BALAT_DROME
ID BALAT_DROME Reviewed; 604 AA.
AC Q961J5; Q9V6H5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Beta-alanine transporter {ECO:0000303|PubMed:28806173, ECO:0000312|FlyBase:FBgn0033778};
DE Short=BalaT {ECO:0000303|PubMed:28806173, ECO:0000312|FlyBase:FBgn0033778};
GN Name=Balat {ECO:0000303|PubMed:28806173, ECO:0000312|FlyBase:FBgn0033778};
GN ORFNames=CG3790 {ECO:0000312|FlyBase:FBgn0033778};
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:0000312|EMBL:AAK92979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK92979.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAK92979.1};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=28806173; DOI=10.7554/elife.29146;
RA Han Y., Xiong L., Xu Y., Tian T., Wang T.;
RT "The beta-alanine transporter BalaT is required for visual
RT neurotransmission in Drosophila.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Beta-alanine transporter required for the uptake of beta-
CC alanine by the glia (PubMed:28806173). Required for the recycling
CC process of the neurotransmitter histamine in photoreceptor neurons of
CC the compound eye and therefore for photoreceptor synaptic transmission
CC (PubMed:28806173). Following histamine release from photoreceptors and
CC its uptake by glia, histamine is conjugated to beta-alanine by e/Ebony
CC to form the inactive metabolite, carcinine (PubMed:28806173).
CC {ECO:0000269|PubMed:28806173}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28806173};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the head and predominantly in the
CC retinal pigment cells of the compound eye.
CC {ECO:0000269|PubMed:28806173}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58448.2; -; Genomic_DNA.
DR EMBL; AY051555; AAK92979.1; -; mRNA.
DR RefSeq; NP_610823.1; NM_136979.3.
DR AlphaFoldDB; Q961J5; -.
DR SMR; Q961J5; -.
DR IntAct; Q961J5; 1.
DR STRING; 7227.FBpp0086928; -.
DR GlyGen; Q961J5; 2 sites.
DR PaxDb; Q961J5; -.
DR PRIDE; Q961J5; -.
DR DNASU; 36417; -.
DR EnsemblMetazoa; FBtr0087815; FBpp0086928; FBgn0033778.
DR GeneID; 36417; -.
DR KEGG; dme:Dmel_CG3790; -.
DR UCSC; CG3790-RA; d. melanogaster.
DR CTD; 36417; -.
DR FlyBase; FBgn0033778; Balat.
DR VEuPathDB; VectorBase:FBgn0033778; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000173250; -.
DR HOGENOM; CLU_001265_33_4_1; -.
DR InParanoid; Q961J5; -.
DR OMA; PFIICME; -.
DR OrthoDB; 655566at2759; -.
DR PhylomeDB; Q961J5; -.
DR Reactome; R-DME-112311; Neurotransmitter clearance.
DR Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-DME-197264; Nicotinamide salvaging.
DR Reactome; R-DME-200425; Carnitine metabolism.
DR Reactome; R-DME-2161517; Abacavir transmembrane transport.
DR Reactome; R-DME-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-DME-549127; Organic cation transport.
DR Reactome; R-DME-561048; Organic anion transport.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR BioGRID-ORCS; 36417; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36417; -.
DR PRO; PR:Q961J5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033778; Expressed in head capsule and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0001761; F:beta-alanine transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0001762; P:beta-alanine transport; IDA:FlyBase.
DR GO; GO:0001694; P:histamine biosynthetic process; IDA:FlyBase.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..604
FT /note="Beta-alanine transporter"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447217"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 24..44
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..151
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..212
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..264
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..268
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 363..383
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..390
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 391..411
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 419..439
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..442
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 443..463
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 474..494
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..501
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 502..522
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 604 AA; 67905 MW; 307DD2D9AD635D82 CRC64;
MDFDEVLREV GSFGLYQKVI ICSVLLPAAL PCAFHAYSQL FIAATPQHFC RVPELEPWTQ
DYVQLVKNLS IPRNRNGAYA ECSMYSRNYT DIVRYLEYRP PPDLLRQQAE DLLKLQPDTT
QVVPCQHGWH YDKSIYSSTV VQEWNLVCDR SFLVTLALVV FGVGGLLGNY VFGYLVDLWG
RRPSFYAYLL LEIIACAASA FAWNYYTWLG LRFVVGLTVP AILASPYVLA IELVGPERRV
FCTIVSNIAY SLGLVVLAGV IYIVRDWREL SLAVSMPLLM LFSCFFVLPE SPRWLMAVGK
TRRAIKILKV MARVNGVRVN RDFVERLQRK LVITRAAETK SSMTTHYGIL DLFRGPNMRR
KTLIITLIWF ANTSVYVGLS YYAPALGGDE IWNFFLAGAV ELPTYLLLWP GLSYFGRRWI
LFISMLVGGV ACVATFLYPD ITLLLYCVGK MGISSSFVVL PLMASELYPT VVRGLGMSFS
SVISMVGPIV IPMINHMGQQ MLVLPLIVMG ALLILGGFAS LLLPETRNRN LPQTLEEGEA
VPLSFLLCCC VESERKPNNI RASPKKRILP EAGTPVFHRV DTPVSDRVPC KIVCSICKNE
MRTL
