ID W5M3C3_LEPOC Unreviewed; 318 AA.
AC W5M3C3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=heme oxygenase (biliverdin-producing) {ECO:0000256|ARBA:ARBA00012360};
DE EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002881.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002881.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134}.
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DR EMBL; AHAT01031940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006637092.2; XM_006637029.2.
DR RefSeq; XP_015215370.1; XM_015359884.1.
DR AlphaFoldDB; W5M3C3; -.
DR STRING; 7918.ENSLOCP00000002881; -.
DR Ensembl; ENSLOCT00000002887.1; ENSLOCP00000002881.1; ENSLOCG00000002449.1.
DR GeneID; 102694370; -.
DR KEGG; loc:102694370; -.
DR CTD; 100329531; -.
DR eggNOG; KOG4480; Eukaryota.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_057050_0_1_1; -.
DR InParanoid; W5M3C3; -.
DR OMA; ANRAFEY; -.
DR OrthoDB; 1366343at2759; -.
DR Proteomes; UP000018468; Linkage group LG13.
DR Bgee; ENSLOCG00000002449; Expressed in larva and 13 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042167; P:heme catabolic process; IBA:GO_Central.
DR GO; GO:0006788; P:heme oxidation; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
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:SF2; HEME OXYGENASE 2; 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 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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 318 AA; 36074 MW; 28EB2DC736DCED13 CRC64;
MPTEKAEGPG QMEDLPNGSS VAYEDHEEEE NVRPGDLSEL LKEGTKESHD KAENTQFVKD
FLKGRIRKEL FKLGTVALYF TYSALEEEME RNKDHPQFAP LYFPLELHRQ EALAQDLEYF
YGEDWREVVE RSEATRHYVE RIHEVGQRAP ELLVAHAYTR YMGDLSGGQV LKKVAQRALR
LPSTGEGVNF YHFAHISSAK EFKQLYRSRM NELELDQDTK ERIVEEANRA FCFNMEIFDE
LDKIGQTIKD EVLDGGLPVY EGKGDIRKCP YYAAKMAAGG GSSYACQVAV ALLRHPMGQV
LMAACVAVLA GVAAWYAM
//
