MOC2A_MOUSE
ID MOC2A_MOUSE Reviewed; 88 AA.
AC Q9Z224; Q9D6Q0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Molybdopterin synthase sulfur carrier subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 small subunit {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Molybdenum cofactor synthesis protein 2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE Short=MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
DE AltName: Full=Sulfur carrier protein MOCS2A {ECO:0000255|HAMAP-Rule:MF_03051};
GN Name=Mocs2 {ECO:0000255|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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10053003; DOI=10.1086/302295;
RA Stallmeyer B., Drugeon G., Reiss J., Haenni A.L., Mendel R.R.;
RT "Human molybdopterin synthase gene: identification of a bicistronic
RT transcript with overlapping reading frames.";
RL Am. J. Hum. Genet. 64:698-705(1999).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Testis;
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).
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:0000255|HAMAP-Rule:MF_03051}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03051}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|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:0000255|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.
CC -!- SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03051}.
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DR EMBL; AF091872; AAD14600.1; -; mRNA.
DR CCDS; CCDS49369.1; -.
DR AlphaFoldDB; Q9Z224; -.
DR SMR; Q9Z224; -.
DR EPD; Q9Z224; -.
DR MaxQB; Q9Z224; -.
DR PRIDE; Q9Z224; -.
DR ProteomicsDB; 291378; -.
DR MGI; MGI:1336894; Mocs2.
DR UniPathway; UPA00344; -.
DR ChiTaRS; Mocs2; mouse.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019008; C:molybdopterin synthase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0030366; F:molybdopterin synthase activity; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
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 PANTHER; PTHR33359; PTHR33359; 1.
DR Pfam; PF02597; ThiS; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..88
FT /note="Molybdopterin synthase sulfur carrier subunit"
FT /id="PRO_0000209135"
FT MOD_RES 88
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
FT MOD_RES 88
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03051"
SQ SEQUENCE 88 AA; 9745 MW; 5F422EE81E7EA81E CRC64;
MVPRCQIDVL YFAKSAEIAG VRSETISVPQ EIKASELWKE LEMLHPGLAD VRNQVIFAVR
QEYVELGDQQ LLLQPGDEVA IIPPISGG
