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UEX_DROME
ID   UEX_DROME               Reviewed;         834 AA.
AC   A0A0B7P9G0;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Unextended protein {ECO:0000312|FlyBase:FBgn0262124};
DE   AltName: Full=Putative metal transporter uex {ECO:0000305};
DE   Flags: Precursor;
GN   Name=uex {ECO:0000312|FlyBase:FBgn0262124};
GN   Synonyms=41Ad {ECO:0000312|FlyBase:FBgn0262124},
GN   GroupIII {ECO:0000312|FlyBase:FBgn0262124},
GN   l(2)41Ad {ECO:0000312|FlyBase:FBgn0262124};
GN   ORFNames=CG42595 {ECO:0000312|FlyBase:FBgn0262124};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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   [3] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH PRL-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31404830; DOI=10.1016/j.isci.2019.07.026;
RA   Guo P., Xu X., Wang F., Yuan X., Tu Y., Zhang B., Zheng H., Yu D., Ge W.,
RA   Gong Z., Yang X., Xi Y.;
RT   "A Novel Neuroprotective Role of Phosphatase of Regenerating Liver-1
RT   against CO2 Stimulation in Drosophila.";
RL   IScience 19:291-302(2019).
CC   -!- FUNCTION: Probable metal transporter (By similarity). Acts downstream
CC       of PRL-1 and protects the nervous system against olfactory carbon
CC       dioxide stimulation (PubMed:31404830). {ECO:0000250|UniProtKB:Q3TWN3,
CC       ECO:0000269|PubMed:31404830}.
CC   -!- SUBUNIT: Interacts with PRL-1, possibly at the plasma membrane.
CC       {ECO:0000269|PubMed:31404830}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31404830};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the nervous system
CC       results in a held-up wing phenotype after eclosion and upon carbon
CC       dioxide stimulation. {ECO:0000269|PubMed:31404830}.
CC   -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
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DR   EMBL; AE013599; AIG63332.1; -; Genomic_DNA.
DR   EMBL; AE013599; EDP28148.2; -; Genomic_DNA.
DR   EMBL; AE013599; EDP28149.2; -; Genomic_DNA.
DR   EMBL; AE013599; ELP57407.1; -; Genomic_DNA.
DR   RefSeq; NP_001104390.2; NM_001110920.4.
DR   RefSeq; NP_001104391.2; NM_001110921.4.
DR   RefSeq; NP_001263162.1; NM_001276233.2.
DR   RefSeq; NP_001288144.1; NM_001301215.1.
DR   AlphaFoldDB; A0A0B7P9G0; -.
DR   SMR; A0A0B7P9G0; -.
DR   STRING; 7227.FBpp0291436; -.
DR   GlyGen; A0A0B7P9G0; 7 sites.
DR   PaxDb; A0A0B7P9G0; -.
DR   EnsemblMetazoa; FBtr0302226; FBpp0291436; FBgn0262124.
DR   EnsemblMetazoa; FBtr0302227; FBpp0291437; FBgn0262124.
DR   EnsemblMetazoa; FBtr0334938; FBpp0306957; FBgn0262124.
DR   EnsemblMetazoa; FBtr0346683; FBpp0312292; FBgn0262124.
DR   GeneID; 5740320; -.
DR   KEGG; dme:Dmel_CG42595; -.
DR   CTD; 5740320; -.
DR   FlyBase; FBgn0262124; uex.
DR   VEuPathDB; VectorBase:FBgn0262124; -.
DR   eggNOG; KOG2118; Eukaryota.
DR   GeneTree; ENSGT00940000169533; -.
DR   OMA; DFTIFAE; -.
DR   OrthoDB; 1446644at2759; -.
DR   PhylomeDB; A0A0B7P9G0; -.
DR   BioGRID-ORCS; 5740320; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; uex; fly.
DR   GenomeRNAi; 5740320; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0262124; Expressed in midgut and 12 other tissues.
DR   ExpressionAtlas; A0A0B7P9G0; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0006873; P:cellular ion homeostasis; ISS:FlyBase.
DR   GO; GO:0071244; P:cellular response to carbon dioxide; IGI:UniProtKB.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR045095; ACDP.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR002550; CNNM.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR12064; PTHR12064; 1.
DR   Pfam; PF01595; DUF21; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS51846; CNNM; 1.
PE   1: Evidence at protein level;
KW   CBS domain; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..834
FT                   /note="Unextended protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5015035038"
FT   TOPO_DOM        21..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..834
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          182..361
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT   DOMAIN          380..441
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          448..515
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          739..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         604..656
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        743
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        751
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   834 AA;  93283 MW;  6EAFD9A83D4E3E41 CRC64;
     MNTYFISFIT IIIFANGING TSVDTSNKLL LQKANDFNLS QNLSSSRTRR TIANSFRIVG
     IRLEDETVET KNGIPTVLVD KEQQFRVFGS GLEENTAITF TNEKNDYGGP CLKPATDLFT
     PIEVSSNGFS ALYSVKFPSF INEFFICAKT AEKTTNHSKA ATTTPLEHQG NSDFLKIKTF
     EPLIPVWLAI IIIVTCLGFS ALFSGLNLGL MSMDRTELKI LRNTGTEKEK KYASKIAPVR
     DQGNYLLCSI LLGNVLVNST FTILLDGLTS GLFAVIFSTL AIVLFGEITP QAVCSRHGLA
     IGAKTILVTK TVMAITAPLS YPVSRILDKL LGEEIGNVYN RERLKELVRV TNDVNDLDKN
     EVNIISGALE LRKKTVADVM THINDAFMLS LDALLDFETV SEIMNSGYSR IPVYDGDRKN
     IVTLLYIKDL AFVDTDDNTP LKTLCEFYQN PVHFVFEDYT LDIMFNQFKE GTIGHIAFVH
     RVNNEGDGDP FYETVGLVTL EDVIEELIQA EIVDETDVFV DNRTKTRRNR YKKADFSAFA
     ERREVQTVRI SPQLTLATFQ YLSTAVDAFK KDVISELILR RLLNQDVFHN IKTKGKSKDD
     PSLYIFTQGK AVDFFVLILE GRVEVTIGKE ALMFESGPFT YFGTQALVPN VVIDSPTQMG
     SLQSLNMDSK IRQSFVPDYS VRAISDVIYI TIKRVLYLTA KKATLLEKSR KSGTFSSETF
     DDEVERLLHS ITENEKPSCF AQNQSTRRLS NRSINSSPTN MNRSPDFVYN SVDEAIQDDT
     KLKNIKHADN VTTSISLVAA ELEDLHSGEQ DTTAASMPLL PKLDDKFESK QSKP
 
 
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