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P22315

- HEMH_MOUSE

UniProt

P22315 - HEMH_MOUSE

Protein

Ferrochelatase, mitochondrial

Gene

Fech

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    Functioni

    Catalyzes the ferrous insertion into protoporphyrin IX.

    Catalytic activityi

    Protoheme + 2 H+ = protoporphyrin + Fe2+.

    Cofactori

    Binds 1 2Fe-2S cluster.

    Enzyme regulationi

    Inhibited by nitric oxide (NO). The 2Fe-2S cluster could act as a NO sensor By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi193 – 1931Iron-sulfur (2Fe-2S)
    Active sitei227 – 2271By similarity
    Active sitei380 – 3801By similarity
    Metal bindingi400 – 4001Iron-sulfur (2Fe-2S)By similarity
    Metal bindingi403 – 4031Iron-sulfur (2Fe-2S)By similarity
    Metal bindingi408 – 4081Iron-sulfur (2Fe-2S)By similarity

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. ferrochelatase activity Source: MGI
    3. heme binding Source: MGI
    4. iron ion binding Source: MGI
    5. iron-responsive element binding Source: MGI
    6. tetrapyrrole binding Source: MGI

    GO - Biological processi

    1. cellular response to dexamethasone stimulus Source: Ensembl
    2. cholesterol metabolic process Source: MGI
    3. detection of UV Source: MGI
    4. erythrocyte differentiation Source: MGI
    5. heme biosynthetic process Source: MGI
    6. iron ion homeostasis Source: MGI
    7. porphyrin-containing compound biosynthetic process Source: MGI
    8. protoporphyrinogen IX metabolic process Source: MGI
    9. regulation of eIF2 alpha phosphorylation by heme Source: MGI
    10. regulation of gene expression Source: MGI
    11. regulation of hemoglobin biosynthetic process Source: MGI
    12. response to arsenic-containing substance Source: Ensembl
    13. response to drug Source: Ensembl
    14. response to ethanol Source: Ensembl
    15. response to insecticide Source: Ensembl
    16. response to lead ion Source: Ensembl
    17. response to light stimulus Source: MGI
    18. response to methylmercury Source: Ensembl
    19. response to platinum ion Source: Ensembl
    20. very-low-density lipoprotein particle assembly Source: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding

    Enzyme and pathway databases

    BRENDAi4.99.1.1. 3474.
    ReactomeiREACT_203298. Heme biosynthesis.
    UniPathwayiUPA00252; UER00325.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ferrochelatase, mitochondrial (EC:4.99.1.1)
    Alternative name(s):
    Heme synthase
    Protoheme ferro-lyase
    Gene namesi
    Name:Fech
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95513. Fech.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Fech are the cause of a viable autosomal recessive mutation (named Fechm1Pas or Fch) that causes jaundice and anemia.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353Mitochondrion1 PublicationAdd
    BLAST
    Chaini54 – 420367Ferrochelatase, mitochondrialPRO_0000008874Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 561N6-acetyllysine1 Publication
    Modified residuei135 – 1351N6-succinyllysine1 Publication
    Modified residuei287 – 2871N6-acetyllysine; alternate1 Publication
    Modified residuei287 – 2871N6-succinyllysine; alternate1 Publication
    Modified residuei412 – 4121N6-acetyllysine; alternate1 Publication
    Modified residuei412 – 4121N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP22315.
    PaxDbiP22315.
    PRIDEiP22315.

    PTM databases

    PhosphoSiteiP22315.

    Expressioni

    Tissue specificityi

    Erythroid and hepatic cells.

    Inductioni

    During erythroid differentiation.

    Gene expression databases

    ArrayExpressiP22315.
    BgeeiP22315.
    CleanExiMM_FECH.
    GenevestigatoriP22315.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    IntActiP22315. 3 interactions.
    MINTiMINT-1842883.

    Structurei

    3D structure databases

    ProteinModelPortaliP22315.
    SMRiP22315. Positions 64-420.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ferrochelatase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0276.
    HOVERGENiHBG051898.
    InParanoidiP22315.
    PhylomeDBiP22315.

    Family and domain databases

    HAMAPiMF_00323. Ferrochelatase.
    InterProiIPR001015. Ferrochelatase.
    IPR019772. Ferrochelatase_AS.
    [Graphical view]
    PANTHERiPTHR11108. PTHR11108. 1 hit.
    PfamiPF00762. Ferrochelatase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00109. hemH. 1 hit.
    PROSITEiPS00534. FERROCHELATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22315-1 [UniParc]FASTAAdd to Basket

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    MLSASANMAA ALRAAGALLR EPLVHGSSRA CQPWRCQSGA AVAATTEKVH    50
    HAKTTKPQAQ PERRKPKTGI LMLNMGGPET LGEVQDFLQR LFLDRDLMTL 100
    PIQNKLAPFI AKRRTPKIQE RRIGGGSPIK MWTSKQGEGM VKLLDELSPA 150
    TAPHKYYIGF RYVHPLTEEA IEEMERDGLE RAIAFTQYPQ YSCSTTGSSL 200
    NAIYRYYNEV GQKPTMKWST IDRWPTHPLL IQCFADHILK ELNHFPEEKR 250
    SEVVILFSAH SLPMSVVNRG DPYPQEVGAT VHKVMEKLGY PNPYRLVWQS 300
    KVGPVPWLGP QTDEAIKGLC ERGRKNILLV PIAFTSDHIE TLYELDIEYS 350
    QVLAQKCGAE NIRRAESLNG NPLFSKALAD LVHSHIQSNK LCSTQLSLNC 400
    PLCVNPVCRK TKSFFTSQQL 420
    Length:420
    Mass (Da):47,130
    Last modified:November 1, 1991 - v2
    Checksum:i9BC4DBD18727105A
    GO

    Sequence cautioni

    The sequence AAA37615.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201E → EQY in AAA37615. (PubMed:1704134)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981M → K in Fechm1Pas. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61215 mRNA. Translation: AAA80530.1.
    M59288 mRNA. Translation: AAA37615.1. Different initiation.
    PIRiA37972.
    UniGeneiMm.1070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61215 mRNA. Translation: AAA80530.1 .
    M59288 mRNA. Translation: AAA37615.1 . Different initiation.
    PIRi A37972.
    UniGenei Mm.1070.

    3D structure databases

    ProteinModelPortali P22315.
    SMRi P22315. Positions 64-420.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P22315. 3 interactions.
    MINTi MINT-1842883.

    PTM databases

    PhosphoSitei P22315.

    Proteomic databases

    MaxQBi P22315.
    PaxDbi P22315.
    PRIDEi P22315.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:95513. Fech.

    Phylogenomic databases

    eggNOGi COG0276.
    HOVERGENi HBG051898.
    InParanoidi P22315.
    PhylomeDBi P22315.

    Enzyme and pathway databases

    UniPathwayi UPA00252 ; UER00325 .
    BRENDAi 4.99.1.1. 3474.
    Reactomei REACT_203298. Heme biosynthesis.

    Miscellaneous databases

    ChiTaRSi FECH. mouse.
    PROi P22315.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22315.
    Bgeei P22315.
    CleanExi MM_FECH.
    Genevestigatori P22315.

    Family and domain databases

    HAMAPi MF_00323. Ferrochelatase.
    InterProi IPR001015. Ferrochelatase.
    IPR019772. Ferrochelatase_AS.
    [Graphical view ]
    PANTHERi PTHR11108. PTHR11108. 1 hit.
    Pfami PF00762. Ferrochelatase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00109. hemH. 1 hit.
    PROSITEi PS00534. FERROCHELATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, sequencing, and expression of mouse ferrochelatase."
      Taketani S., Nakahashi Y., Osumi T., Tokunaga R.
      J. Biol. Chem. 265:19377-19380(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 54-63.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-420, PROTEIN SEQUENCE OF 239-243 AND 330-335.
      Strain: ICR.
      Tissue: Liver.
    3. "Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases."
      Dailey H.A., Sellers V.M., Dailey T.A.
      J. Biol. Chem. 269:390-395(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135; LYS-287 AND LYS-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-287 AND LYS-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. Cited for: VARIANT FECHM1PAS LYS-98.
      Tissue: Liver.

    Entry informationi

    Entry nameiHEMH_MOUSE
    AccessioniPrimary (citable) accession number: P22315
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3