MOC2B_MOUSE
ID MOC2B_MOUSE Reviewed; 189 AA.
AC Q9Z223; Q8C5E5; Q8R1M7; Q9DCK1;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Molybdopterin synthase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE EC=2.8.1.12 {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2 large subunit {ECO:0000255|HAMAP-Rule:MF_03052};
DE AltName: Full=Molybdenum cofactor synthesis protein 2B {ECO:0000255|HAMAP-Rule:MF_03052};
DE Short=MOCS2B {ECO:0000255|HAMAP-Rule:MF_03052};
GN Name=Mocs2 {ECO:0000255|HAMAP-Rule:MF_03052};
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
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: Catalytic subunit of the molybdopterin synthase complex, a
CC complex that catalyzes the conversion of precursor Z into
CC molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms
CC from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene
CC group. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2
CC [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly +
CC 4 H(+) + molybdopterin; Xref=Rhea:RHEA:26333, Rhea:RHEA-COMP:12160,
CC Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58698, ChEBI:CHEBI:59648, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03052};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBUNIT: Heterotetramer; composed of 2 small (MOCS2A) and 2 large
CC (MOCS2B) subunits. {ECO:0000255|HAMAP-Rule:MF_03052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC Rule:MF_03052}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Z223-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z223-1; Sequence=VSP_010081, VSP_010082;
CC Name=3;
CC IsoId=Q9Z223-3; Sequence=VSP_036808;
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the small subunit (MOCS2A) from an overlapping reading
CC frame.
CC -!- SIMILARITY: Belongs to the MoaE family. MOCS2B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03052}.
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DR EMBL; AF091872; AAD14601.1; -; mRNA.
DR EMBL; AK002719; BAB22306.1; -; mRNA.
DR EMBL; AK010112; BAB26707.2; -; mRNA.
DR EMBL; AK078782; BAC37393.1; -; mRNA.
DR EMBL; CH466568; EDL18371.1; -; Genomic_DNA.
DR EMBL; CH466568; EDL18372.1; -; Genomic_DNA.
DR EMBL; BC024371; AAH24371.1; -; mRNA.
DR CCDS; CCDS49371.1; -. [Q9Z223-2]
DR RefSeq; NP_001106845.1; NM_001113374.1.
DR RefSeq; NP_038854.2; NM_013826.3.
DR AlphaFoldDB; Q9Z223; -.
DR SMR; Q9Z223; -.
DR MINT; Q9Z223; -.
DR STRING; 10090.ENSMUSP00000125797; -.
DR iPTMnet; Q9Z223; -.
DR PhosphoSitePlus; Q9Z223; -.
DR EPD; Q9Z223; -.
DR MaxQB; Q9Z223; -.
DR PaxDb; Q9Z223; -.
DR PeptideAtlas; Q9Z223; -.
DR PRIDE; Q9Z223; -.
DR ProteomicsDB; 252586; -. [Q9Z223-2]
DR ProteomicsDB; 252587; -. [Q9Z223-1]
DR ProteomicsDB; 252588; -. [Q9Z223-3]
DR DNASU; 17434; -.
DR GeneID; 17434; -.
DR KEGG; mmu:17434; -.
DR UCSC; uc007rxv.2; mouse. [Q9Z223-2]
DR CTD; 4338; -.
DR MGI; MGI:1336894; Mocs2.
DR eggNOG; KOG3307; Eukaryota.
DR InParanoid; Q9Z223; -.
DR OrthoDB; 1419096at2759; -.
DR TreeFam; TF314334; -.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 17434; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Mocs2; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z223; protein.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019008; C:molybdopterin synthase complex; ISO:MGI.
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:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR CDD; cd00756; MoaE; 1.
DR Gene3D; 3.90.1170.40; -; 1.
DR HAMAP; MF_03052; MOC2B; 1.
DR InterPro; IPR036563; MoaE_sf.
DR InterPro; IPR028888; MOCS2B_euk.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR Pfam; PF02391; MoaE; 1.
DR SUPFAM; SSF54690; SSF54690; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Molybdenum cofactor biosynthesis;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..189
FT /note="Molybdopterin synthase catalytic subunit"
FT /id="PRO_0000163112"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT BINDING 166..168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03052"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96007"
FT VAR_SEQ 127..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036808"
FT VAR_SEQ 168..170
FT /note="EIY -> GLT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10053003"
FT /id="VSP_010081"
FT VAR_SEQ 171..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10053003"
FT /id="VSP_010082"
FT CONFLICT 15
FT /note="T -> M (in Ref. 1; AAD14601 and 2; BAB22306/
FT BAB26707/BAC37393)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="S -> L (in Ref. 1; AAD14601 and 2; BAB22306/
FT BAB26707/BAC37393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 20924 MW; E16ACB553F92E3BF CRC64;
MSSLEISNSC FSPETRSPSS RQSVEDNASE PSGKDVDDVQ EKPKDIIQFT AEKLSVGEVS
QLVVSPLCGA VSLFVGTTRN NFEGKKVISL EYEAYVPMAE NEIRKICNDI RQKWPVRHIA
VFHRLGLVPV SEASTVIAVS SAHRAASLEA VSYAIDSLKA KVPIWKKEIY EESTSSWKRN
KECFWAAGD
