CSUP_DROME
ID CSUP_DROME Reviewed; 449 AA.
AC Q9V3A4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein catecholamines up;
GN Name=Catsup; ORFNames=CG10449;
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=10471719; DOI=10.1093/genetics/153.1.361;
RA Stathakis D.G., Burton D.Y., McIvor W.E., Krishnakumar S., Wright T.R.,
RA O'Donnell J.M.;
RT "The catecholamines up (Catsup) protein of Drosophila melanogaster
RT functions as a negative regulator of tyrosine hydroxylase activity.";
RL Genetics 153:361-382(1999).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
CC -!- FUNCTION: Negatively regulates tyrosine hydroxylase activity.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC KE4/Catsup subfamily. {ECO:0000305}.
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DR EMBL; AF216584; AAF37226.1; -; mRNA.
DR EMBL; AE014134; AAF53744.1; -; Genomic_DNA.
DR EMBL; AY058528; AAL13757.1; -; mRNA.
DR RefSeq; NP_524931.1; NM_080192.3.
DR AlphaFoldDB; Q9V3A4; -.
DR SMR; Q9V3A4; -.
DR BioGRID; 71703; 10.
DR DIP; DIP-18253N; -.
DR IntAct; Q9V3A4; 10.
DR STRING; 7227.FBpp0080687; -.
DR GlyGen; Q9V3A4; 1 site.
DR PaxDb; Q9V3A4; -.
DR PRIDE; Q9V3A4; -.
DR DNASU; 48805; -.
DR EnsemblMetazoa; FBtr0081143; FBpp0080687; FBgn0002022.
DR GeneID; 48805; -.
DR KEGG; dme:Dmel_CG10449; -.
DR CTD; 48805; -.
DR FlyBase; FBgn0002022; Catsup.
DR VEuPathDB; VectorBase:FBgn0002022; -.
DR eggNOG; KOG2693; Eukaryota.
DR GeneTree; ENSGT00940000160076; -.
DR HOGENOM; CLU_015114_0_1_1; -.
DR InParanoid; Q9V3A4; -.
DR OMA; IWLHSIG; -.
DR OrthoDB; 657777at2759; -.
DR PhylomeDB; Q9V3A4; -.
DR Reactome; R-DME-442380; Zinc influx into cells by the SLC39 gene family.
DR BioGRID-ORCS; 48805; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Catsup; fly.
DR GenomeRNAi; 48805; -.
DR PRO; PR:Q9V3A4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002022; Expressed in wing disc and 40 other tissues.
DR ExpressionAtlas; Q9V3A4; baseline and differential.
DR Genevisible; Q9V3A4; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0030234; F:enzyme regulator activity; IMP:FlyBase.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0010312; P:detoxification of zinc ion; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; HMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0042069; P:regulation of catecholamine metabolic process; IMP:FlyBase.
DR GO; GO:2000274; P:regulation of epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR003689; ZIP.
DR Pfam; PF02535; Zip; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..449
FT /note="Protein catecholamines up"
FT /id="PRO_0000213693"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 57..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 48658 MW; F7111A254C07AB4C CRC64;
MAKQVADYQC SKLQLYQKLA LVVILGAVLF SLPALCAGQG NPSFKYSREA NENFDPQKAP
RAEHHHHHDH DHDHGHHHHG HDHDHDHDHG HDHGHHHHGH DHDHDHDHGH HHHGHDERHT
KAKPDLDMST IWLHSIGSTL LISAAPFVLL YIIPLDNSEA MKPRLKVLLA FASGGLLGDA
FLHLIPHATH PHSHGEHGHD HGHDHHHHHD GEEHEHGHSH DMSIGLWVLG GIIAFLSVEK
LVRILKGGHG GHGHSHGAPK PKPVPAKKKS SDKEDSGDGD KPAKPAKIKS KKPEAEPEGE
VEISGYLNLA ADFAHNFTDG LAIGASYLAG NSIGIVTTIT ILLHEVPHEI GDFAILIKSG
CSRRKAMLLQ LVTALGALAG TALALLGAGG GDGSAPWVLP FTAGGFIYIA TVSVLPELLE
ESTKLKQSLK EIFALLTGVA LMIVIAKFE
