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   27-MAR-2024, entry version 200.
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   PDB; 8HBE; EM; 3.20 A; B=1-619.
DR   PDB; 8HBF; EM; 3.10 A; B=1-619.
DR   PDB; 8HBH; EM; 3.10 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   PDBsum; 8HBE; -.
DR   PDBsum; 8HBF; -.
DR   PDBsum; 8HBH; -.
DR   AlphaFoldDB; Q02153; -.
DR   EMDB; EMD-30618; -.
DR   EMDB; EMD-30619; -.
DR   EMDB; EMD-30620; -.
DR   EMDB; EMD-30621; -.
DR   EMDB; EMD-34623; -.
DR   EMDB; EMD-34627; -.
DR   EMDB; EMD-34632; -.
DR   EMDB; EMD-9883; -.
DR   EMDB; EMD-9884; -.
DR   EMDB; EMD-9885; -.
DR   SMR; Q02153; -.
DR   BioGRID; 109238; 33.
DR   ComplexPortal; CPX-2860; Soluble guanylate cyclase complex, SGCalpha2-SGCbeta1 variant.
DR   ComplexPortal; CPX-928; Soluble guanylate cyclase complex, SGCalpha1-SGCbeta1 variant.
DR   CORUM; Q02153; -.
DR   IntAct; Q02153; 14.
DR   MINT; Q02153; -.
DR   STRING; 9606.ENSP00000426786; -.
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; 9606-ENSP00000264424; -.
DR   PeptideAtlas; Q02153; -.
DR   ProteomicsDB; 58052; -. [Q02153-1]
DR   ProteomicsDB; 58053; -. [Q02153-2]
DR   ProteomicsDB; 6567; -.
DR   Pumba; Q02153; -.
DR   Antibodypedia; 4395; 332 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   AGR; HGNC:4687; -.
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; 2898719at2759; -.
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; 8 hits in 1143 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 208 other cell types or tissues.
DR   ExpressionAtlas; Q02153; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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; IDA:ComplexPortal.
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; 6.10.250.780; -; 1.
DR   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 3.30.450.260; Haem NO binding associated domain; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 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   PANTHER; PTHR45655:SF2; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-1; 1.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   Genevisible; Q02153; HS.
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..17
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           19..28
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:7D9R"
FT   HELIX           45..58
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           63..80
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:7D9R"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           94..99
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           101..111
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:7D9R"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          128..136
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          138..141
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:8HBH"
FT   HELIX           145..158
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          162..164
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:8HBE"
FT   STRAND          175..183
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:5MNW"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          218..223
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          227..232
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           234..239
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:8HBE"
FT   HELIX           250..253
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          254..259
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           265..270
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            271..273
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:8HBE"
FT   STRAND          305..313
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            314..317
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          318..325
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           330..335
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          345..347
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           349..397
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   HELIX           400..407
FT                   /evidence="ECO:0007829|PDB:8HBF"
FT   STRAND          415..427
FT                   /evidence="ECO:0007829|PDB:2WZ1"
FT   HELIX           430..436
FT                   /evidence="ECO:0007829|PDB:2WZ1"
FT   STRAND          439..441
FT                   /evidence="ECO:0007829|PDB:8HBH"
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          509..516
FT                   /evidence="ECO:0007829|PDB:8HBH"
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
//