ID F1RK58_PIG Unreviewed; 294 AA.
AC F1RK58; A0A4X1VMC1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=heme oxygenase (biliverdin-producing) {ECO:0000256|ARBA:ARBA00012360};
DE EC=1.14.14.18 {ECO:0000256|ARBA:ARBA00012360};
GN Name=HMOX2 {ECO:0000313|Ensembl:ENSSSCP00000008480.3,
GN ECO:0000313|VGNC:VGNC:88912};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000008480.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000008480.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000008480.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HDB66700.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
RN [3] {ECO:0000313|Ensembl:ENSSSCP00000008480.3}
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; DQIR01211223; HDB66700.1; -; Transcribed_RNA.
DR EMBL; DQIR01230886; HDB86363.1; -; Transcribed_RNA.
DR RefSeq; XP_013851127.1; XM_013995673.1.
DR Ensembl; ENSSSCT00000008704.5; ENSSSCP00000008480.3; ENSSSCG00000007942.5.
DR Ensembl; ENSSSCT00005045966.1; ENSSSCP00005028236.1; ENSSSCG00005028954.1.
DR GeneID; 396622; -.
DR CTD; 3163; -.
DR VGNC; VGNC:88912; HMOX2.
DR GeneTree; ENSGT00390000017673; -.
DR HOGENOM; CLU_057050_0_1_1; -.
DR OMA; ANRAFEY; -.
DR OrthoDB; 1366343at2759; -.
DR TreeFam; TF314786; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000007942; Expressed in testis and 44 other cell types or tissues.
DR Genevisible; F1RK58; SS.
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: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 1: Evidence at protein level;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1RK58};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 33607 MW; 286CA50BEC81CC21 CRC64;
MSVELETSEG VDEPEEKSSG APEKENHTRM ADLSELLKEG TKEAHDRAES TQFVKDFLKG
NIRKELFKLA TTALYFTYSA LEEEMDRNKD HPAFAPLYFP TELHRKEALV KDMEYFYGGD
WEEQAQCSEA TRKYVERIHY VGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST
GEGTQFYLFE NVDNAQQFKQ FYRARMNALD LNLETKEKIV EEANKAFEYN MQVFNELDQA
GSLLAKETLA DGLPVHDGKG DVRKCPYYSG EQDKGGKTSF QVYKLYARLL RVAA
//
