CIN_DROME
ID CIN_DROME Reviewed; 601 AA.
AC P39205; Q0KHX9; Q9U1M0; Q9V3E2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Molybdenum cofactor synthesis protein cinnamon;
DE Includes:
DE RecName: Full=Molybdopterin adenylyltransferase;
DE Short=MPT adenylyltransferase;
DE EC=2.7.7.75;
DE AltName: Full=Domain G;
DE Includes:
DE RecName: Full=Molybdopterin molybdenumtransferase;
DE Short=MPT Mo-transferase;
DE EC=2.10.1.1;
DE AltName: Full=Domain E;
GN Name=cin; ORFNames=CG2945;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8088525; DOI=10.1093/genetics/137.3.791;
RA Kamdar K.P., Shelton M.E., Finnerty V.;
RT "The Drosophila molybdenum cofactor gene cinnamon is homologous to three
RT Escherichia coli cofactor proteins and to the rat protein gephyrin.";
RL Genetics 137:791-801(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=10394904; DOI=10.1007/s004380050010;
RA Wittle A.E., Kamdar K.P., Finnerty V.;
RT "The Drosophila cinnamon gene is functionally homologous to Arabidopsis
RT cnx1 and has a similar expression pattern to the mammalian gephyrin gene.";
RL Mol. Gen. Genet. 261:672-680(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum
CC cofactor. In the first step, molybdopterin is adenylated. Subsequently,
CC molybdate is inserted into adenylated molybdopterin and AMP is
CC released. {ECO:0000269|PubMed:10394904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + molybdopterin = adenylyl-molybdopterin +
CC diphosphate; Xref=Rhea:RHEA:31331, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58698,
CC ChEBI:CHEBI:62727; EC=2.7.7.75;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-
CC molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727,
CC ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- DEVELOPMENTAL STAGE: Detected primarily in the epidermal cells of the
CC segmental grooves during germ-band retraction (7-9 hours after egg
CC laying). {ECO:0000269|PubMed:10394904}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000305}.
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DR EMBL; L19876; AAA65877.1; -; mRNA.
DR EMBL; AE014298; AAN09010.1; -; Genomic_DNA.
DR EMBL; AL050231; CAB65851.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL050231; CAB65852.1; -; Genomic_DNA.
DR EMBL; AY069078; AAL39223.1; -; mRNA.
DR PIR; S47896; S47896.
DR RefSeq; NP_477030.1; NM_057682.4.
DR RefSeq; NP_726659.1; NM_166835.4.
DR AlphaFoldDB; P39205; -.
DR SMR; P39205; -.
DR BioGRID; 57547; 2.
DR STRING; 7227.FBpp0070063; -.
DR iPTMnet; P39205; -.
DR PaxDb; P39205; -.
DR PRIDE; P39205; -.
DR EnsemblMetazoa; FBtr0070064; FBpp0070063; FBgn0000316.
DR EnsemblMetazoa; FBtr0070065; FBpp0070064; FBgn0000316.
DR GeneID; 30973; -.
DR KEGG; dme:Dmel_CG2945; -.
DR UCSC; CG2945-RA; d. melanogaster.
DR CTD; 30973; -.
DR FlyBase; FBgn0000316; cin.
DR VEuPathDB; VectorBase:FBgn0000316; -.
DR eggNOG; KOG2371; Eukaryota.
DR GeneTree; ENSGT00390000016577; -.
DR HOGENOM; CLU_010186_2_2_1; -.
DR InParanoid; P39205; -.
DR OMA; PLLDKEC; -.
DR OrthoDB; 1114121at2759; -.
DR PhylomeDB; P39205; -.
DR Reactome; R-DME-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 30973; 0 hits in 1 CRISPR screen.
DR ChiTaRS; cin; fly.
DR GenomeRNAi; 30973; -.
DR PRO; PR:P39205; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000316; Expressed in ovary and 11 other tissues.
DR ExpressionAtlas; P39205; baseline and differential.
DR Genevisible; P39205; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; ISS:FlyBase.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IBA:GO_Central.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IBA:GO_Central.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IBA:GO_Central.
DR GO; GO:0072579; P:glycine receptor clustering; IBA:GO_Central.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR GO; GO:0018315; P:molybdenum incorporation into molybdenum-molybdopterin complex; IBA:GO_Central.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:FlyBase.
DR GO; GO:0098970; P:postsynaptic neurotransmitter receptor diffusion trapping; IBA:GO_Central.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 2.40.340.10; -; 1.
DR Gene3D; 3.40.980.10; -; 2.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR PANTHER; PTHR10192; PTHR10192; 2.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF53218; SSF53218; 2.
DR SUPFAM; SSF63867; SSF63867; 1.
DR SUPFAM; SSF63882; SSF63882; 1.
DR TIGRFAMs; TIGR00177; molyb_syn; 2.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Magnesium; Metal-binding; Molybdenum;
KW Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..601
FT /note="Molybdenum cofactor synthesis protein cinnamon"
FT /id="PRO_0000170962"
FT REGION 3..153
FT /note="MPT adenylyltransferase"
FT REGION 173..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..596
FT /note="MPT Mo-transferase"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 414
FT /note="S -> T (in Ref. 1; AAA65877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65733 MW; DFA6926E955BF287 CRC64;
MESITFGVLT ISDTCWQEPE KDTSGPILRQ LIGETFANTQ VIGNIVPDEK DIIQQELRKW
IDREELRVIL TTGGTGFAPR DVTPEATRQL LEKECPQLSM YITLESIKQT QYAALSRGLC
GIAGNTLILN LPGSEKAVKE CFQTISALLP HAVHLIGDDV SLVRKTHAEV QGSAQKSHIC
PHKTGTGTDS DRNSPYPMLP VQEVLSIIFN TVQKTANLNK ILLEMNAPVN IPPFRASIKD
GYAMKSTGFS GTKRVLGCIA AGDSPNSLPL AEDECYKINT GAPLPLEADC VVQVEDTKLL
QLDKNGQESL VDILVEPQAG LDVRPVGYDL STNDRIFPAL DPSPVVVKSL LASVGNRLIL
SKPKVAIVST GSELCSPRNQ LTPGKIFDSN TTMLTELLVY FGFNCMHTCV LSDSFQRTKE
SLLELFEVVD FVICSGGVSM GDKDFVKSVL EDLQFRIHCG RVNIKPGKPM TFASRKDKYF
FGLPGNPVSA FVTFHLFALP AIRFAAGWDR CKCSLSVLNV KLLNDFSLDS RPEFVRASVI
SKSGELYASV NGNQISSRLQ SIVGADVLIN LPARTSDRPL AKAGEIFPAS VLRFDFISKY
E
