; R-HSA-71064; Lysine catabolism. DR SignaLink; Q14894; -. DR BioGRID-ORCS; 1428; 13 hits in 1150 CRISPR screens. DR ChiTaRS; CRYM; human. DR EvolutionaryTrace; Q14894; -. DR GeneWiki; CRYM; -. DR GenomeRNAi; 1428; -. DR Pharos; Q14894; Tbio. DR PRO; PR:Q14894; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q14894; Protein. DR Bgee; ENSG00000103316; Expressed in cortical plate and 172 other cell types or tissues. DR ExpressionAtlas; Q14894; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome. DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0047127; F:thiomorpholine-carboxylate dehydrogenase activity; IDA:FlyBase. DR GO; GO:0070324; F:thyroid hormone binding; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB. DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB. DR GO; GO:0042403; P:thyroid hormone metabolic process; IBA:GO_Central. DR GO; GO:0070327; P:thyroid hormone transport; IMP:UniProtKB. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR003462; ODC_Mu_crystall. DR InterPro; IPR023401; ODC_N. DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1. DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1. DR Pfam; PF02423; OCD_Mu_crystall; 1. DR PIRSF; PIRSF001439; CryM; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q14894; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Deafness; Direct protein sequencing; KW Disease variant; NAD; NADP; Non-syndromic deafness; Oxidoreductase; KW Reference proteome. FT CHAIN 1..314 FT /note="Ketimine reductase mu-crystallin" FT /id="PRO_0000200678" FT BINDING 143..148 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17242435" FT BINDING 168 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17242435" FT BINDING 169 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000269|PubMed:17242435" FT VARIANT 314 FT /note="K -> KYNKGT (in DFNA40)" FT /evidence="ECO:0000269|PubMed:12471561" FT /id="VAR_073780" FT VARIANT 314 FT /note="K -> T (in DFNA40; dbSNP:rs104894512)" FT /evidence="ECO:0000269|PubMed:12471561" FT /id="VAR_073781" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 10..16 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 24..35 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 48..52 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 57..66 FT /evidence="ECO:0007829|PDB:2I99" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 71..80 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 89..99 FT /evidence="ECO:0007829|PDB:2I99" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 113..131 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 146..158 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 162..167 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 171..180 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 191..195 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 238..243 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 244..249 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 251..257 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:2I99" FT TURN 263..265 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:2I99" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:2I99" FT HELIX 296..310 FT /evidence="ECO:0007829|PDB:2I99" SQ SEQUENCE 314 AA; 33776 MW; A49D316B41CE6648 CRC64; MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK //