AB19G_ARATH
ID AB19G_ARATH Reviewed; 725 AA.
AC Q9M3D6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ABC transporter G family member 19;
DE Short=ABC transporter ABCG.19;
DE Short=AtABCG19;
DE AltName: Full=White-brown complex homolog protein 19;
DE Short=AtWBC19;
GN Name=ABCG19; Synonyms=WBC19; OrderedLocusNames=At3g55130;
GN ORFNames=T26I12.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11346655; DOI=10.1074/jbc.m103104200;
RA Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A.;
RT "The Arabidopsis thaliana ABC protein superfamily, a complete inventory.";
RL J. Biol. Chem. 276:30231-30244(2001).
RN [5]
RP FUNCTION, BIOTECHNOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=16116418; DOI=10.1038/nbt1134;
RA Mentewab A., Stewart C.N. Jr.;
RT "Overexpression of an Arabidopsis thaliana ABC transporter confers
RT kanamycin resistance to transgenic plants.";
RL Nat. Biotechnol. 23:1177-1180(2005).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18299247; DOI=10.1016/j.tplants.2008.02.001;
RA Verrier P.J., Bird D., Burla B., Dassa E., Forestier C., Geisler M.,
RA Klein M., Kolukisaoglu H.U., Lee Y., Martinoia E., Murphy A., Rea P.A.,
RA Samuels L., Schulz B., Spalding E.J., Yazaki K., Theodoulou F.L.;
RT "Plant ABC proteins - a unified nomenclature and updated inventory.";
RL Trends Plant Sci. 13:151-159(2008).
CC -!- FUNCTION: Confers selective resistance to kanamycin.
CC {ECO:0000269|PubMed:16116418}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16116418};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16116418}.
CC -!- BIOTECHNOLOGY: WBC19 may be a good alternative as a selective marker of
CC transgenic plants to avoid the use of bacterial antibiotic resistance
CC protein (such as neo/nptII). {ECO:0000269|PubMed:16116418}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; AL132954; CAB75747.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79343.1; -; Genomic_DNA.
DR EMBL; AY045932; AAK76606.1; -; mRNA.
DR EMBL; AY079387; AAL85118.1; -; mRNA.
DR PIR; T47652; T47652.
DR RefSeq; NP_191073.1; NM_115371.3.
DR AlphaFoldDB; Q9M3D6; -.
DR SMR; Q9M3D6; -.
DR BioGRID; 9995; 7.
DR IntAct; Q9M3D6; 6.
DR STRING; 3702.AT3G55130.1; -.
DR TCDB; 3.A.1.204.27; the atp-binding cassette (abc) superfamily.
DR PaxDb; Q9M3D6; -.
DR PRIDE; Q9M3D6; -.
DR ProteomicsDB; 245141; -.
DR EnsemblPlants; AT3G55130.1; AT3G55130.1; AT3G55130.
DR GeneID; 824679; -.
DR Gramene; AT3G55130.1; AT3G55130.1; AT3G55130.
DR KEGG; ath:AT3G55130; -.
DR Araport; AT3G55130; -.
DR TAIR; locus:2100641; AT3G55130.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_8_1; -.
DR InParanoid; Q9M3D6; -.
DR OMA; KDCDSFR; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q9M3D6; -.
DR PRO; PR:Q9M3D6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3D6; baseline and differential.
DR Genevisible; Q9M3D6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005775; C:vacuolar lumen; IDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007034; P:vacuolar transport; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..725
FT /note="ABC transporter G family member 19"
FT /id="PRO_0000240691"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 73..325
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 419..629
FT /note="ABC transmembrane type-2"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 725 AA; 80657 MW; 790C535A7929CC16 CRC64;
MNLSLSGRKI AMTRVSAETQ YITPIGSPTL DELLKDCDSF RKGDSGDGVK SDDPAHHIID
VEALYVKPVP YVLNFNNLQY DVTLRRRFGF SRQNGVKTLL DDVSGEASDG DILAVLGASG
AGKSTLIDAL AGRVAEGSLR GSVTLNGEKV LQSRLLKVIS AYVMQDDLLF PMLTVKETLM
FASEFRLPRS LSKSKKMERV EALIDQLGLR NAANTVIGDE GHRGVSGGER RRVSIGIDII
HDPIVLFLDE PTSGLDSTNA FMVVQVLKRI AQSGSIVIMS IHQPSARIVE LLDRLIILSR
GKSVFNGSPA SLPGFFSDFG RPIPEKENIS EFALDLVREL EGSNEGTKAL VDFNEKWQQN
KISLIQSAPQ TNKLDQDRSL SLKEAINASV SRGKLVSGSS RSNPTSMETV SSYANPSLFE
TFILAKRYMK NWIRMPELVG TRIATVMVTG CLLATVYWKL DHTPRGAQER LTLFAFVVPT
MFYCCLDNVP VFIQERYIFL RETTHNAYRT SSYVISHSLV SLPQLLAPSL VFSAITFWTV
GLSGGLEGFV FYCLLIYASF WSGSSVVTFI SGVVPNIMLC YMVSITYLAY CLLLSGFYVN
RDRIPFYWTW FHYISILKYP YEAVLINEFD DPSRCFVRGV QVFDSTLLGG VSDSGKVKLL
ETLSKSLRTK ITESTCLRTG SDLLAQQGIT QLSKWDCLWI TFASGLFFRI LFYFALLFGS
RNKRT