GCYB1_HUMAN
ID GCYB1_HUMAN Reviewed; 619 AA.
AC Q02153; B7Z426; Q86WY5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Guanylate cyclase soluble subunit beta-1 {ECO:0000305};
DE Short=GCS-beta-1;
DE EC=4.6.1.2 {ECO:0000269|PubMed:1352257, ECO:0000269|PubMed:23505436, ECO:0000269|PubMed:24669844};
DE AltName: Full=Guanylate cyclase soluble subunit beta-3 {ECO:0000303|PubMed:1352257};
DE Short=GCS-beta-3;
DE AltName: Full=Soluble guanylate cyclase small subunit;
GN Name=GUCY1B1 {ECO:0000312|HGNC:HGNC:4687};
GN Synonyms=GUC1B3, GUCSB3, GUCY1B3;
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1352257; DOI=10.1016/0014-5793(92)80594-7;
RA Giuili G., Scholl U., Bulle F., Guellaeen G.;
RT "Molecular cloning of the cDNAs coding for the two subunits of soluble
RT guanylyl cyclase from human brain.";
RL FEBS Lett. 304:83-88(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HSGC-2).
RC TISSUE=Kidney;
RA Gansemans Y., Brouckaert P., Fiers W.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSGC-1).
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 [6]
RP PROTEIN SEQUENCE OF 337-545, AND ALTERNATIVE SPLICING.
RC TISSUE=Lung;
RX PubMed=1680753; DOI=10.1016/0014-5793(91)81248-7;
RA Chhajilani V., Fraendberg P.-A., Ahlner J., Axelsson K.L., Wikberg J.E.S.;
RT "Heterogeneity in human soluble guanylate cyclase due to alternative
RT splicing.";
RL FEBS Lett. 290:157-158(1991).
RN [7] {ECO:0007744|PDB:2WZ1, ECO:0007744|PDB:3UVJ}
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 408-619 IN COMPLEX WITH GUCY1A1,
RP INTERACTION WITH GUCY1A1, SUBUNIT, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=23505436; DOI=10.1371/journal.pone.0057644;
RA Allerston C.K., von Delft F., Gileadi O.;
RT "Crystal structures of the catalytic domain of human soluble guanylate
RT cyclase.";
RL PLoS ONE 8:E57644-E57644(2013).
RN [8] {ECO:0007744|PDB:4NI2}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 408-608 IN COMPLEX WITH GUCY1A1,
RP INTERACTION WITH GUCY1A1, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24669844; DOI=10.1021/bi500129k;
RA Seeger F., Quintyn R., Tanimoto A., Williams G.J., Tainer J.A.,
RA Wysocki V.H., Garcin E.D.;
RT "Interfacial residues promote an optimal alignment of the catalytic center
RT in human soluble guanylate cyclase: heterodimerization is required but not
RT sufficient for activity.";
RL Biochemistry 53:2153-2165(2014).
CC -!- FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the
CC biosynthesis of the signaling molecule cGMP.
CC {ECO:0000250|UniProtKB:P16068, ECO:0000269|PubMed:1352257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:1352257};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P16068};
CC Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for
CC responding to nitric oxide, but not for catalytic activity.
CC {ECO:0000250|UniProtKB:P16068};
CC -!- ACTIVITY REGULATION: Activated by nitric oxide in the presence of
CC magnesium or manganese ions. {ECO:0000269|PubMed:1352257}.
CC -!- SUBUNIT: The active enzyme is formed by a heterodimer of an alpha and a
CC beta subunit. Heterodimer with GUCY1A1 (PubMed:1352257,
CC PubMed:23505436, PubMed:24669844). Can also form inactive homodimers in
CC vitro (PubMed:23505436, PubMed:24669844). {ECO:0000269|PubMed:23505436,
CC ECO:0000269|PubMed:24669844}.
CC -!- INTERACTION:
CC Q02153; Q02108: GUCY1A1; NbExp=2; IntAct=EBI-6911707, EBI-3910037;
CC Q02153-1; Q02108-1: GUCY1A1; NbExp=2; IntAct=EBI-25372164, EBI-25372173;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=HSGC-1;
CC IsoId=Q02153-1; Sequence=Displayed;
CC Name=HSGC-2;
CC IsoId=Q02153-2; Sequence=VSP_001813;
CC Name=3;
CC IsoId=Q02153-3; Sequence=VSP_054365;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex and cerebellum (at protein
CC level). {ECO:0000269|PubMed:1352257}.
CC -!- MISCELLANEOUS: There are two types of guanylate cyclases: soluble forms
CC and membrane-associated receptor forms.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; X66533; CAA47144.1; -; mRNA.
DR EMBL; AF020340; AAB94877.1; -; mRNA.
DR EMBL; AK296680; BAH12412.1; -; mRNA.
DR EMBL; AC114761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047620; AAH47620.2; -; mRNA.
DR CCDS; CCDS47154.1; -. [Q02153-1]
DR CCDS; CCDS77976.1; -. [Q02153-2]
DR CCDS; CCDS77977.1; -. [Q02153-3]
DR PIR; S23097; S23097.
DR RefSeq; NP_000848.1; NM_000857.3. [Q02153-1]
DR RefSeq; NP_001278881.1; NM_001291952.1. [Q02153-3]
DR RefSeq; NP_001278882.1; NM_001291953.1.
DR RefSeq; NP_001278883.1; NM_001291954.1. [Q02153-2]
DR PDB; 2WZ1; X-ray; 1.63 A; A/B=408-619.
DR PDB; 3UVJ; X-ray; 2.08 A; B/D=408-619.
DR PDB; 4NI2; X-ray; 1.90 A; B=408-608.
DR PDB; 5MNW; NMR; -; A=1-188.
DR PDB; 6JT0; EM; 4.00 A; B=1-619.
DR PDB; 6JT1; EM; 3.90 A; B=1-619.
DR PDB; 6JT2; EM; 3.80 A; B=1-619.
DR PDB; 7D9R; EM; 3.30 A; B=1-619.
DR PDB; 7D9S; EM; 3.40 A; B=1-619.
DR PDB; 7D9T; EM; 4.10 A; B=1-619.
DR PDB; 7D9U; EM; 3.80 A; B=1-619.
DR PDBsum; 2WZ1; -.
DR PDBsum; 3UVJ; -.
DR PDBsum; 4NI2; -.
DR PDBsum; 5MNW; -.
DR PDBsum; 6JT0; -.
DR PDBsum; 6JT1; -.
DR PDBsum; 6JT2; -.
DR PDBsum; 7D9R; -.
DR PDBsum; 7D9S; -.
DR PDBsum; 7D9T; -.
DR PDBsum; 7D9U; -.
DR AlphaFoldDB; Q02153; -.
DR SMR; Q02153; -.
DR BioGRID; 109238; 30.
DR ComplexPortal; CPX-928; Soluble guanylate cyclase complex, SGCalpha1-SGCbeta1 variant.
DR CORUM; Q02153; -.
DR IntAct; Q02153; 13.
DR MINT; Q02153; -.
DR STRING; 9606.ENSP00000264424; -.
DR BindingDB; Q02153; -.
DR ChEMBL; CHEMBL3137281; -.
DR DrugBank; DB09401; Isosorbide.
DR DrugBank; DB15456; Vericiguat.
DR DrugCentral; Q02153; -.
DR GuidetoPHARMACOLOGY; 1290; -.
DR iPTMnet; Q02153; -.
DR PhosphoSitePlus; Q02153; -.
DR BioMuta; GUCY1B3; -.
DR DMDM; 399328; -.
DR EPD; Q02153; -.
DR jPOST; Q02153; -.
DR MassIVE; Q02153; -.
DR MaxQB; Q02153; -.
DR PaxDb; Q02153; -.
DR PeptideAtlas; Q02153; -.
DR PRIDE; Q02153; -.
DR ProteomicsDB; 58052; -. [Q02153-1]
DR ProteomicsDB; 58053; -. [Q02153-2]
DR ProteomicsDB; 6567; -.
DR Antibodypedia; 4395; 296 antibodies from 36 providers.
DR DNASU; 2983; -.
DR Ensembl; ENST00000264424.13; ENSP00000264424.8; ENSG00000061918.14. [Q02153-1]
DR Ensembl; ENST00000503520.5; ENSP00000420842.1; ENSG00000061918.14. [Q02153-2]
DR Ensembl; ENST00000505764.5; ENSP00000426319.1; ENSG00000061918.14. [Q02153-3]
DR GeneID; 2983; -.
DR KEGG; hsa:2983; -.
DR MANE-Select; ENST00000264424.13; ENSP00000264424.8; NM_000857.5; NP_000848.1.
DR UCSC; uc003ipc.4; human. [Q02153-1]
DR CTD; 2983; -.
DR DisGeNET; 2983; -.
DR GeneCards; GUCY1B1; -.
DR HGNC; HGNC:4687; GUCY1B1.
DR HPA; ENSG00000061918; Low tissue specificity.
DR MIM; 139397; gene.
DR neXtProt; NX_Q02153; -.
DR OpenTargets; ENSG00000061918; -.
DR PharmGKB; PA29068; -.
DR VEuPathDB; HostDB:ENSG00000061918; -.
DR eggNOG; KOG4171; Eukaryota.
DR GeneTree; ENSGT00940000157483; -.
DR InParanoid; Q02153; -.
DR OMA; PCEDHAK; -.
DR OrthoDB; 531253at2759; -.
DR PhylomeDB; Q02153; -.
DR TreeFam; TF351403; -.
DR BRENDA; 4.6.1.2; 2681.
DR PathwayCommons; Q02153; -.
DR Reactome; R-HSA-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q02153; -.
DR SIGNOR; Q02153; -.
DR BioGRID-ORCS; 2983; 7 hits in 1063 CRISPR screens.
DR EvolutionaryTrace; Q02153; -.
DR GeneWiki; GUCY1B3; -.
DR GenomeRNAi; 2983; -.
DR Pharos; Q02153; Tclin.
DR PRO; PR:Q02153; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q02153; protein.
DR Bgee; ENSG00000061918; Expressed in middle temporal gyrus and 206 other tissues.
DR ExpressionAtlas; Q02153; baseline and differential.
DR Genevisible; Q02153; HS.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0008074; C:guanylate cyclase complex, soluble; IDA:UniProtKB.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0047805; F:cytidylate cyclase activity; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:ProtInc.
DR GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0070482; P:response to oxygen levels; IBA:GO_Central.
DR GO; GO:0099555; P:trans-synaptic signaling by nitric oxide, modulating synaptic transmission; IEA:Ensembl.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.450.260; -; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.90.1520.10; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR038158; H-NOX_domain_sf.
DR InterPro; IPR011644; Heme_NO-bd.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR042463; HNOB_dom_associated_sf.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07700; HNOB; 1.
DR Pfam; PF07701; HNOBA; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cGMP biosynthesis; Cytoplasm;
KW Direct protein sequencing; GTP-binding; Heme; Iron; Lyase; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..619
FT /note="Guanylate cyclase soluble subunit beta-1"
FT /id="PRO_0000074116"
FT DOMAIN 421..554
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 105
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250|UniProtKB:P16068"
FT VAR_SEQ 1..26
FT /note="MYGFVNHALELLVIRNYGPEVWEDIK -> MLMCFI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054365"
FT VAR_SEQ 393..425
FT /note="Missing (in isoform HSGC-2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_001813"
FT HELIX 3..28
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 63..81
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5MNW"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5MNW"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5MNW"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:7D9R"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:7D9S"
FT HELIX 349..397
FT /evidence="ECO:0007829|PDB:7D9R"
FT HELIX 400..407
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 415..427
FT /evidence="ECO:0007829|PDB:2WZ1"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:2WZ1"
FT HELIX 443..461
FT /evidence="ECO:0007829|PDB:2WZ1"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:7D9R"
FT STRAND 479..487
FT /evidence="ECO:0007829|PDB:2WZ1"
FT HELIX 492..507
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 519..533
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 539..544
FT /evidence="ECO:0007829|PDB:2WZ1"
FT HELIX 545..555
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:2WZ1"
FT HELIX 566..571
FT /evidence="ECO:0007829|PDB:2WZ1"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 582..590
FT /evidence="ECO:0007829|PDB:2WZ1"
FT STRAND 599..607
FT /evidence="ECO:0007829|PDB:2WZ1"
SQ SEQUENCE 619 AA; 70514 MW; 231E4E660DE02AA1 CRC64;
MYGFVNHALE LLVIRNYGPE VWEDIKKEAQ LDEEGQFLVR IIYDDSKTYD LVAAASKVLN
LNAGEILQMF GKMFFVFCQE SGYDTILRVL GSNVREFLQN LDALHDHLAT IYPGMRAPSF
RCTDAEKGKG LILHYYSERE GLQDIVIGII KTVAQQIHGT EIDMKVIQQR NEECDHTQFL
IEEKESKEED FYEDLDRFEE NGTQESRISP YTFCKAFPFH IIFDRDLVVT QCGNAIYRVL
PQLQPGNCSL LSVFSLVRPH IDISFHGILS HINTVFVLRS KEGLLDVEKL ECEDELTGTE
ISCLRLKGQM IYLPEADSIL FLCSPSVMNL DDLTRRGLYL SDIPLHDATR DLVLLGEQFR
EEYKLTQELE ILTDRLQLTL RALEDEKKKT DTLLYSVLPP SVANELRHKR PVPAKRYDNV
TILFSGIVGF NAFCSKHASG EGAMKIVNLL NDLYTRFDTL TDSRKNPFVY KVETVGDKYM
TVSGLPEPCI HHARSICHLA LDMMEIAGQV QVDGESVQIT IGIHTGEVVT GVIGQRMPRY
CLFGNTVNLT SRTETTGEKG KINVSEYTYR CLMSPENSDP QFHLEHRGPV SMKGKKEPMQ
VWFLSRKNTG TEETKQDDD
