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Database: UniProt
Entry: A0A2K6R7D6_RHIRO
LinkDB: A0A2K6R7D6_RHIRO
Original site: A0A2K6R7D6_RHIRO 
ID   A0A2K6R7D6_RHIRO        Unreviewed;       303 AA.
AC   A0A2K6R7D6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Heme oxygenase 1 {ECO:0000256|ARBA:ARBA00040247};
DE            EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN   Name=HMOX1 {ECO:0000313|Ensembl:ENSRROP00000036947.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000036947.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000036947.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A2K6R7D6; -.
DR   STRING; 61622.ENSRROP00000036947; -.
DR   Ensembl; ENSRROT00000061415.1; ENSRROP00000036947.1; ENSRROG00000041914.1.
DR   GeneTree; ENSGT00390000017673; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; IEA:Ensembl.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR   GO; GO:0072719; P:cellular response to cisplatin; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0042167; P:heme catabolic process; IEA:Ensembl.
DR   GO; GO:0006788; P:heme oxidation; IEA:Ensembl.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0016236; P:macroautophagy; IEA:Ensembl.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR   GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0002246; P:wound healing involved in inflammatory response; IEA:Ensembl.
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   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}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          239..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  34339 MW;  54F73DC550BCE819 CRC64;
     LFSSVLRAAA PSTGRMERPQ PDSMPQDLSE ALKEATKEVH TQAENAEFMR NFQKGQVTRE
     GFKLVMASLH HIYVALEEEI ERNKESPVFT PVYFPEELHR KAALEQDLAF WYGPRWQEVI
     PYTPAMQRYV KRLHEVGRTE PELLVAHAYT RYLGDLSGGQ MLKKIAQKAL DLPSSGEGLA
     FFTFPNIVSA TKFKQLYRSR MNSLEMTPVV RQRVIEEAKT AFLLNIQLFE ELQELLTHDT
     KDQSPSQAPG LRQRASNKGQ DSAPVETPRG KPPLNARSQA PLLRWVLTLS FLVATVAVGL
     YAM
//
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