ID A37C_DROME Reviewed; 504 AA.
AC P18487; O18376; O18377; O18378; O96568; Q95TY1; Q9VIZ7;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 3.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Protein anon-37Cs;
GN Name=anon-37Cs; Synonyms=cs, l(2)37Cs; ORFNames=CG10561;
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 [GENOMIC DNA].
RC STRAIN=St. Lucia;
RX PubMed=10231575; DOI=10.1016/s0378-1119(99)00096-7;
RA Tatarenkov A., Saez A.G., Ayala F.J.;
RT "A compact gene cluster in Drosophila: the unrelated Cs gene is compressed
RT between duplicated amd and Ddc.";
RL Gene 231:111-120(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3478553; DOI=10.1007/bf00329656;
RA Eveleth D.D., Marsh J.L.;
RT "Overlapping transcription units in Drosophila: sequence and structure of
RT the Cs gene.";
RL Mol. Gen. Genet. 209:290-298(1987).
RN [3]
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 [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 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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=2874495; DOI=10.1038/322279a0;
RA Spencer C.A., Gietz R.D., Hodgetts R.B.;
RT "Overlapping transcription units in the dopa decarboxylase region of
RT Drosophila.";
RL Nature 322:279-281(1986).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=3007242; DOI=10.1016/0012-1606(86)90402-1;
RA Spencer C.A., Gietz R.D., Hodgetts R.B.;
RT "Analysis of the transcription unit adjacent to the 3'-end of the dopa
RT decarboxylase gene in Drosophila melanogaster.";
RL Dev. Biol. 114:260-264(1986).
CC -!- FUNCTION: Has a non-vital function.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Low levels seen in adult heads, thorax, abdomen and
CC ovaries, high levels in testes. {ECO:0000269|PubMed:2874495}.
CC -!- DEVELOPMENTAL STAGE: Abundant in embryos and adults.
CC {ECO:0000269|PubMed:2874495, ECO:0000269|PubMed:3007242}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA29405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA29405.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA29406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA29406.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA29407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA29407.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA29408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA29408.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF091328; AAC67581.1; -; Genomic_DNA.
DR EMBL; X05991; CAA29405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05991; CAA29406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05991; CAA29407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X05991; CAA29408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014134; AAF53761.2; -; Genomic_DNA.
DR EMBL; AY058445; AAL13674.1; -; mRNA.
DR PIR; S01102; S01102.
DR PIR; S01103; S01103.
DR PIR; S01104; S01104.
DR PIR; S01105; S01105.
DR RefSeq; NP_476608.1; NM_057260.4.
DR AlphaFoldDB; P18487; -.
DR SMR; P18487; -.
DR BioGRID; 61174; 2.
DR DIP; DIP-18447N; -.
DR STRING; 7227.FBpp0080699; -.
DR PaxDb; 7227-FBpp0080699; -.
DR DNASU; 35189; -.
DR EnsemblMetazoa; FBtr0081155; FBpp0080699; FBgn0002036.
DR GeneID; 35189; -.
DR KEGG; dme:Dmel_CG10561; -.
DR AGR; FB:FBgn0002036; -.
DR FlyBase; FBgn0002036; CG10561.
DR VEuPathDB; VectorBase:FBgn0002036; -.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000174397; -.
DR HOGENOM; CLU_004498_2_3_1; -.
DR InParanoid; P18487; -.
DR OMA; HITSCPV; -.
DR OrthoDB; 2642916at2759; -.
DR PhylomeDB; P18487; -.
DR Reactome; R-DME-141334; PAOs oxidise polyamines to amines.
DR Reactome; R-DME-351200; Interconversion of polyamines.
DR BioGRID-ORCS; 35189; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35189; -.
DR PRO; PR:P18487; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002036; Expressed in testis and 26 other cell types or tissues.
DR ExpressionAtlas; P18487; baseline and differential.
DR Genevisible; P18487; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF416; SPERMINE OXIDASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..504
FT /note="Protein anon-37Cs"
FT /id="PRO_0000064404"
FT CONFLICT 53
FT /note="A -> S (in Ref. 5; AAL13674)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> R (in Ref. 1; AAC67581/CAA29408)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="G -> D (in Ref. 1; AAC67581)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="G -> S (in Ref. 1; AAC67581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56202 MW; 7C594AE7417A6687 CRC64;
MQCFKLASRR SLYNARVLQA DNIGDKQRSP DLEAARQNTQ IVVVGAGLAG LSAAQHLLSH
GFRRTVILEA TDRYGGRINT QRFGDTYCEL GAKWVKIDGS QDSMYELLRN TEGLGKQIKQ
PDRATYLQDG SRINPAMVEL IDTLFRQLCR GFKVSERVKT GGDLHSLDNV MNYFRTESDR
IIGVSFQHPK DQLAAREIFQ SLFKEFGSIL GCCLEYVNIE HITKCPVQQE QRPLYVPTGL
DNVVDDLIQN MDKAQLQTGK PVGQIQWTPA PMKSVGCLDG SLYNADHIIC TLPLGVLKSF
AGVLFRPTLP LDKMLAIRNL GFGNPLKIYL SYKKPIGRWL KGSLRPLGTL LNPSVEQQPE
RNWTQQVVEI SQVPSSQHVL EVHVGGGYYE EIEKLPDEEL LEQITGLLRR CVSSHLVPYP
QELLRSNWST SACYLGGRPY FSTNSSARDV QRLAAPLGEK SPGLLFAGDA TSLRGFGTID
AARSSGIREA QRIIDYYLKS VHCG
//
