STR2_PETHY
ID STR2_PETHY Reviewed; 720 AA.
AC A0A0M4FLW6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=ABC transporter G family member STR2 {ECO:0000303|PubMed:25971550};
DE EC=7.6.2.-;
DE AltName: Full=Protein STUNTED ARBUSCULE 2 {ECO:0000303|PubMed:25971550};
GN Name=STR2 {ECO:0000303|PubMed:25971550};
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 [MRNA], AND INDUCTION BY RAM1 AND RHIZOPHAGUS
RP IRREGULARIS.
RC STRAIN=cv. W138;
RX PubMed=25971550; DOI=10.1104/pp.15.00310;
RA Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA Vandenbussche M., Reinhardt D.;
RT "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL Plant Physiol. 168:788-797(2015).
CC -!- FUNCTION: Together with STR, required for arbuscule development in
CC arbuscular mycorrhizal (AM) symbiosis. {ECO:0000250|UniProtKB:D3GE74}.
CC -!- SUBUNIT: Heterodimerizes with STR; the resulting transporter is located
CC in the peri-arbuscular membrane. {ECO:0000250|UniProtKB:D3GE74}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D3GE74};
CC Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-
CC arbuscular membrane of arbuscular mycorrhiza (AM).
CC {ECO:0000250|UniProtKB:D3GE74}.
CC -!- INDUCTION: Regulated by RAM1 during arbuscular mycorrhiza (AM)
CC formation after inoculation with Rhizophagus irregularis.
CC {ECO:0000269|PubMed:25971550}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Stunted arbuscule (STR) subfamily. {ECO:0000305}.
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; KR612266; ALC79556.1; -; mRNA.
DR AlphaFoldDB; A0A0M4FLW6; -.
DR SMR; A0A0M4FLW6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP: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; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..720
FT /note="ABC transporter G family member STR2"
FT /id="PRO_0000450021"
FT TOPO_DOM 1..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 468..488
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..502
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 503..523
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 548..568
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..575
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 576..596
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 605..625
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..693
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 694..714
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..720
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 25..274
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 313..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 720 AA; 80854 MW; 0792D7B56632BE04 CRC64;
MRHANGRRGD TTIDIGKPVN FTGGLEFSNL TYTVIKKIKD SDGKWLNQEV DLLHQITGYA
PKGCVTAVMG PSGAGKSTFL DGLAGRISSL RGRVSVDGMD MTPSFIKRTS AYIMQDDRLF
PMLTVYETLL FAADLRLGPI SMTDKRQRVE KLIEQLGLSS ARNTYIGDEG TRGVSGGERR
RVSIGVDIIH GPSLLFLDEP TSGLDSTSAH SVIDKVHAIA RAGSTVILTI HQPSSRIQLL
LDHLIILARG QLMYQGSPKD VSLHLGRMGR KVPKGESSIE NLIDVIQEYD QSELGVEALA
AFALTGMKPP PLGAHEMSIV PPSPAPSHRE GRGHDRSNKR LHLKDQDFDH SLRSNWNTSK
SWSASHSGVL QTLGFSPARH HRDHRNQNSV SSSLGDYAYT SENFRSIPTP HTQSSECTLN
ENDFMTPYAA ANTNAYQYLG PKFANSFLSE TWILMRRNFI NIRRTPELFL SRLVVLTVMG
IMMATMFMHP KKNLQGITNR LSFFIFTVCL FFFSSNDAVP AFIQERFIFV RETSHNKYRA
SSYTIAGLIT YLPFLAVQAA VYAVIVWFAL SLRGPFIYFL IVLYMSLLST NSFVVFVSSV
VPNYILGYAA VIAFTALFFL FCGYFLNSHD MPQYWKWMNY ISTMTYPYEG LLMNQFQTSQ
TFGIDPLGRS ITGNGILKSL NISQVESKKW EKVYIMLAWA IVYRILFYIV LRFFSKNQRT
