CDO1_HUMAN
ID CDO1_HUMAN Reviewed; 200 AA.
AC Q16878; B2RAK4; P78513; Q6FHZ8; Q8TB64;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cysteine dioxygenase type 1;
DE EC=1.13.11.20 {ECO:0000269|PubMed:17135237};
DE AltName: Full=Cysteine dioxygenase type I;
DE Short=CDO;
DE Short=CDO-I;
GN Name=CDO1;
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], AND VARIANT ILE-45.
RC TISSUE=Liver;
RX PubMed=7524679; DOI=10.1016/0167-4838(94)90144-9;
RA McCann K.P., Akbari M.T., Williams A.C., Ramsden D.B.;
RT "Human cysteine dioxygenase type I: primary structure derived from base
RT sequencing of cDNA.";
RL Biochim. Biophys. Acta 1209:107-110(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10427686; DOI=10.1271/bbb.63.1017;
RA Tsuboyama-Kasaoka N., Hosokawa Y., Kodama H., Matsumoto A., Oka J.,
RA Totani M.;
RT "Human cysteine dioxygenase gene: structural organization, tissue-specific
RT expression and downregulation by phorbol 12-myristate 13-acetate.";
RL Biosci. Biotechnol. Biochem. 63:1017-1024(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-45.
RX PubMed=9497919; DOI=10.1136/mp.50.5.269;
RA Ramsden D.B., Kapadi A.L., Fitch N.J., Farmer M.J., Bennett P.,
RA Williams A.C.;
RT "Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5' flanking
RT region and intron-exon structure of the gene.";
RL Mol. Pathol. 50:269-271(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-200 OF WILD-TYPE AND MUTANTS
RP ARG-60; CYS-93; TYR-157 AND CYS-164 IN COMPLEX WITH L-CYSTEINE AND DIVALENT
RP METAL IONS, CROSS-LINK, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PTM,
RP MUTAGENESIS OF ARG-60; CYS-93; TYR-157 AND CYS-164, AND IRON-BINDING SITES.
RX PubMed=17135237; DOI=10.1074/jbc.m609337200;
RA Ye S., Wu X., Wei L., Tang D., Sun P., Bartlam M., Rao Z.;
RT "An insight into the mechanism of human cysteine dioxygenase. Key roles of
RT the thioether-bonded tyrosine-cysteine cofactor.";
RL J. Biol. Chem. 282:3391-3402(2007).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-143.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the oxidation of cysteine to cysteine sulfinic acid
CC with addition of molecular dioxygen. {ECO:0000269|PubMed:17135237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+);
CC Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20;
CC Evidence={ECO:0000269|PubMed:17135237};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000305|PubMed:17135237};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:17135237};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:P60334};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17135237};
CC Note=Binds 1 Fe(2+) cation per subunit. Zn(2+) can be used to a much
CC lesser extent (PubMed:17135237). Ni(2+) can be used to a lesser extent
CC (By similarity). {ECO:0000250|UniProtKB:P60334,
CC ECO:0000269|PubMed:17135237};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for L-cysteine {ECO:0000269|PubMed:17135237};
CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC from L-cysteine: step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17135237}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and placenta. Low
CC expression in heart, brain and pancreas. Also detected in
CC hepatoblastoma Hep-G2 cells. {ECO:0000269|PubMed:10427686}.
CC -!- INDUCTION: In hepatoblastoma Hep-G2 cells, down-regulated by phorbol
CC 12-myristate 13-acetate (PMA). {ECO:0000269|PubMed:10427686}.
CC -!- PTM: The thioether cross-link between Cys-93 and Tyr-157 plays a
CC structural role through stabilizing the Fe(2+) ion, and prevents the
CC production of highly damaging free hydroxyl radicals by holding the
CC oxygen radical via hydroxyl hydrogen. {ECO:0000269|PubMed:17135237}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR EMBL; Z31357; CAA83234.1; -; mRNA.
DR EMBL; Z23010; CAA80552.1; -; mRNA.
DR EMBL; D85782; BAA12873.1; -; Genomic_DNA.
DR EMBL; D85777; BAA12872.1; -; mRNA.
DR EMBL; AK314231; BAG36901.1; -; mRNA.
DR EMBL; U80055; AAB58352.1; -; Genomic_DNA.
DR EMBL; U60232; AAB58352.1; JOINED; Genomic_DNA.
DR EMBL; U78979; AAB58352.1; JOINED; Genomic_DNA.
DR EMBL; CR536540; CAG38777.1; -; mRNA.
DR EMBL; CH471086; EAW48957.1; -; Genomic_DNA.
DR EMBL; BC024241; AAH24241.1; -; mRNA.
DR CCDS; CCDS4121.1; -.
DR PIR; S50192; S50192.
DR RefSeq; NP_001310494.1; NM_001323565.1.
DR RefSeq; NP_001310495.1; NM_001323566.1.
DR RefSeq; NP_001310496.1; NM_001323567.1.
DR RefSeq; NP_001792.2; NM_001801.2.
DR PDB; 2IC1; X-ray; 2.70 A; A=1-200.
DR PDB; 6BGF; X-ray; 2.25 A; A=2-200.
DR PDB; 6BGM; X-ray; 2.21 A; A=2-200.
DR PDB; 6BPR; X-ray; 1.96 A; A=2-200.
DR PDB; 6BPS; X-ray; 2.10 A; A=2-200.
DR PDB; 6BPT; X-ray; 2.40 A; A=2-200.
DR PDB; 6BPU; X-ray; 1.80 A; A=2-200.
DR PDB; 6BPV; X-ray; 1.95 A; A=2-200.
DR PDB; 6BPW; X-ray; 2.43 A; A=2-200.
DR PDB; 6BPX; X-ray; 2.15 A; A=2-200.
DR PDB; 6CDH; X-ray; 1.82 A; A=2-200.
DR PDB; 6CDN; X-ray; 2.06 A; A=2-200.
DR PDB; 6E87; X-ray; 1.95 A; A=2-200.
DR PDB; 6N42; X-ray; 2.20 A; A=2-200.
DR PDB; 6N43; X-ray; 2.29 A; A=2-200.
DR PDBsum; 2IC1; -.
DR PDBsum; 6BGF; -.
DR PDBsum; 6BGM; -.
DR PDBsum; 6BPR; -.
DR PDBsum; 6BPS; -.
DR PDBsum; 6BPT; -.
DR PDBsum; 6BPU; -.
DR PDBsum; 6BPV; -.
DR PDBsum; 6BPW; -.
DR PDBsum; 6BPX; -.
DR PDBsum; 6CDH; -.
DR PDBsum; 6CDN; -.
DR PDBsum; 6E87; -.
DR PDBsum; 6N42; -.
DR PDBsum; 6N43; -.
DR AlphaFoldDB; Q16878; -.
DR SMR; Q16878; -.
DR BioGRID; 107468; 12.
DR IntAct; Q16878; 9.
DR STRING; 9606.ENSP00000250535; -.
DR DrugBank; DB04339; Carbocisteine.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB00157; NADH.
DR iPTMnet; Q16878; -.
DR PhosphoSitePlus; Q16878; -.
DR BioMuta; CDO1; -.
DR DMDM; 76800649; -.
DR EPD; Q16878; -.
DR jPOST; Q16878; -.
DR MassIVE; Q16878; -.
DR PaxDb; Q16878; -.
DR PeptideAtlas; Q16878; -.
DR PRIDE; Q16878; -.
DR ProteomicsDB; 61117; -.
DR Antibodypedia; 25433; 179 antibodies from 29 providers.
DR DNASU; 1036; -.
DR Ensembl; ENST00000250535.5; ENSP00000250535.4; ENSG00000129596.5.
DR GeneID; 1036; -.
DR KEGG; hsa:1036; -.
DR MANE-Select; ENST00000250535.5; ENSP00000250535.4; NM_001801.3; NP_001792.2.
DR UCSC; uc003krg.4; human.
DR CTD; 1036; -.
DR DisGeNET; 1036; -.
DR GeneCards; CDO1; -.
DR HGNC; HGNC:1795; CDO1.
DR HPA; ENSG00000129596; Tissue enhanced (liver).
DR MIM; 603943; gene.
DR neXtProt; NX_Q16878; -.
DR OpenTargets; ENSG00000129596; -.
DR PharmGKB; PA26327; -.
DR VEuPathDB; HostDB:ENSG00000129596; -.
DR eggNOG; KOG4064; Eukaryota.
DR GeneTree; ENSGT00390000018226; -.
DR HOGENOM; CLU_079443_1_0_1; -.
DR InParanoid; Q16878; -.
DR OMA; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR PhylomeDB; Q16878; -.
DR TreeFam; TF105636; -.
DR BioCyc; MetaCyc:HS05299-MON; -.
DR BRENDA; 1.13.11.20; 2681.
DR PathwayCommons; Q16878; -.
DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR SignaLink; Q16878; -.
DR SIGNOR; Q16878; -.
DR UniPathway; UPA00012; UER00537.
DR BioGRID-ORCS; 1036; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; CDO1; human.
DR EvolutionaryTrace; Q16878; -.
DR GenomeRNAi; 1036; -.
DR Pharos; Q16878; Tbio.
DR PRO; PR:Q16878; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q16878; protein.
DR Bgee; ENSG00000129596; Expressed in calcaneal tendon and 178 other tissues.
DR Genevisible; Q16878; HS.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006534; P:cysteine metabolic process; TAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0019448; P:L-cysteine catabolic process; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0000097; P:sulfur amino acid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0042412; P:taurine biosynthetic process; TAS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010300; CDO_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR12918; PTHR12918; 1.
DR Pfam; PF05995; CDO_I; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Thioether bond.
FT CHAIN 1..200
FT /note="Cysteine dioxygenase type 1"
FT /id="PRO_0000206606"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17135237"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17135237"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:17135237"
FT CROSSLNK 93..157
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000269|PubMed:17135237"
FT VARIANT 45
FT /note="T -> I (in dbSNP:rs1042867)"
FT /evidence="ECO:0000269|PubMed:7524679,
FT ECO:0000269|PubMed:9497919"
FT /id="VAR_023536"
FT VARIANT 143
FT /note="E -> Q (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036170"
FT MUTAGEN 60
FT /note="R->Q: Reduces enzyme activity by 70%. Reduces iron
FT and zinc incorporation by 50%."
FT /evidence="ECO:0000269|PubMed:17135237"
FT MUTAGEN 93
FT /note="C->S: Reduces enzyme activity and iron incorporation
FT by 50%. Zinc incorporation increased by 20%."
FT /evidence="ECO:0000269|PubMed:17135237"
FT MUTAGEN 157
FT /note="Y->F: Almost total loss of enzyme activity and iron
FT incorporation. Reduces zinc incorporation by 20%."
FT /evidence="ECO:0000269|PubMed:17135237"
FT MUTAGEN 164
FT /note="C->S: Reduces enzyme activity by 20%. Little effect
FT on iron incorporation. No effect on zinc incorporation."
FT /evidence="ECO:0000269|PubMed:17135237"
FT CONFLICT 137
FT /note="I -> V (in Ref. 7; AAH24241)"
FT /evidence="ECO:0000305"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6BPU"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6BPU"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6BPU"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6BPU"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6BPU"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6BPU"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:6BPU"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6BPU"
SQ SEQUENCE 200 AA; 22972 MW; E4EF87221D05C14D CRC64;
MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR
NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG NLKETLFAWP DKKSNEMVKK
SERVLRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT
FHSKFGIRTP NATSGSLENN
