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Database: UniProt
Entry: E0A2T5_CHICK
LinkDB: E0A2T5_CHICK
Original site: E0A2T5_CHICK 
ID   E0A2T5_CHICK            Unreviewed;       296 AA.
AC   E0A2T5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=heme oxygenase (biliverdin-producing) {ECO:0000256|ARBA:ARBA00012360};
DE            EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN   Name=hmox1 {ECO:0000313|EMBL:ADK26061.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|EMBL:ADK26061.1};
RN   [1] {ECO:0000313|EMBL:ADK26061.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang Z., Deng X.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADK26061.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21406370;
RA   Wang Z.P., Liu R.F., Wang A.R., Li J.Y., Deng X.M.;
RT   "Expression and activity analysis reveal that heme oxygenase (decycling) 1
RT   is associated with blue egg formation.";
RL   Poult. Sci. 90:836-841(2011).
CC   -!- SIMILARITY: Belongs to the heme oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006134}.
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DR   EMBL; HM237181; ADK26061.1; -; mRNA.
DR   AlphaFoldDB; E0A2T5; -.
DR   VEuPathDB; HostDB:geneid_396287; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006788; P:heme oxidation; IEA:InterPro.
DR   CDD; cd19165; HemeO; 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   2: Evidence at transcript level;
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   ECO:0000313|EMBL:ADK26061.1}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          231..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   296 AA;  33479 MW;  37481D1C7530BBB8 CRC64;
     METSQPHNAE SMSQDLSELL KEATKEVHEQ AENTPFMKNF QKGQVSLHEF KLVTASLYFI
     YSALEEEIER NKDNPVYAPV YFPMELHRKA ALEKDLEYFY GSNRRAEIPC PEATQKYVER
     LHVIGKKHPE LLVAHAYTRY LGDLSGGQVL KKIAQKALQL PSTGEGLAFF TFDGVSNATK
     FKQLYRSRMN ALEMDHATKK RVLEEAKKAF LLNIQVFEAL QKLVSKSQEN GHAVQPKAEL
     RTRSVNKSHE NSPAAGKDSE RTSRMQADML TTSPLVRWLL ALGFIATTVA VGLFAM
//
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