ID F6ZGI7_MOUSE Unreviewed; 88 AA.
AC F6ZGI7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000256|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000256|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000256|HAMAP-Rule:MF_03051};
DE Short=MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
DE AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000256|HAMAP-Rule:MF_03051};
GN Name=Mocs2 {ECO:0000313|Ensembl:ENSMUSP00000129021.2,
GN ECO:0000313|MGI:MGI:1336894};
GN Synonyms=MOCS2 {ECO:0000256|HAMAP-Rule:MF_03051};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000129021.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000129021.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129021.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000129021.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129021.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Acts as a sulfur carrier required for molybdopterin
CC biosynthesis. Component of the molybdopterin synthase complex that
CC catalyzes the conversion of precursor Z into molybdopterin by mediating
CC the incorporation of 2 sulfur atoms into precursor Z to generate a
CC dithiolene group. In the complex, serves as sulfur donor by being
CC thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction
CC with MOCS2B, the sulfur is then transferred to precursor Z to form
CC molybdopterin. {ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046, ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|HAMAP-
CC Rule:MF_03051}.
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-
CC adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then
CC thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC {ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the large subunit (MOCS2B) from an overlapping reading
CC frame. {ECO:0000256|HAMAP-Rule:MF_03051}.
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03051}.
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DR RefSeq; NP_038854.2; NM_013826.3.
DR ProteomicsDB; 334418; -.
DR Antibodypedia; 23330; 179 antibodies from 23 providers.
DR DNASU; 17434; -.
DR Ensembl; ENSMUST00000165022.9; ENSMUSP00000128965.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000166104.9; ENSMUSP00000129021.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000183407.2; ENSMUSP00000139011.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000184214.8; ENSMUSP00000139285.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000184245.8; ENSMUSP00000139355.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000184335.8; ENSMUSP00000139064.2; ENSMUSG00000015536.15.
DR Ensembl; ENSMUST00000184781.8; ENSMUSP00000138856.2; ENSMUSG00000015536.15.
DR GeneID; 17434; -.
DR UCSC; uc007rxu.2; mouse.
DR AGR; MGI:1336894; -.
DR CTD; 4338; -.
DR MGI; MGI:1336894; Mocs2.
DR VEuPathDB; HostDB:ENSMUSG00000015536; -.
DR GeneTree; ENSGT00510000047669; -.
DR HOGENOM; CLU_114601_4_3_1; -.
DR OrthoDB; 9021at2759; -.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 17434; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Mocs2; mouse.
DR Proteomes; UP000000589; Chromosome 13.
DR Bgee; ENSMUSG00000015536; Expressed in lens of camera-type eye and 253 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030366; F:molybdopterin synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00754; Ubl_MoaD; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03051; MOCS2A; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR044672; MOCS2A.
DR InterPro; IPR028887; MOCS2A_euk.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR NCBIfam; TIGR01682; moaD; 1.
DR PANTHER; PTHR33359; MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT; 1.
DR PANTHER; PTHR33359:SF1; MOLYBDOPTERIN SYNTHASE SULFUR CARRIER SUBUNIT; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03051};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_03051};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03051};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_03051};
KW Proteomics identification {ECO:0007829|EPD:F6ZGI7,
KW ECO:0007829|MaxQB:F6ZGI7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT MOD_RES 88
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
FT MOD_RES 88
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03051"
SQ SEQUENCE 88 AA; 9701 MW; 82E22EE81E66D1F9 CRC64;
MVPRCQIDVL YFAKSAEIAG VRSETISVPQ EIKASELWKE LESLHPGLAD VRNQVIFAVR
QEYVELGDQQ LLLQPGDEVA IIPPISGG
//
