ABCG1_PETHY
ID ABCG1_PETHY Reviewed; 633 AA.
AC H9BZ66;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=ABC transporter G family member 1 {ECO:0000303|PubMed:22345641};
DE Short=ABC transporter ABCG.1 {ECO:0000303|PubMed:22345641};
DE Short=PhABCG1 {ECO:0000303|PubMed:22345641};
GN Name=ABCG1 {ECO:0000303|PubMed:22345641};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION BY ODO1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Mitchell, and cv. R27;
RX PubMed=22345641; DOI=10.1093/jxb/ers034;
RA Van Moerkercke A., Galvan-Ampudia C.S., Verdonk J.C., Haring M.A.,
RA Schuurink R.C.;
RT "Regulators of floral fragrance production and their target genes in
RT petunia are not exclusively active in the epidermal cells of petals.";
RL J. Exp. Bot. 63:3157-3171(2012).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28663500; DOI=10.1126/science.aan0826;
RA Adebesin F., Widhalm J.R., Boachon B., Lefevre F., Pierman B., Lynch J.H.,
RA Alam I., Junqueira B., Benke R., Ray S., Porter J.A., Yanagisawa M.,
RA Wetzstein H.Y., Morgan J.A., Boutry M., Schuurink R.C., Dudareva N.;
RT "Emission of volatile organic compounds from petunia flowers is facilitated
RT by an ABC transporter.";
RL Science 356:1386-1388(2017).
CC -!- FUNCTION: ABC transporter controlling the release of volatile organic
CC compounds (VOCs), including floral volatile benzenoids and
CC phenylpropanoids (FVBP), in flowers of fragrant cultivars (e.g. cv.
CC Mitchell and cv. V26) (PubMed:22345641, PubMed:28663500). This scent,
CC mostly produced in the evening and night by the petals, attracts the
CC pollinators (e.g. the night-active hawkmoth pollinator Manduca sexta)
CC (PubMed:22345641). {ECO:0000269|PubMed:22345641,
CC ECO:0000269|PubMed:28663500}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8RXN0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22345641};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Restricted to the petals, with the highest
CC expression in the limb and, to a lesser extent, in petal tubes,
CC probably in both epidermal and mesophyll cell layers.
CC {ECO:0000269|PubMed:22345641}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during flower development with highest
CC levels in open flowers, and fades out as flowers are senescing.
CC {ECO:0000269|PubMed:22345641}.
CC -!- INDUCTION: In fragrant cultivars (e.g. cv. Mitchell and cv. V26),
CC increases before the onset of volatile emission at the end of the light
CC period, peaks at night and decreases when volatile emission declines
CC early morning; this precise regulation is tuned by ODO1 binding and
CC activation of its promoter. {ECO:0000269|PubMed:22345641}.
CC -!- DISRUPTION PHENOTYPE: Disturbed release of volatile organic compounds
CC (VOCs) in flowers, including benzoides and phenylpropanoids, which
CC accumulate to toxic levels in the plasma membrane.
CC {ECO:0000269|PubMed:28663500}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC {ECO:0000255|PROSITE-ProRule:PRU01700}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ088099; AFC36404.1; -; Genomic_DNA.
DR AlphaFoldDB; H9BZ66; -.
DR SMR; H9BZ66; -.
DR TCDB; 3.A.1.204.23; the atp-binding cassette (abc) superfamily.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
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; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..633
FT /note="ABC transporter G family member 1"
FT /id="PRO_0000451493"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 23..265
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 340..552
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 633 AA; 69836 MW; 852FB234FD84C13E CRC64;
MTNQLPNKVE LAEVVPQNGG VFLTWEDLWV TASSVKDGSK AILKGLTGYA MPGELLAIMG
PSGSGKSTLL DTIAGRLGSS TRQSGDILIN GRRQTLAYGS SAYVTQDDTL LATLTIKEAV
YYSAELQLPN SMSKSEKKEI ADVTLKGMGL QDAMETRIGG WSGKGISGGQ KRRVSICLEI
LTRPKLLFLD EPTSGLDSAA SYYVMKAIAS QCQGRTIIAS IHQPSVDVFS LFHSLCLLSS
GRTVYFGPAS AANEFFALSG FPCPTLQNPS DHFLKTINSD FDQDIEEGST RRKSTEEVID
ILIKSYKASD KYNAVQSQVA EICQQEGEML DKRSHASFIT QSLVLTRRSF INMSRDLGYY
WLRLAVYVVI AVGLGSLYYD VGFSAASVQA RGSMLMFVAS FITFMAIGGF PSFVEDMKVF
QREKLNGHYG SGSFVIANTL SAMPYLLLVS LIPGAIAYFM TGLQNGFEHF IYFALVLFTC
MMIVESLMMI VASMVPNFLM GLIAGAGIQA LMLLSGGFFR LPNDLPKPFW KYPLHYVAFH
KYAYEGMFKN EFEGLKIHDV NGEDILRNTW QMNMDYSKWI DLVILLGMLV LYRVLFLLVV
KAGEIVKPAI RAFMSHSPNQ INSAERPLDV FDS
