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Protein

Ferrochelatase, mitochondrial

Gene

Fech

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the ferrous insertion into protoporphyrin IX.

Catalytic activityi

Protoheme + 2 H+ = protoporphyrin + Fe2+.

Cofactori

[2Fe-2S] clusterNote: 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: protoheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes protoheme from protoporphyrin-IX.
Proteins known to be involved in this subpathway in this organism are:
  1. Ferrochelatase (Fech), Ferrochelatase (Fech), Ferrochelatase (Fech), Ferrochelatase (Fech), Ferrochelatase, mitochondrial (Fech)
This subpathway is part of the pathway protoheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoheme from protoporphyrin-IX, the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi193Iron-sulfur (2Fe-2S)1
Active sitei227By similarity1
Active sitei380By similarity1
Metal bindingi400Iron-sulfur (2Fe-2S)By similarity1
Metal bindingi403Iron-sulfur (2Fe-2S)By similarity1
Metal bindingi408Iron-sulfur (2Fe-2S)By similarity1

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • ferrochelatase activity Source: MGI
  • heme binding Source: MGI
  • iron ion binding Source: MGI
  • iron-responsive element binding Source: MGI
  • tetrapyrrole binding Source: MGI

GO - Biological processi

  • cholesterol metabolic process Source: MGI
  • detection of UV Source: MGI
  • erythrocyte differentiation Source: MGI
  • heme biosynthetic process Source: MGI
  • iron ion homeostasis Source: MGI
  • porphyrin-containing compound biosynthetic process Source: MGI
  • protoporphyrinogen IX metabolic process Source: MGI
  • regulation of eIF2 alpha phosphorylation by heme Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of hemoglobin biosynthetic process Source: MGI
  • response to light stimulus Source: MGI
  • very-low-density lipoprotein particle assembly Source: MGI

Keywordsi

Molecular functionLyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BRENDAi4.99.1.1 3474
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:95513 Fech

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53Mitochondrion1 PublicationAdd BLAST53
ChainiPRO_000000887454 – 420Ferrochelatase, mitochondrialAdd BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei56N6-acetyllysineCombined sources1
Modified residuei135N6-succinyllysineCombined sources1
Modified residuei287N6-acetyllysine; alternateCombined sources1
Modified residuei287N6-succinyllysine; alternateCombined sources1
Modified residuei412N6-acetyllysine; alternateCombined sources1
Modified residuei412N6-succinyllysine; alternateCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP22315
MaxQBiP22315
PaxDbiP22315
PeptideAtlasiP22315
PRIDEiP22315

PTM databases

iPTMnetiP22315
PhosphoSitePlusiP22315

Expressioni

Tissue specificityi

Erythroid and hepatic cells.

Inductioni

During erythroid differentiation.

Gene expression databases

CleanExiMM_FECH

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PGRMC2O151732EBI-7174007,EBI-1050125From Homo sapiens.

Protein-protein interaction databases

IntActiP22315, 9 interactors
MINTiP22315
STRINGi10090.ENSMUSP00000025484

Structurei

3D structure databases

ProteinModelPortaliP22315
SMRiP22315
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ferrochelatase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1321 Eukaryota
COG0276 LUCA
HOVERGENiHBG051898
InParanoidiP22315
PhylomeDBiP22315

Family and domain databases

CDDicd00419 Ferrochelatase_C, 1 hit
cd03411 Ferrochelatase_N, 1 hit
HAMAPiMF_00323 Ferrochelatase, 1 hit
InterProiView protein in InterPro
IPR001015 Ferrochelatase
IPR019772 Ferrochelatase_AS
IPR033644 Ferrochelatase_C
IPR033659 Ferrochelatase_N
PANTHERiPTHR11108 PTHR11108, 1 hit
PfamiView protein in Pfam
PF00762 Ferrochelatase, 1 hit
TIGRFAMsiTIGR00109 hemH, 1 hit
PROSITEiView protein in PROSITE
PS00534 FERROCHELATASE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P22315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSASANMAA ALRAAGALLR EPLVHGSSRA CQPWRCQSGA AVAATTEKVH
60 70 80 90 100
HAKTTKPQAQ PERRKPKTGI LMLNMGGPET LGEVQDFLQR LFLDRDLMTL
110 120 130 140 150
PIQNKLAPFI AKRRTPKIQE RRIGGGSPIK MWTSKQGEGM VKLLDELSPA
160 170 180 190 200
TAPHKYYIGF RYVHPLTEEA IEEMERDGLE RAIAFTQYPQ YSCSTTGSSL
210 220 230 240 250
NAIYRYYNEV GQKPTMKWST IDRWPTHPLL IQCFADHILK ELNHFPEEKR
260 270 280 290 300
SEVVILFSAH SLPMSVVNRG DPYPQEVGAT VHKVMEKLGY PNPYRLVWQS
310 320 330 340 350
KVGPVPWLGP QTDEAIKGLC ERGRKNILLV PIAFTSDHIE TLYELDIEYS
360 370 380 390 400
QVLAQKCGAE NIRRAESLNG NPLFSKALAD LVHSHIQSNK LCSTQLSLNC
410 420
PLCVNPVCRK TKSFFTSQQL
Length:420
Mass (Da):47,130
Last modified:November 1, 1991 - v2
Checksum:i9BC4DBD18727105A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti120E → EQY in AAA37615 (PubMed:1704134).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti98M → K in Fechm1Pas. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61215 mRNA Translation: AAA80530.1
M59288 mRNA Translation: AAA37615.1 Different initiation.
PIRiA37972
UniGeneiMm.1070

Similar proteinsi

Entry informationi

Entry nameiHEMH_MOUSE
AccessioniPrimary (citable) accession number: P22315
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: November 1, 1991
Last modified: May 23, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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