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P22315

- HEMH_MOUSE

UniProt

P22315 - HEMH_MOUSE

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Protein

Ferrochelatase, mitochondrial

Gene
Fech
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.UniRule annotation

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.UniRule annotation

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.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi193 – 1931Iron-sulfur (2Fe-2S)
Active sitei227 – 2271 By similarity
Active sitei380 – 3801 By 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
Complete GO annotation...

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
Complete GO annotation...

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, mitochondrialUniRule annotationPRO_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.UniRule annotation

Gene expression databases

ArrayExpressiP22315.
BgeeiP22315.
CleanExiMM_FECH.
GenevestigatoriP22315.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiP22315. 3 interactions.
MINTiMINT-1842883.

Structurei

3D structure databases

ProteinModelPortaliP22315.
SMRiP22315. Positions 64-420.

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.

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

« Hide

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.

Natural variant

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

Sequence conflict

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

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