GenomeNet

Database: UniProt
Entry: P30519
LinkDB: P30519
Original site: P30519 
ID   HMOX2_HUMAN             Reviewed;         316 AA.
AC   P30519; A8MT35; D3DUD5; I3L430; O60605;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   12-AUG-2020, entry version 197.
DE   RecName: Full=Heme oxygenase 2;
DE            Short=HO-2;
DE            EC=1.14.14.18 {ECO:0000250|UniProtKB:O48782};
GN   Name=HMOX2; Synonyms=HO2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=7890772; DOI=10.1074/jbc.270.11.6345;
RA   Ishikawa K.;
RT   "Heme oxygenase-2. Properties of the heme complex of the purified tryptic
RT   fragment of recombinant human heme oxygenase-2.";
RL   J. Biol. Chem. 270:6345-6350(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=1575508; DOI=10.1016/0003-9861(92)90481-b;
RA   McCoubrey W.K. Jr., Ewing J.F., Maines M.D.;
RT   "Human heme oxygenase-2: characterization and expression of a full-length
RT   cDNA and evidence suggesting that the two HO-2 transcripts may differ by
RT   choice of polyadenylation signal.";
RL   Arch. Biochem. Biophys. 295:13-20(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-137 AND LEU-146.
RG   NIEHS SNPs program;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-148 (ISOFORM 2).
RA   Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
RA   Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L.,
RA   Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A.,
RA   Wohldmann P., Wilson R.;
RT   "The WashU-Merck EST project.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 2-17; 30-38; 48-59; 138-168; 206-214 AND 219-246,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA   Bienvenut W.V., Bilsland A.E., Keith W.N.;
RL   Submitted (JAN-2010) to UniProtKB.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-166.
RC   TISSUE=Intestine;
RA   Follett J., Ahn J.-Y.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, AND HEME-BINDING SITE.
RX   PubMed=17965015; DOI=10.1074/jbc.m707396200;
RA   Bianchetti C.M., Yi L., Ragsdale S.W., Phillips G.N. Jr.;
RT   "Comparison of apo- and heme-bound crystal structures of a truncated human
RT   heme oxygenase-2.";
RL   J. Biol. Chem. 282:37624-37631(2007).
CC   -!- FUNCTION: Heme oxygenase cleaves the heme ring at the alpha methene
CC       bridge to form biliverdin. Biliverdin is subsequently converted to
CC       bilirubin by biliverdin reductase. Under physiological conditions, the
CC       activity of heme oxygenase is highest in the spleen, where senescent
CC       erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be
CC       implicated in the production of carbon monoxide in brain where it could
CC       act as a neurotransmitter.
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 [NADPH--
CC         hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964,
CC         Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:57991, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:60344; EC=1.14.14.18;
CC         Evidence={ECO:0000250|UniProtKB:O48782};
CC   -!- INTERACTION:
CC       P30519; Q13520: AQP6; NbExp=3; IntAct=EBI-712096, EBI-13059134;
CC       P30519; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-712096, EBI-11343438;
CC       P30519; P07307-3: ASGR2; NbExp=3; IntAct=EBI-712096, EBI-12808270;
CC       P30519; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-712096, EBI-747430;
CC       P30519; P11912: CD79A; NbExp=3; IntAct=EBI-712096, EBI-7797864;
CC       P30519; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-712096, EBI-17233035;
CC       P30519; Q15125: EBP; NbExp=3; IntAct=EBI-712096, EBI-3915253;
CC       P30519; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-712096, EBI-18535450;
CC       P30519; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-712096, EBI-11037623;
CC       P30519; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-712096, EBI-781551;
CC       P30519; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-712096, EBI-18304435;
CC       P30519; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-712096, EBI-18938272;
CC       P30519; O00258: GET1; NbExp=3; IntAct=EBI-712096, EBI-18908258;
CC       P30519; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-712096, EBI-13345167;
CC       P30519; Q8TED1: GPX8; NbExp=3; IntAct=EBI-712096, EBI-11721746;
CC       P30519; P48051: KCNJ6; NbExp=3; IntAct=EBI-712096, EBI-12017638;
CC       P30519; Q13571: LAPTM5; NbExp=3; IntAct=EBI-712096, EBI-2865663;
CC       P30519; O14880: MGST3; NbExp=3; IntAct=EBI-712096, EBI-724754;
CC       P30519; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-712096, EBI-10192441;
CC       P30519; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-712096, EBI-18397230;
CC       P30519; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-712096, EBI-3920694;
CC       P30519; O95470: SGPL1; NbExp=3; IntAct=EBI-712096, EBI-1046170;
CC       P30519; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-712096, EBI-10262251;
CC       P30519; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-712096, EBI-17280858;
CC       P30519; P27105: STOM; NbExp=3; IntAct=EBI-712096, EBI-1211440;
CC       P30519; P21579: SYT1; NbExp=3; IntAct=EBI-712096, EBI-524909;
CC       P30519; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-712096, EBI-8638294;
CC       P30519; Q9Y320: TMX2; NbExp=3; IntAct=EBI-712096, EBI-6447886;
CC       P30519; Q3ZAQ7: VMA21; NbExp=3; IntAct=EBI-712096, EBI-1055364;
CC   -!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P30519-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P30519-2; Sequence=VSP_055031;
CC   -!- INDUCTION: Heme oxygenase 2 activity is non-inducible.
CC   -!- SIMILARITY: Belongs to the heme oxygenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=W38932; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/hmox2/";
DR   EMBL; D21243; BAA04789.1; -; mRNA.
DR   EMBL; S34389; AAB22110.2; -; mRNA.
DR   EMBL; BT019788; AAV38591.1; -; mRNA.
DR   EMBL; AY771350; AAV28730.1; -; Genomic_DNA.
DR   EMBL; AC007606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471112; EAW85299.1; -; Genomic_DNA.
DR   EMBL; CH471112; EAW85300.1; -; Genomic_DNA.
DR   EMBL; BC002396; AAH02396.1; -; mRNA.
DR   EMBL; W38932; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF051306; AAC05297.1; -; mRNA.
DR   CCDS; CCDS10517.1; -. [P30519-1]
DR   CCDS; CCDS66931.1; -. [P30519-2]
DR   PIR; I60119; I60119.
DR   PIR; S21700; S21700.
DR   RefSeq; NP_001120676.1; NM_001127204.1. [P30519-1]
DR   RefSeq; NP_001120677.1; NM_001127205.1. [P30519-1]
DR   RefSeq; NP_001120678.1; NM_001127206.2. [P30519-1]
DR   RefSeq; NP_001273196.1; NM_001286267.1.
DR   RefSeq; NP_001273197.1; NM_001286268.1. [P30519-1]
DR   RefSeq; NP_001273198.1; NM_001286269.1. [P30519-1]
DR   RefSeq; NP_001273199.1; NM_001286270.1. [P30519-1]
DR   RefSeq; NP_001273200.1; NM_001286271.1. [P30519-2]
DR   RefSeq; NP_002125.3; NM_002134.3. [P30519-1]
DR   RefSeq; XP_016878685.1; XM_017023196.1. [P30519-1]
DR   RefSeq; XP_016878686.1; XM_017023197.1. [P30519-1]
DR   PDB; 2Q32; X-ray; 2.40 A; A/B=1-264.
DR   PDB; 2QPP; X-ray; 2.61 A; A/B=1-264.
DR   PDB; 2RGZ; X-ray; 2.61 A; A/B=1-264.
DR   PDB; 4WMH; X-ray; 2.50 A; A=31-237.
DR   PDB; 5UC8; X-ray; 2.00 A; A/B/C/D=30-242.
DR   PDB; 5UC9; X-ray; 1.90 A; A/B/C/D=30-242.
DR   PDB; 5UCA; X-ray; 2.12 A; A/B/C/D=30-242.
DR   PDBsum; 2Q32; -.
DR   PDBsum; 2QPP; -.
DR   PDBsum; 2RGZ; -.
DR   PDBsum; 4WMH; -.
DR   PDBsum; 5UC8; -.
DR   PDBsum; 5UC9; -.
DR   PDBsum; 5UCA; -.
DR   SMR; P30519; -.
DR   BioGRID; 109406; 122.
DR   DIP; DIP-53564N; -.
DR   IntAct; P30519; 101.
DR   MINT; P30519; -.
DR   STRING; 9606.ENSP00000477572; -.
DR   ChEMBL; CHEMBL2546; -.
DR   DrugBank; DB00157; NADH.
DR   DrugBank; DB04912; Stannsoporfin.
DR   iPTMnet; P30519; -.
DR   MetOSite; P30519; -.
DR   PhosphoSitePlus; P30519; -.
DR   SwissPalm; P30519; -.
DR   BioMuta; HMOX2; -.
DR   DMDM; 1170328; -.
DR   EPD; P30519; -.
DR   jPOST; P30519; -.
DR   MassIVE; P30519; -.
DR   MaxQB; P30519; -.
DR   PaxDb; P30519; -.
DR   PeptideAtlas; P30519; -.
DR   PRIDE; P30519; -.
DR   ProteomicsDB; 47391; -.
DR   ProteomicsDB; 54710; -. [P30519-1]
DR   Antibodypedia; 11116; 606 antibodies.
DR   DNASU; 3163; -.
DR   Ensembl; ENST00000219700; ENSP00000219700; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000398595; ENSP00000381595; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000406590; ENSP00000385100; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000414777; ENSP00000391637; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000458134; ENSP00000394103; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000570646; ENSP00000459214; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000575120; ENSP00000460926; ENSG00000103415. [P30519-2]
DR   Ensembl; ENST00000612525; ENSP00000481295; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000615778; ENSP00000484422; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000619528; ENSP00000484423; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000619913; ENSP00000484467; ENSG00000103415. [P30519-1]
DR   Ensembl; ENST00000620445; ENSP00000478785; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000621065; ENSP00000481811; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000622146; ENSP00000483319; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000631540; ENSP00000487673; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000631677; ENSP00000488579; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000632458; ENSP00000488880; ENSG00000277424. [P30519-1]
DR   Ensembl; ENST00000633319; ENSP00000488769; ENSG00000277424. [P30519-2]
DR   GeneID; 3163; -.
DR   KEGG; hsa:3163; -.
DR   UCSC; uc002cwq.5; human. [P30519-1]
DR   CTD; 3163; -.
DR   DisGeNET; 3163; -.
DR   EuPathDB; HostDB:ENSG00000103415.11; -.
DR   GeneCards; HMOX2; -.
DR   HGNC; HGNC:5014; HMOX2.
DR   HPA; ENSG00000103415; Low tissue specificity.
DR   MIM; 141251; gene.
DR   neXtProt; NX_P30519; -.
DR   OpenTargets; ENSG00000103415; -.
DR   PharmGKB; PA29342; -.
DR   eggNOG; KOG4480; Eukaryota.
DR   GeneTree; ENSGT00390000017673; -.
DR   HOGENOM; CLU_057050_0_1_1; -.
DR   InParanoid; P30519; -.
DR   KO; K21418; -.
DR   OrthoDB; 1424194at2759; -.
DR   PhylomeDB; P30519; -.
DR   TreeFam; TF314786; -.
DR   BRENDA; 1.14.99.3; 2681.
DR   PathwayCommons; P30519; -.
DR   Reactome; R-HSA-189483; Heme degradation.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-917937; Iron uptake and transport.
DR   SIGNOR; P30519; -.
DR   BioGRID-ORCS; 3163; 8 hits in 876 CRISPR screens.
DR   ChiTaRS; HMOX2; human.
DR   EvolutionaryTrace; P30519; -.
DR   GeneWiki; HMOX2; -.
DR   GenomeRNAi; 3163; -.
DR   Pharos; P30519; Tchem.
DR   PRO; PR:P30519; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P30519; protein.
DR   Bgee; ENSG00000103415; Expressed in testis and 236 other tissues.
DR   ExpressionAtlas; P30519; baseline and differential.
DR   Genevisible; P30519; HS.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR   GO; GO:0042167; P:heme catabolic process; IBA:GO_Central.
DR   GO; GO:0006788; P:heme oxidation; IBA:GO_Central.
DR   GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   Gene3D; 1.20.910.10; -; 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; PTHR10720; 1.
DR   Pfam; PF01126; Heme_oxygenase; 1.
DR   PIRSF; PIRSF000343; Haem_Oase; 1.
DR   PRINTS; PR00088; HAEMOXYGNASE.
DR   SUPFAM; SSF48613; SSF48613; 1.
DR   PROSITE; PS00593; HEME_OXYGENASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW   Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome;
KW   Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:25944712, ECO:0000269|Ref.9"
FT   CHAIN           2..316
FT                   /note="Heme oxygenase 2"
FT                   /id="PRO_0000209691"
FT   REPEAT          264..269
FT                   /note="HRM 1"
FT   REPEAT          281..286
FT                   /note="HRM 2"
FT   METAL           45
FT                   /note="Iron (heme axial ligand)"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:25944712, ECO:0000269|Ref.9"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   VAR_SEQ         1..29
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.8"
FT                   /id="VSP_055031"
FT   VARIANT         137
FT                   /note="R -> Q (in dbSNP:rs17884623)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_021067"
FT   VARIANT         146
FT                   /note="P -> L (in dbSNP:rs17880805)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_021068"
FT   CONFLICT        107
FT                   /note="E -> T (in Ref. 8; W38932)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..166
FT                   /note="QV -> KC (in Ref. 10; AAC05297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="Missing (in Ref. 2; AAB22110)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="Missing (in Ref. 2; AAB22110)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281..288
FT                   /note="SCPFRTAM -> LSLPTSY (in Ref. 2; AAB22110)"
FT                   /evidence="ECO:0000305"
FT   HELIX           33..49
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           52..58
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           64..87
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   TURN            88..90
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   TURN            92..94
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           95..97
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           100..103
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           106..117
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           121..124
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           129..144
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           146..148
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           149..175
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           185..187
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           195..207
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   HELIX           213..238
FT                   /evidence="ECO:0000244|PDB:5UC9"
FT   TURN            243..247
FT                   /evidence="ECO:0000244|PDB:2Q32"
SQ   SEQUENCE   316 AA;  36033 MW;  BF4B6A341F1A81AC CRC64;
     MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG
     NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN
     WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST
     GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA
     GSTLARETLE DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL
     AAGVALAAGL LAWYYM
//
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