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Protein

Molybdenum cofactor biosynthesis protein 1

Gene

Mocs1

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

Functioni

Isoform Mocs1a and isoform Mocs1b probably form a complex that catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).By similarity

Catalytic activityi

GTP = cyclic pyranopterin phosphate + diphosphate.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.By similarity

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731GTPBy similarity
Metal bindingi80 – 801Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Metal bindingi84 – 841Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Binding sitei86 – 861S-adenosyl-L-methionineBy similarity
Metal bindingi87 – 871Iron-sulfur 1 (4Fe-4S-S-AdoMet)By similarity
Binding sitei123 – 1231GTPBy similarity
Binding sitei127 – 1271S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei154 – 1541GTPBy similarity
Binding sitei178 – 1781S-adenosyl-L-methionineBy similarity
Binding sitei215 – 2151GTPBy similarity
Binding sitei249 – 2491S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi312 – 3121Iron-sulfur 2 (4Fe-4S-substrate)By similarity
Metal bindingi315 – 3151Iron-sulfur 2 (4Fe-4S-substrate)By similarity
Metal bindingi329 – 3291Iron-sulfur 2 (4Fe-4S-substrate)By similarity
Active sitei606 – 6061For molybdenum cofactor biosynthesis protein C activitySequence analysis

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • cyclic pyranopterin monophosphate synthase activity Source: MGI
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • molybdopterin cofactor biosynthetic process Source: MGI
  • Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

4Fe-4S, GTP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-MMU-947581. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdenum cofactor biosynthesis protein 1
Including the following 2 domains:
Cyclic pyranopterin monophosphate synthase (EC:4.1.99.18)
Alternative name(s):
Molybdenum cofactor biosynthesis protein A
Cyclic pyranopterin monophosphate synthase accessory protein
Alternative name(s):
Molybdenum cofactor biosynthesis protein C
Gene namesi
Name:Mocs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1928904. Mocs1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Death between days 1 and 11 after birth, due to a progressive neurological disorder caused by massive cell death. Death is caused by the absence of molybdenum cofactor, resulting in elevated sulfite and diminished sulfate levels throughout the organism. Mice do not possess any sulfite oxidase or xanthine dehydrogenase activity. No organ abnormalities are observed and the synaptic localization of inhibitory receptors appears normal. Long-term rescue results have been obtained in mice lacking Mocs1 thanks to an adeno-associated virus-mediated gene transfer.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636636Molybdenum cofactor biosynthesis protein 1PRO_0000369400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphoserineBy similarity
Modified residuei198 – 1981N6-acetyllysineBy similarity
Modified residuei528 – 5281N6-acetyllysineCombined sources
Isoform Mocs1a (identifier: Q5RKZ7-2)
Modified residuei385 – 38511-thioglycineBy similarity

Post-translational modificationi

Isoform Mocs1a is probably thiocarboxylated at its C-terminus. Thiocarboxylation probably plays a central role in molybdenum cofactor biosynthesis. Thiocarboxylation is absent in isoform Mocs1b, which lacks the C-terminal Gly residue.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5RKZ7.
MaxQBiQ5RKZ7.
PaxDbiQ5RKZ7.
PeptideAtlasiQ5RKZ7.
PRIDEiQ5RKZ7.

PTM databases

iPTMnetiQ5RKZ7.
PhosphoSiteiQ5RKZ7.

Expressioni

Gene expression databases

BgeeiQ5RKZ7.
ExpressionAtlasiQ5RKZ7. baseline and differential.
GenevisibleiQ5RKZ7. MM.

Interactioni

Subunit structurei

Isoform Mocs1a and isoform Mocs1b probably form a heterooligomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000133694.

Structurei

3D structure databases

ProteinModelPortaliQ5RKZ7.
SMRiQ5RKZ7. Positions 61-351, 490-635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383Molybdenum cofactor biosynthesis protein AAdd
BLAST
Regioni317 – 3193GTP bindingBy similarity
Regioni414 – 636223Molybdenum cofactor biosynthesis protein CAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the MoaC family.Curated
In the N-terminal section; belongs to the MoaA/NifB/PqqE family.Curated

Phylogenomic databases

eggNOGiKOG2876. Eukaryota.
COG0315. LUCA.
COG2896. LUCA.
GeneTreeiENSGT00390000016567.
HOGENOMiHOG000228683.
InParanoidiQ5RKZ7.
KOiK03639.
OMAiDMCKAVT.
OrthoDBiEOG72JWHH.
PhylomeDBiQ5RKZ7.
TreeFamiTF300424.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.70.640. 1 hit.
HAMAPiMF_01224_B. MoaC_B.
MF_01225_B. MoaA_B.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR023045. Mo_CF_biosynth-C.
IPR023046. Mo_CF_biosynth-C_bac.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR002820. Mopterin_CF_biosynth-C_dom.
IPR007197. rSAM.
[Graphical view]
PfamiPF01967. MoaC. 1 hit.
PF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55040. SSF55040. 1 hit.
TIGRFAMsiTIGR02666. moaA. 1 hit.
TIGR00581. moaC. 1 hit.
PROSITEiPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Mocs1b (identifier: Q5RKZ7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAARPAFGIV RQLLRSNARG CSSGAPVTQP RPGEPSRPTR EGLSLRLQFL
60 70 80 90 100
QEHAAPFSAF LTDSFGRQHS YLRISLTEKC NLRCQYCMPE EGVPLTPKAD
110 120 130 140 150
LLTTEEILTL ARLFVKEGVD KIRLTGGEPL IRPDVVDIVA RLHGLEGLRT
160 170 180 190 200
IGLTTNGINL ARLLPRLQQA GLNAVNISLD TLVPAKFEFI VRRKGFHKVM
210 220 230 240 250
EGIHKAIELG YKPVKVNCVV MRGLNEDELL DFVALTEGLP LDVRFIEYMP
260 270 280 290 300
FDGNKWNFKK MVSYKEMLDT IRQRWPGLEK LPEEDSSTAK AFKIPGFQGQ
310 320 330 340 350
ISFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEEE
360 370 380 390 400
LLRIIGAAVG RKKRQHAGMF NIAQMKNRPM ILIGVLLMLQ DSPPARWSNF
410 420 430 440 450
SWDPLRVRNP SARQCLSDQM ASLWKRHCIP KALPLSQQCL GSGSPQRHYS
460 470 480 490 500
SYPDPDTHSK CLSTGSQAPD APSGPGPTSN QLTHVDSAGR ASMVDVGGKP
510 520 530 540 550
ETERVAVASA MVLLGPVAFK LVQQNQLKKG DALVVAQLAG VQAAKLTSQL
560 570 580 590 600
IPLCHHVALS HVQVHLELDS TRHAVLIQAS CRARGPTGVE MEALTSAAMA
610 620 630
ALTVYDMCKA VSRDIVVTEV KLISKTGGQR GDFHRA
Length:636
Mass (Da):69,859
Last modified:April 14, 2009 - v2
Checksum:i9AEFB16970B3EE9F
GO
Isoform Mocs1a (identifier: Q5RKZ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     385-385: V → G
     386-636: Missing.

Show »
Length:385
Mass (Da):42,980
Checksum:i5A2486FF1AF54912
GO
Isoform 3 (identifier: Q5RKZ7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-387: Missing.

Show »
Length:249
Mass (Da):26,628
Checksum:iF714394D01C4D122
GO

Sequence cautioni

The sequence AAI47413.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671M → V in AAF67845 (PubMed:10917590).Curated
Sequence conflicti274 – 2741R → Q in AAH49914 (PubMed:15489334).Curated
Sequence conflicti289 – 2891A → T in AAF67845 (PubMed:10917590).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 387387Missing in isoform 3. 1 PublicationVSP_036849Add
BLAST
Alternative sequencei385 – 3851V → G in isoform Mocs1a. 2 PublicationsVSP_036850
Alternative sequencei386 – 636251Missing in isoform Mocs1a. 2 PublicationsVSP_036851Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC165258 Genomic DNA. No translation available.
BC027444 mRNA. Translation: AAH27444.1.
BC049914 mRNA. Translation: AAH49914.1.
BC147411 mRNA. Translation: AAI47412.1.
BC147412 mRNA. Translation: AAI47413.1. Different initiation.
BC172067 mRNA. Translation: AAI72067.1.
AF214016 mRNA. Translation: AAF67845.1.
AF214016 mRNA. Translation: AAF67846.1.
CCDSiCCDS50143.1. [Q5RKZ7-1]
CCDS57100.1. [Q5RKZ7-2]
RefSeqiNP_064426.2. NM_020042.2. [Q5RKZ7-1]
NP_082740.1. NM_028464.1. [Q5RKZ7-2]
UniGeneiMm.22256.

Genome annotation databases

EnsembliENSMUST00000024797; ENSMUSP00000024797; ENSMUSG00000064120. [Q5RKZ7-2]
ENSMUST00000173033; ENSMUSP00000133694; ENSMUSG00000064120. [Q5RKZ7-1]
GeneIDi56738.
KEGGimmu:56738.
UCSCiuc008cyg.2. mouse. [Q5RKZ7-1]
uc008cyh.2. mouse. [Q5RKZ7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC165258 Genomic DNA. No translation available.
BC027444 mRNA. Translation: AAH27444.1.
BC049914 mRNA. Translation: AAH49914.1.
BC147411 mRNA. Translation: AAI47412.1.
BC147412 mRNA. Translation: AAI47413.1. Different initiation.
BC172067 mRNA. Translation: AAI72067.1.
AF214016 mRNA. Translation: AAF67845.1.
AF214016 mRNA. Translation: AAF67846.1.
CCDSiCCDS50143.1. [Q5RKZ7-1]
CCDS57100.1. [Q5RKZ7-2]
RefSeqiNP_064426.2. NM_020042.2. [Q5RKZ7-1]
NP_082740.1. NM_028464.1. [Q5RKZ7-2]
UniGeneiMm.22256.

3D structure databases

ProteinModelPortaliQ5RKZ7.
SMRiQ5RKZ7. Positions 61-351, 490-635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000133694.

PTM databases

iPTMnetiQ5RKZ7.
PhosphoSiteiQ5RKZ7.

Proteomic databases

EPDiQ5RKZ7.
MaxQBiQ5RKZ7.
PaxDbiQ5RKZ7.
PeptideAtlasiQ5RKZ7.
PRIDEiQ5RKZ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024797; ENSMUSP00000024797; ENSMUSG00000064120. [Q5RKZ7-2]
ENSMUST00000173033; ENSMUSP00000133694; ENSMUSG00000064120. [Q5RKZ7-1]
GeneIDi56738.
KEGGimmu:56738.
UCSCiuc008cyg.2. mouse. [Q5RKZ7-1]
uc008cyh.2. mouse. [Q5RKZ7-2]

Organism-specific databases

CTDi4337.
MGIiMGI:1928904. Mocs1.

Phylogenomic databases

eggNOGiKOG2876. Eukaryota.
COG0315. LUCA.
COG2896. LUCA.
GeneTreeiENSGT00390000016567.
HOGENOMiHOG000228683.
InParanoidiQ5RKZ7.
KOiK03639.
OMAiDMCKAVT.
OrthoDBiEOG72JWHH.
PhylomeDBiQ5RKZ7.
TreeFamiTF300424.

Enzyme and pathway databases

UniPathwayiUPA00344.
ReactomeiR-MMU-947581. Molybdenum cofactor biosynthesis.

Miscellaneous databases

PROiQ5RKZ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ5RKZ7.
ExpressionAtlasiQ5RKZ7. baseline and differential.
GenevisibleiQ5RKZ7. MM.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.30.70.640. 1 hit.
HAMAPiMF_01224_B. MoaC_B.
MF_01225_B. MoaA_B.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR023045. Mo_CF_biosynth-C.
IPR023046. Mo_CF_biosynth-C_bac.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR002820. Mopterin_CF_biosynth-C_dom.
IPR007197. rSAM.
[Graphical view]
PfamiPF01967. MoaC. 1 hit.
PF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55040. SSF55040. 1 hit.
TIGRFAMsiTIGR02666. moaA. 1 hit.
TIGR00581. moaC. 1 hit.
PROSITEiPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 99-636 (ISOFORM MOCS1A), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-636 (ISOFORM MOCS1B).
    Strain: FVB/N.
    Tissue: Brain and Liver.
  3. "Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic MOCS1A and MOCS1B open reading frames."
    Gray T.A., Nicholls R.D.
    RNA 6:928-936(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-636 (ISOFORM MOCS1A), NUCLEOTIDE SEQUENCE [MRNA] OF 388-594 (ISOFORM MOCS1B).
  4. "Molybdenum cofactor-deficient mice resemble the phenotype of human patients."
    Lee H.-J., Adham I.M., Schwarz G., Kneussel M., Sass J.O., Engel W., Reiss J.
    Hum. Mol. Genet. 11:3309-3317(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "The pathogenesis of molybdenum cofactor deficiency, its delay by maternal clearance, and its expression pattern in microarray analysis."
    Reiss J., Bonin M., Schwegler H., Sass J.O., Garattini E., Wagner S., Lee H.-J., Engel W., Riess O., Schwarz G.
    Mol. Genet. Metab. 85:12-20(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  6. "Long-term rescue of a lethal inherited disease by adeno-associated virus-mediated gene transfer in a mouse model of molybdenum-cofactor deficiency."
    Kuegler S., Hahnewald R., Garrido M., Reiss J.
    Am. J. Hum. Genet. 80:291-297(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Spleen and Testis.
  8. "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-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMOCS1_MOUSE
AccessioniPrimary (citable) accession number: Q5RKZ7
Secondary accession number(s): B2RVW8
, B7ZWI5, Q8R058, Q9JL32, Q9JL33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 14, 2009
Last modified: July 6, 2016
This is version 96 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.