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Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)]

 XDH_RAT                 Reviewed;        1331 AA.
P22985; Q63157;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 158.
RecName: Full=Xanthine dehydrogenase/oxidase;
Includes:
RecName: Full=Xanthine dehydrogenase;
Short=XD;
EC=1.17.1.4 {ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076};
Includes:
RecName: Full=Xanthine oxidase;
Short=XO;
EC=1.17.3.2 {ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076};
AltName: Full=Xanthine oxidoreductase;
Short=XOR;
Name=Xdh;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ENZYME
REGULATION, PROTEOLYTIC CONVERSION, AND SUBUNIT.
TISSUE=Liver;
PubMed=2387845;
Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., Nishino T.;
"Proteolytic conversion of xanthine dehydrogenase from the NAD-
dependent type to the O2-dependent type. Amino acid sequence of rat
liver xanthine dehydrogenase and identification of the cleavage sites
of the enzyme protein during irreversible conversion by trypsin.";
J. Biol. Chem. 265:14170-14175(1990).
[2]
NUCLEOTIDE SEQUENCE OF 1-55.
STRAIN=Sprague-Dawley;
PubMed=8208609; DOI=10.1093/nar/22.10.1846;
Chow C.W., Clark M., Rinaldo J., Chalkley R.;
"Identification of the rat xanthine dehydrogenase/oxidase promoter.";
Nucleic Acids Res. 22:1846-1854(1994).
[3]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11993848; DOI=10.1078/0065-1281-00629;
Frederiks W.M., Vreeling-Sindelarova H.;
"Ultrastructural localization of xanthine oxidoreductase activity in
isolated rat liver cells.";
Acta Histochem. 104:29-37(2002).
[4]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT
ALA-535/ARG-992/SER-1324 IN COMPLEX WITH FAD; URIC ACID AND
IRON-SULFUR CENTERS, CATALYTIC ACTIVITY, DISULFIDE BOND, ENZYME
REGULATION, MUTAGENESIS OF CYS-535; CYS-992 AND CYS-1316, AND
COFACTOR.
PubMed=15878860; DOI=10.1074/jbc.M501830200;
Nishino T., Okamoto K., Kawaguchi Y., Hori H., Matsumura T.,
Eger B.T., Pai E.F., Nishino T.;
"Mechanism of the conversion of xanthine dehydrogenase to xanthine
oxidase: identification of the two cysteine disulfide bonds and
crystal structure of a non-convertible rat liver xanthine
dehydrogenase mutant.";
J. Biol. Chem. 280:24888-24894(2005).
[5]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF MUTANT ALA-335/LEU-336 IN
COMPLEX WITH FAD AND IRON-SULFUR CENTER, MUTAGENESIS OF
335-TRP-PHE-336, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
PubMed=17301076; DOI=10.1093/jb/mvm054;
Asai R., Nishino T., Matsumura T., Okamoto K., Igarashi K., Pai E.F.,
Nishino T.;
"Two mutations convert mammalian xanthine oxidoreductase to highly
superoxide-productive xanthine oxidase.";
J. Biochem. 141:525-534(2007).
-!- FUNCTION: Key enzyme in purine degradation. Catalyzes the
oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of
xanthine to uric acid. Contributes to the generation of reactive
oxygen species. {ECO:0000269|PubMed:17301076}.
-!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
{ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076}.
-!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
NADH. {ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076}.
-!- CATALYTIC ACTIVITY: Xanthine + H(2)O + O(2) = urate + H(2)O(2).
{ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Note=Binds 2 [2Fe-2S] clusters.;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000250};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000250};
-!- ENZYME REGULATION: Can be converted from the dehydrogenase form
(D) to the oxidase form (O) irreversibly by proteolysis or
reversibly through the oxidation of sulfhydryl groups.
{ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:2387845}.
-!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11993848}.
Cytoplasm {ECO:0000269|PubMed:11993848}. Secreted {ECO:0000250}.
-!- INDUCTION: By interferon.
-!- PTM: Subject to partial proteolysis; this alters the enzyme from
the dehydrogenase form (D) to the oxidase form (O).
-!- PTM: Contains sulfhydryl groups that are easily oxidized (in
vitro); this alters the enzyme from the dehydrogenase form (D) to
the oxidase form (O).
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
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EMBL; J05579; AAA42349.1; -; mRNA.
EMBL; AH000836; AAA18869.1; -; Unassigned_DNA.
RefSeq; NP_058850.1; NM_017154.1.
UniGene; Rn.202951; -.
PDB; 1WYG; X-ray; 2.60 A; A=1-1331.
PDB; 2E3T; X-ray; 2.28 A; A/B=1-1331.
PDB; 3AN1; X-ray; 1.73 A; A/B=1-1331.
PDB; 4YRW; X-ray; 1.99 A; A/B=1-1315.
PDB; 4YSW; X-ray; 1.99 A; A/B=1-1315.
PDB; 4YTY; X-ray; 2.20 A; A/B=1-1331.
PDB; 4YTZ; X-ray; 2.30 A; A/B=1-1315.
PDBsum; 1WYG; -.
PDBsum; 2E3T; -.
PDBsum; 3AN1; -.
PDBsum; 4YRW; -.
PDBsum; 4YSW; -.
PDBsum; 4YTY; -.
PDBsum; 4YTZ; -.
SMR; P22985; -.
STRING; 10116.ENSRNOP00000009634; -.
BindingDB; P22985; -.
ChEMBL; CHEMBL1075246; -.
iPTMnet; P22985; -.
PhosphoSitePlus; P22985; -.
PaxDb; P22985; -.
PRIDE; P22985; -.
GeneID; 497811; -.
KEGG; rno:497811; -.
UCSC; RGD:62043; rat.
CTD; 7498; -.
RGD; 62043; Xdh.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
HOVERGEN; HBG004182; -.
InParanoid; P22985; -.
KO; K00106; -.
PhylomeDB; P22985; -.
BioCyc; MetaCyc:MONOMER-15163; -.
BRENDA; 1.17.1.4; 5301.
BRENDA; 1.17.3.2; 5301.
SABIO-RK; P22985; -.
EvolutionaryTrace; P22985; -.
PRO; PR:P22985; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IDA:RGD.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IBA:GO_Central.
GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:UniProtKB.
GO; GO:0004855; F:xanthine oxidase activity; IDA:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0010044; P:response to aluminum ion; IDA:RGD.
GO; GO:0009115; P:xanthine catabolic process; IDA:UniProtKB.
Gene3D; 1.10.150.120; -; 1.
Gene3D; 3.10.20.30; -; 1.
Gene3D; 3.30.365.10; -; 4.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR012675; Beta-grasp_dom.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
InterPro; IPR022407; OxRdtase_Mopterin_BS.
InterPro; IPR014307; Xanthine_DH_ssu.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
Glycoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
Oxidoreductase; Peroxisome; Reference proteome; Secreted.
CHAIN 1 1331 Xanthine dehydrogenase/oxidase.
/FTId=PRO_0000166086.
DOMAIN 4 91 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 228 413 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 256 263 FAD. {ECO:0000269|PubMed:15878860,
ECO:0000269|PubMed:17301076}.
NP_BIND 346 350 FAD. {ECO:0000269|PubMed:15878860,
ECO:0000269|PubMed:17301076}.
ACT_SITE 1261 1261 Proton acceptor.
METAL 43 43 Iron-sulfur 1.
METAL 48 48 Iron-sulfur 1.
METAL 51 51 Iron-sulfur 1.
METAL 73 73 Iron-sulfur 1.
METAL 112 112 Iron-sulfur 2.
METAL 115 115 Iron-sulfur 2.
METAL 147 147 Iron-sulfur 2.
METAL 149 149 Iron-sulfur 2.
METAL 767 767 Molybdenum. {ECO:0000250}.
METAL 798 798 Molybdenum; via carbonyl oxygen.
{ECO:0000250}.
METAL 912 912 Molybdenum; via amide nitrogen.
{ECO:0000250}.
METAL 1079 1079 Molybdenum; via amide nitrogen.
{ECO:0000250}.
BINDING 336 336 FAD. {ECO:0000250}.
BINDING 359 359 FAD. {ECO:0000269|PubMed:15878860,
ECO:0000269|PubMed:17301076}.
BINDING 403 403 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:15878860,
ECO:0000269|PubMed:17301076}.
BINDING 421 421 FAD. {ECO:0000250}.
BINDING 802 802 Substrate.
BINDING 880 880 Substrate.
BINDING 914 914 Substrate. {ECO:0000250}.
BINDING 1010 1010 Substrate; via amide nitrogen.
CARBOHYD 1073 1073 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 535 992 In oxidase form.
{ECO:0000305|PubMed:15878860}.
MUTAGEN 335 336 WF->AL: Converts the enzyme to the
oxidase form that utilizes molecular
oxygen as electron acceptor. Interferes
with normal conversion to the
dehydrogenase form by reducing agents.
{ECO:0000269|PubMed:17301076}.
MUTAGEN 535 535 C->A: Slows the conversion from the
dehydrogenase form to the oxidase form;
when associated with R-992. Abolishes
conversion from the dehydrogenase form to
the oxidase form; when associated with R-
992 and S-1316.
{ECO:0000269|PubMed:15878860}.
MUTAGEN 992 992 C->R: Slows the conversion from the
dehydrogenase form to the oxidase form;
when associated with A-535. Abolishes
conversion from the dehydrogenase form to
the oxidase form; when associated with A-
535 and S-1316.
{ECO:0000269|PubMed:15878860}.
MUTAGEN 1316 1316 C->S: Abolishes conversion from the
dehydrogenase form to the oxidase form;
when associated with A-535 and R-992.
{ECO:0000269|PubMed:15878860}.
STRAND 6 10 {ECO:0000244|PDB:3AN1}.
STRAND 13 17 {ECO:0000244|PDB:3AN1}.
HELIX 26 32 {ECO:0000244|PDB:3AN1}.
STRAND 44 48 {ECO:0000244|PDB:3AN1}.
STRAND 52 59 {ECO:0000244|PDB:3AN1}.
TURN 60 63 {ECO:0000244|PDB:3AN1}.
STRAND 64 71 {ECO:0000244|PDB:3AN1}.
HELIX 72 74 {ECO:0000244|PDB:3AN1}.
HELIX 77 79 {ECO:0000244|PDB:3AN1}.
STRAND 84 86 {ECO:0000244|PDB:3AN1}.
HELIX 88 91 {ECO:0000244|PDB:3AN1}.
STRAND 94 96 {ECO:0000244|PDB:1WYG}.
HELIX 99 106 {ECO:0000244|PDB:3AN1}.
HELIX 116 129 {ECO:0000244|PDB:3AN1}.
HELIX 135 140 {ECO:0000244|PDB:3AN1}.
TURN 141 144 {ECO:0000244|PDB:3AN1}.
STRAND 148 150 {ECO:0000244|PDB:3AN1}.
HELIX 153 159 {ECO:0000244|PDB:3AN1}.
HELIX 160 162 {ECO:0000244|PDB:3AN1}.
HELIX 197 199 {ECO:0000244|PDB:3AN1}.
HELIX 205 207 {ECO:0000244|PDB:3AN1}.
HELIX 213 218 {ECO:0000244|PDB:3AN1}.
STRAND 226 229 {ECO:0000244|PDB:3AN1}.
STRAND 234 237 {ECO:0000244|PDB:3AN1}.
HELIX 241 250 {ECO:0000244|PDB:3AN1}.
HELIX 263 269 {ECO:0000244|PDB:3AN1}.
STRAND 275 279 {ECO:0000244|PDB:3AN1}.
HELIX 284 287 {ECO:0000244|PDB:3AN1}.
STRAND 289 291 {ECO:0000244|PDB:3AN1}.
STRAND 293 299 {ECO:0000244|PDB:3AN1}.
HELIX 304 317 {ECO:0000244|PDB:3AN1}.
HELIX 320 322 {ECO:0000244|PDB:3AN1}.
HELIX 324 334 {ECO:0000244|PDB:3AN1}.
HELIX 339 342 {ECO:0000244|PDB:3AN1}.
HELIX 347 353 {ECO:0000244|PDB:3AN1}.
HELIX 361 366 {ECO:0000244|PDB:3AN1}.
STRAND 370 375 {ECO:0000244|PDB:3AN1}.
STRAND 378 383 {ECO:0000244|PDB:3AN1}.
HELIX 386 388 {ECO:0000244|PDB:3AN1}.
STRAND 402 409 {ECO:0000244|PDB:3AN1}.
STRAND 415 422 {ECO:0000244|PDB:3AN1}.
STRAND 424 428 {ECO:0000244|PDB:3AN1}.
STRAND 432 441 {ECO:0000244|PDB:3AN1}.
STRAND 445 461 {ECO:0000244|PDB:3AN1}.
TURN 466 468 {ECO:0000244|PDB:3AN1}.
HELIX 470 472 {ECO:0000244|PDB:3AN1}.
STRAND 476 478 {ECO:0000244|PDB:3AN1}.
HELIX 479 492 {ECO:0000244|PDB:3AN1}.
HELIX 504 528 {ECO:0000244|PDB:3AN1}.
TURN 529 531 {ECO:0000244|PDB:4YTY}.
HELIX 532 535 {ECO:0000244|PDB:3AN1}.
HELIX 540 546 {ECO:0000244|PDB:3AN1}.
STRAND 555 559 {ECO:0000244|PDB:3AN1}.
STRAND 565 567 {ECO:0000244|PDB:1WYG}.
HELIX 582 586 {ECO:0000244|PDB:3AN1}.
HELIX 593 595 {ECO:0000244|PDB:3AN1}.
STRAND 603 609 {ECO:0000244|PDB:3AN1}.
STRAND 611 621 {ECO:0000244|PDB:3AN1}.
HELIX 625 627 {ECO:0000244|PDB:3AN1}.
STRAND 631 635 {ECO:0000244|PDB:3AN1}.
HELIX 637 639 {ECO:0000244|PDB:3AN1}.
STRAND 645 647 {ECO:0000244|PDB:3AN1}.
STRAND 652 655 {ECO:0000244|PDB:3AN1}.
STRAND 658 660 {ECO:0000244|PDB:3AN1}.
STRAND 666 674 {ECO:0000244|PDB:3AN1}.
HELIX 675 683 {ECO:0000244|PDB:3AN1}.
STRAND 686 691 {ECO:0000244|PDB:3AN1}.
HELIX 698 703 {ECO:0000244|PDB:3AN1}.
STRAND 707 710 {ECO:0000244|PDB:3AN1}.
STRAND 712 717 {ECO:0000244|PDB:3AN1}.
HELIX 719 725 {ECO:0000244|PDB:3AN1}.
STRAND 727 736 {ECO:0000244|PDB:3AN1}.
STRAND 748 753 {ECO:0000244|PDB:3AN1}.
STRAND 760 764 {ECO:0000244|PDB:3AN1}.
HELIX 769 780 {ECO:0000244|PDB:3AN1}.
HELIX 784 786 {ECO:0000244|PDB:3AN1}.
STRAND 787 792 {ECO:0000244|PDB:3AN1}.
TURN 798 801 {ECO:0000244|PDB:3AN1}.
STRAND 802 804 {ECO:0000244|PDB:1WYG}.
HELIX 806 819 {ECO:0000244|PDB:3AN1}.
STRAND 823 826 {ECO:0000244|PDB:3AN1}.
HELIX 829 835 {ECO:0000244|PDB:3AN1}.
STRAND 842 850 {ECO:0000244|PDB:3AN1}.
STRAND 856 866 {ECO:0000244|PDB:3AN1}.
HELIX 874 883 {ECO:0000244|PDB:3AN1}.
TURN 884 888 {ECO:0000244|PDB:3AN1}.
STRAND 892 901 {ECO:0000244|PDB:3AN1}.
TURN 912 915 {ECO:0000244|PDB:3AN1}.
HELIX 916 934 {ECO:0000244|PDB:3AN1}.
HELIX 938 945 {ECO:0000244|PDB:3AN1}.
HELIX 964 974 {ECO:0000244|PDB:3AN1}.
HELIX 977 990 {ECO:0000244|PDB:3AN1}.
STRAND 992 1008 {ECO:0000244|PDB:3AN1}.
HELIX 1012 1014 {ECO:0000244|PDB:3AN1}.
STRAND 1016 1023 {ECO:0000244|PDB:3AN1}.
STRAND 1029 1034 {ECO:0000244|PDB:3AN1}.
STRAND 1038 1040 {ECO:0000244|PDB:3AN1}.
HELIX 1042 1054 {ECO:0000244|PDB:3AN1}.
HELIX 1058 1060 {ECO:0000244|PDB:3AN1}.
STRAND 1061 1063 {ECO:0000244|PDB:4YSW}.
TURN 1068 1070 {ECO:0000244|PDB:3AN1}.
TURN 1079 1081 {ECO:0000244|PDB:1WYG}.
HELIX 1082 1107 {ECO:0000244|PDB:3AN1}.
STRAND 1108 1111 {ECO:0000244|PDB:3AN1}.
HELIX 1113 1122 {ECO:0000244|PDB:3AN1}.
STRAND 1128 1134 {ECO:0000244|PDB:3AN1}.
TURN 1142 1145 {ECO:0000244|PDB:3AN1}.
STRAND 1151 1165 {ECO:0000244|PDB:3AN1}.
TURN 1166 1168 {ECO:0000244|PDB:3AN1}.
STRAND 1171 1181 {ECO:0000244|PDB:3AN1}.
HELIX 1188 1207 {ECO:0000244|PDB:3AN1}.
TURN 1224 1226 {ECO:0000244|PDB:3AN1}.
HELIX 1232 1234 {ECO:0000244|PDB:3AN1}.
STRAND 1237 1243 {ECO:0000244|PDB:3AN1}.
TURN 1250 1252 {ECO:0000244|PDB:1WYG}.
HELIX 1253 1255 {ECO:0000244|PDB:3AN1}.
HELIX 1264 1267 {ECO:0000244|PDB:3AN1}.
HELIX 1268 1285 {ECO:0000244|PDB:3AN1}.
STRAND 1286 1289 {ECO:0000244|PDB:2E3T}.
HELIX 1301 1307 {ECO:0000244|PDB:3AN1}.
HELIX 1311 1316 {ECO:0000244|PDB:3AN1}.
SEQUENCE 1331 AA; 146243 MW; BF2586A9C63A0B2C CRC64;
MTADELVFFV NGKKVVEKNA DPETTLLVYL RRKLGLCGTK LGCGEGGCGA CTVMISKYDR
LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV QERIARSHGS QCGFCTPGIV
MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT GYRPILQGFR TFAKDGGCCG GSGNNPNCCM
NQTKDQTVSL SPSLFNPEDF KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST
MEELLDLKAQ HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN IITASPISDL
NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE EILLSIEIPY SKEGEFFSAF
KQASRREDDI AKVTSGMRVL FKPGTIEVQE LSLCFGGMAD RTISALKTTP KQLSKSWNEE
LLQSVCAGLA EELQLAPDAP GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP
TFASATLLFQ KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN DETVFAKDEV
TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD AINNNSFYGS EIKIEKGDLK
KGFSEADNVV SGELYIGGQE HFYLETNCTI AVPKGEAGEM ELFVSTQNTM KTQSFVAKML
GVPDNRIVVR VKRMGGGFGG KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH
PFLAKYKVGF MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG DLTHFNQKLE
GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI IPTKFGISFT LPFLNQGGAL
VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA SRALKIPTSK IHISETSTNT VPNTSPTAAS
ASADLNGQGV YEACQTILKR LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY
SFETNSGNPF HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK RAIYASKAVG
EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT PEKIRNACVD QFTTLCVTGV
PENCKSWSVR I


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