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Database: UniProt
Entry: Q02153
LinkDB: Q02153
Original site: Q02153 
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   23-FEB-2022, entry version 189.
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   SMR; Q02153; -.
DR   BioGRID; 109238; 30.
DR   ComplexPortal; CPX-928; Soluble guanylate cyclase complex, SGCalpha1-SGCbeta1 variant.
DR   CORUM; Q02153; -.
DR   IntAct; Q02153; 12.
DR   STRING; 9606.ENSP00000264424; -.
DR   BindingDB; Q02153; -.
DR   ChEMBL; CHEMBL3137281; -.
DR   DrugCentral; Q02153; -.
DR   GuidetoPHARMACOLOGY; 1290; -.
DR   iPTMnet; Q02153; -.
DR   PhosphoSitePlus; Q02153; -.
DR   BioMuta; GUCY1B3; -.
DR   DMDM; 399328; -.
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; 291 antibodies from 36 providers.
DR   DNASU; 2983; -.
DR   Ensembl; ENST00000264424; ENSP00000264424; ENSG00000061918.
DR   Ensembl; ENST00000503520; ENSP00000420842; ENSG00000061918. [Q02153-2]
DR   Ensembl; ENST00000505764; ENSP00000426319; ENSG00000061918. [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; VQTGCTI; -.
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; 5 hits in 1033 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 caudate nucleus and 241 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:0048786; C:presynaptic active zone; IBA:GO_Central.
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:0099555; P:trans-synaptic signaling by nitric oxide, modulating synaptic transmission; IBA:GO_Central.
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   METAL           105
FT                   /note="Iron (heme proximal ligand)"
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..16
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           19..28
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   TURN            39..41
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           45..58
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           63..80
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           85..88
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           101..107
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           143..155
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   STRAND          177..184
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:5MNW"
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          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
//
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