ID A0A2I2ZWA6_GORGO Unreviewed; 285 AA.
AC A0A2I2ZWA6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Heme oxygenase {ECO:0000256|PIRNR:PIRNR000343};
DE EC=1.14.14.18 {ECO:0000256|PIRNR:PIRNR000343};
GN Name=HMOX1 {ECO:0000313|Ensembl:ENSGGOP00000051341.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000051341.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000051341.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000051341.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000051341.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the oxidative cleavage of heme at the alpha-methene
CC bridge carbon, released as carbon monoxide (CO), to generate biliverdin
CC IXalpha, while releasing the central heme iron chelate as ferrous iron.
CC {ECO:0000256|ARBA:ARBA00037361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] =
CC biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57991,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:60344; EC=1.14.14.18;
CC Evidence={ECO:0000256|ARBA:ARBA00036473};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21765;
CC Evidence={ECO:0000256|ARBA:ARBA00036473};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00037869}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00037869}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00037869}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134, ECO:0000256|PIRNR:PIRNR000343}.
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DR EMBL; CABD030120954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2ZWA6; -.
DR Ensembl; ENSGGOT00000043364.1; ENSGGOP00000051341.1; ENSGGOG00000009660.3.
DR GeneTree; ENSGT00390000017673; -.
DR Proteomes; UP000001519; Chromosome 22.
DR Bgee; ENSGGOG00000009660; Expressed in liver and 5 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006788; P:heme oxidation; IEA:UniProtKB-UniRule.
DR CDD; cd00232; HemeO-like; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR InterPro; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR018207; Haem_oxygenase_CS.
DR PANTHER; PTHR10720; HEME OXYGENASE; 1.
DR PANTHER; PTHR10720:SF1; HEME OXYGENASE 1; 1.
DR Pfam; PF01126; Heme_oxygenase; 1.
DR PIRSF; PIRSF000343; Haem_Oase; 1.
DR PRINTS; PR00088; HAEMOXYGNASE.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000343};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000343};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000343};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 220..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 22
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-2"
FT BINDING 131
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
FT BINDING 180
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000256|PIRSR:PIRSR000343-1"
SQ SEQUENCE 285 AA; 32423 MW; BED3829B62C9B794 CRC64;
GVRDHMPQDL SEALKEATKE VHTQAENAEF MRNFQKGQVT RDGFKLVMAS LYHIYVALEE
EIERNKESPV FAPVYFPEEL HRKAALEQDL AFWYGPRWQE VIPYTPAMQR YVKRLHEVGR
TEPELLVAHA YTRYLGDLSG GQVLKKIAQK ALDLPSSGEG LAFFTFPNIA SATKFKQLYR
SRMNSLEMTP AVRQRVIEEA KTAFLLNIQL FEELQELLTH DTKDQSPSRA PGLRQRASNK
VQDSAPVETP RGKPPLNTHS QAPLLRWVLT LSFLVATVAV GLYAM
//