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   24-JAN-2024, entry version 182.
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}.
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; 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; 14.
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; 9606-ENSP00000250535; -.
DR   PeptideAtlas; Q16878; -.
DR   ProteomicsDB; 61117; -.
DR   Antibodypedia; 25433; 202 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   AGR; HGNC:1795; -.
DR   CTD; 1036; -.
DR   DisGeNET; 1036; -.
DR   GeneCards; CDO1; -.
DR   HGNC; HGNC:1795; CDO1.
DR   HPA; ENSG00000129596; Tissue enhanced (choroid plexus, 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; MLLCWGE; -.
DR   OrthoDB; 314969at2759; -.
DR   PhylomeDB; Q16878; -.
DR   TreeFam; TF105636; -.
DR   BioCyc; MetaCyc:HS05299-MONOMER; -.
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 1153 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 180 other cell types or tissues.
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: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   CDD; cd10548; cupin_CDO; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR010300; CDO_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR12918; CYSTEINE DIOXYGENASE; 1.
DR   PANTHER; PTHR12918:SF1; CYSTEINE DIOXYGENASE TYPE 1; 1.
DR   Pfam; PF05995; CDO_I; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   Genevisible; Q16878; HS.
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
//