P39205 (CIN_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Molybdenum cofactor synthesis protein cinnamon

Including the following 2 domains:

1. Molybdopterin adenylyltransferase
   Short name=MPT adenylyltransferase
   EC=2.7.7.75
   Alternative name(s):
   Domain G
2. Molybdopterin molybdenumtransferase
   Short name=MPT Mo-transferase
   EC=2.10.1.1
   Alternative name(s):
   Domain E

Gene names

Name:	cin
ORF Names:	CG2945

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	601 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Ref.3
Catalytic activity	ATP + molybdopterin = diphosphate + adenylyl-molybdopterin. Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.
Cofactor	Magnesium By similarity.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Developmental stage	Detected primarily in the epidermal cells of the segmental grooves during germ-band retraction (7-9 hours after egg laying). Ref.3
Sequence similarities	In the N-terminal section; belongs to the MoaB/Mog family. In the C-terminal section; belongs to the MoeA family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Molybdenum Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW embryonic development via the syncytial blastoderm Traceable author statement PubMed 3089870. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 601	601	Molybdenum cofactor synthesis protein cinnamon		PRO_0000170962
Regions
	Region	3 – 153	151	MPT adenylyltransferase
	Region	184 – 596	413	MPT Mo-transferase
Amino acid modifications
	Modified residue	376	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	414	1	S → T in AAA65877. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39205 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DFA6926E955BF287	FASTA	601	65,733
	10 20 30 40 50 60 MESITFGVLT ISDTCWQEPE KDTSGPILRQ LIGETFANTQ VIGNIVPDEK DIIQQELRKW 70 80 90 100 110 120 IDREELRVIL TTGGTGFAPR DVTPEATRQL LEKECPQLSM YITLESIKQT QYAALSRGLC 130 140 150 160 170 180 GIAGNTLILN LPGSEKAVKE CFQTISALLP HAVHLIGDDV SLVRKTHAEV QGSAQKSHIC 190 200 210 220 230 240 PHKTGTGTDS DRNSPYPMLP VQEVLSIIFN TVQKTANLNK ILLEMNAPVN IPPFRASIKD 250 260 270 280 290 300 GYAMKSTGFS GTKRVLGCIA AGDSPNSLPL AEDECYKINT GAPLPLEADC VVQVEDTKLL 310 320 330 340 350 360 QLDKNGQESL VDILVEPQAG LDVRPVGYDL STNDRIFPAL DPSPVVVKSL LASVGNRLIL 370 380 390 400 410 420 SKPKVAIVST GSELCSPRNQ LTPGKIFDSN TTMLTELLVY FGFNCMHTCV LSDSFQRTKE 430 440 450 460 470 480 SLLELFEVVD FVICSGGVSM GDKDFVKSVL EDLQFRIHCG RVNIKPGKPM TFASRKDKYF 490 500 510 520 530 540 FGLPGNPVSA FVTFHLFALP AIRFAAGWDR CKCSLSVLNV KLLNDFSLDS RPEFVRASVI 550 560 570 580 590 600 SKSGELYASV NGNQISSRLQ SIVGADVLIN LPARTSDRPL AKAGEIFPAS VLRFDFISKY E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin." Kamdar K.P., Shelton M.E., Finnerty V. Genetics 137:791-801(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"The Drosophila cinnamon gene is functionally homologous to Arabidopsis cnx1 and has a similar expression pattern to the mammalian gephyrin gene." Wittle A.E., Kamdar K.P., Finnerty V. Mol. Gen. Genet. 261:672-680(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE. Strain: Canton-S.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[6]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[7]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19876 mRNA. Translation: AAA65877.1. AE014298 Genomic DNA. Translation: AAN09010.1. AL050231 Genomic DNA. Translation: CAB65851.1. Sequence problems. AL050231 Genomic DNA. Translation: CAB65852.1. AY069078 mRNA. Translation: AAL39223.1.
PIR	S47896.
RefSeq	NP_477030.1. NM_057682.3. NP_726659.1. NM_166835.3.
UniGene	Dm.2294.
3D structure databases
ProteinModelPortal	P39205.
SMR	P39205. Positions 7-156, 198-592.
ModBase	Search...
Proteomic databases
PaxDb	P39205.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070064; FBpp0070063; FBgn0000316. FBtr0070065; FBpp0070064; FBgn0000316.
GeneID	30973.
KEGG	dme:Dmel_CG2945.
UCSC	CG2945-RA. d. melanogaster.
Organism-specific databases
CTD	30973.
FlyBase	FBgn0000316. cin.
Phylogenomic databases
eggNOG	COG0303.
GeneTree	ENSGT00390000016577.
HOGENOM	HOG000218563.
InParanoid	P39205.
KO	K15376.
OMA	KINTGAP.
OrthoDB	EOG4WM38S.
PhylomeDB	P39205.
Enzyme and pathway databases
UniPathway	UPA00344.
Gene expression databases
GermOnline	CG2945. Drosophila melanogaster.
Family and domain databases
Gene3D	2.40.340.10. 1 hit. 3.40.980.10. 2 hits.
InterPro	IPR020817. Mo_cofactor_synthesis. IPR008284. MoCF_biosynth_CS. IPR005111. MoeA_C_domain_IV. IPR005110. MoeA_linker/N. IPR001453. Mopterin-bd_dom. [Graphical view]
Pfam	PF00994. MoCF_biosynth. 2 hits. PF03454. MoeA_C. 1 hit. PF03453. MoeA_N. 1 hit. [Graphical view]
SMART	SM00852. MoCF_biosynth. 2 hits. [Graphical view]
SUPFAM	SSF53218. MoCF_biosynth. 2 hits. SSF63867. MoeA_C. 1 hit. SSF63882. MoeA_N. 1 hit.
TIGRFAMs	TIGR00177. molyb_syn. 2 hits.
PROSITE	PS01078. MOCF_BIOSYNTHESIS_1. 1 hit. PS01079. MOCF_BIOSYNTHESIS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	30973.
NextBio	771251.

Entry information

Entry name

CIN_DROME

Accession

Primary (citable) accession number: P39205
Secondary accession number(s): Q0KHX9, Q9U1M0, Q9V3E2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project