CRYM_HUMAN
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 03-AUG-2022, entry version 188.
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 3,4-dehydro-thiomorpholine-3-
CC carboxylate as substrate (at pH 5.0 and 37 degrees Celsius)
CC {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}.
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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; 7.
DR MINT; Q14894; -.
DR STRING; 9606.ENSP00000219599; -.
DR DrugBank; DB05235; NRP409.
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; Q14894; -.
DR PeptideAtlas; Q14894; -.
DR PRIDE; Q14894; -.
DR ProteomicsDB; 60215; -.
DR Antibodypedia; 12355; 329 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 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; 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; 1345495at2759; -.
DR PhylomeDB; Q14894; -.
DR TreeFam; TF105309; -.
DR BioCyc; MetaCyc:ENSG00000103316-MON; -.
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 1072 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 170 other tissues.
DR ExpressionAtlas; Q14894; baseline and differential.
DR Genevisible; Q14894; HS.
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:0042562; F:hormone binding; IBA:GO_Central.
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; 3.30.1780.10; -; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; PTHR13812; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
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
