STR1_PETHY
ID STR1_PETHY Reviewed; 830 AA.
AC A0A0M3R8G1;
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 STR {ECO:0000303|PubMed:25971550};
DE EC=7.6.2.-;
DE AltName: Full=Protein STUNTED ARBUSCULE {ECO:0000303|PubMed:25971550};
GN Name=STR {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 STR2, required for arbuscule development in
CC arbuscular mycorrhizal (AM) symbiosis. {ECO:0000250|UniProtKB:D3GE74}.
CC -!- SUBUNIT: Heterodimerizes with STR2; the resulting transporter is
CC located in the peri-arbuscular membrane.
CC {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}.
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DR EMBL; KR612265; ALC79555.1; -; mRNA.
DR AlphaFoldDB; A0A0M3R8G1; -.
DR SMR; A0A0M3R8G1; -.
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..830
FT /note="ABC transporter G family member STR"
FT /id="PRO_0000450020"
FT TOPO_DOM 1..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..588
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 589..609
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 631..651
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..661
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 662..682
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 691..711
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..798
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 799..819
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 46..297
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 333..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 830 AA; 93660 MW; 39641293FB5CD61A CRC64;
MAKFKRTDTN RSLENLLDQD KSAQMSKNGG SLAKQPTRKL IPGHGLEFNN LSYSVIKKVK
KDGVWINKEA YLLNDISGQA LRGEIMAIMG PSGAGKSTFL DALAGRIARG SLEGTVRIDG
KPVTTSYMKM ISSYVMQDDQ LFPMLTVFET FMFAAEVRLP PSISRAEKKK RVHELLEQLG
LTSATHTYIG DEGRRGVSGG ERRRVSIGID IIHKPSLLFL DEPTSGLDST SAFSVVEKVK
DIAKSGSIVL MTIHQPSFRI QMLLDRITVL ARGRLVYLGS PTGVAAFLAG FARPVPDGEN
SLEYLLDVIK EYDESTVGLD PLVLYQRDGI KPDQAAKTPV RKPPKTPKIP RTPYAKSPWT
KHISLKSSHF STGNMNSQRD PKDHSDQQSD VNNFDYEDDD DEDEFDKSLE RRAPHTPMSM
QSGVYPRLAS HFYKDFSVWL YNGVKGTPRR PPTWNNNGAI KAPISGSGFK SMSSSQFSMT
QQTPGPGNKT PIFTPGRDVI EYSSYNPSYE EVFEIEEVLD EPVHRHKFAN PWVREVLVLS
WRTTLNVIRT PELFLSREIV LTVMGLVLSS FFKKLSHFDF KTINHLLNFY IFTICLVFFS
SNDAVPTFIQ ERFIFIRETS HNAYRASSYV ISSLIVYLPF FAIQGFTFAG ITQYILHLNS
SILSFWLILY SSLVTSNAYV MLVSALVPSY ITGYAVVIAT TALFFLTCGF FLKRTQIPLV
WRWLHYISAI KYPFEALLIN EFKGSKHCYD GDLSDLSPGP LGDVKFSALR NNSRAALPQN
CTLIGEDVLF SMDIREENIW LDIVILLAWG VLYRLFFYVV LRFYSKNERK
