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STR1_MEDTR
ID   STR1_MEDTR              Reviewed;         817 AA.
AC   D3GE74;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=ABC transporter G family member STR {ECO:0000303|PubMed:20453115};
DE            EC=7.6.2.-;
DE   AltName: Full=Protein STUNTED ARBUSCULE {ECO:0000303|PubMed:20453115};
GN   Name=STR {ECO:0000303|PubMed:20453115};
GN   OrderedLocusNames=MTR_8g107450 {ECO:0000312|EMBL:AET05608.1};
GN   ORFNames=MtrunA17_Chr8g0393191 {ECO:0000312|EMBL:RHN43934.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   TISSUE SPECIFICITY, INDUCTION BY GLOMUS VERSIFORME, INTERACTION WITH STR2,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=20453115; DOI=10.1105/tpc.110.074955;
RA   Zhang Q., Blaylock L.A., Harrison M.J.;
RT   "Two Medicago truncatula half-ABC transporters are essential for arbuscule
RT   development in arbuscular mycorrhizal symbiosis.";
RL   Plant Cell 22:1483-1497(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA   Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA   Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA   De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA   Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA   Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA   Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA   Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA   Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA   Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA   Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA   Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA   Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA   O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA   Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA   Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA   Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA   Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA   White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA   Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA   Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jemalong A17;
RX   PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA   Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA   Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA   Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA   Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA   Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA   Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 4:1017-1025(2018).
RN   [5]
RP   INDUCTION BY RAM1 AND GLOMUS VERSIFORME.
RX   PubMed=26511916; DOI=10.1104/pp.15.01155;
RA   Park H.-J., Floss D.S., Levesque-Tremblay V., Bravo A., Harrison M.J.;
RT   "Hyphal branching during arbuscule development requires reduced arbuscular
RT   mycorrhiza1.";
RL   Plant Physiol. 169:2774-2788(2015).
CC   -!- FUNCTION: Together with STR2, required for arbuscule development in
CC       arbuscular mycorrhizal (AM) symbiosis. {ECO:0000269|PubMed:20453115}.
CC   -!- SUBUNIT: Heterodimerizes with STR2; the resulting transporter is
CC       located in the peri-arbuscular membrane. {ECO:0000269|PubMed:20453115}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20453115};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-
CC       arbuscular membrane of arbuscular mycorrhiza (AM).
CC       {ECO:0000269|PubMed:20453115}.
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in the vascular tissue of
CC       roots. {ECO:0000269|PubMed:20453115}.
CC   -!- INDUCTION: Accumulates in roots cortical cells containing arbuscules,
CC       in a RAM1-dependent manner, upon arbuscular mycorrhizal (AM) symbiosis
CC       with Glomus versiforme (PubMed:20453115, PubMed:26511916). Triggered by
CC       RAM1 (PubMed:26511916). {ECO:0000269|PubMed:20453115,
CC       ECO:0000269|PubMed:26511916}.
CC   -!- DISRUPTION PHENOTYPE: Stunted arbuscule phenotype due to an impaired
CC       arbuscule development during arbuscular mycorrhizal (AM) symbiosis with
CC       Glomus versiforme; normal initial phases of the symbiosis, including
CC       hyphopodia formation and fungal entry into the cortex, as well as
CC       normal arbuscule development initiation, including arbuscule-associated
CC       genes expression, but strongly delayed and impaired arbuscule
CC       development (PubMed:20453115). Normal nodulation in the presence of
CC       Sinorhizobium meliloti (PubMed:20453115).
CC       {ECO:0000269|PubMed:20453115}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Stunted arbuscule (STR) subfamily. {ECO:0000305}.
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DR   EMBL; FJ659114; ACV73541.1; -; Genomic_DNA.
DR   EMBL; FJ659115; ACV73542.1; -; mRNA.
DR   EMBL; CM001224; AET05608.1; -; Genomic_DNA.
DR   EMBL; PSQE01000008; RHN43934.1; -; Genomic_DNA.
DR   RefSeq; XP_003631132.1; XM_003631084.2.
DR   AlphaFoldDB; D3GE74; -.
DR   SMR; D3GE74; -.
DR   STRING; 3880.AET05608; -.
DR   TCDB; 3.A.1.204.22; the atp-binding cassette (abc) superfamily.
DR   EnsemblPlants; AET05608; AET05608; MTR_8g107450.
DR   GeneID; 11412901; -.
DR   Gramene; AET05608; AET05608; MTR_8g107450.
DR   KEGG; mtr:MTR_8g107450; -.
DR   eggNOG; KOG0061; Eukaryota.
DR   HOGENOM; CLU_000604_57_8_1; -.
DR   OMA; SVWVYHG; -.
DR   OrthoDB; 1022017at2759; -.
DR   Proteomes; UP000002051; Chromosome 8.
DR   Proteomes; UP000265566; Chromosome 8.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0085042; C:periarbuscular membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0036377; P:arbuscular mycorrhizal association; IMP:UniProtKB.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..817
FT                   /note="ABC transporter G family member STR"
FT                   /id="PRO_0000450018"
FT   TOPO_DOM        1..542
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        543..563
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        564..579
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        580..600
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        601..621
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        622..642
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        643..657
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        658..678
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        679..681
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        682..702
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        703..787
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        788..808
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        809..817
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          43..294
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CARBOHYD        762
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   817 AA;  91885 MW;  70B5CE92E5EA19D6 CRC64;
     MARLERDGTN KSLESLMDSH KPGGTTTNLN QLRTQKSIPG YGLEFTNLSY SIIKKQKKDG
     VWINKETYLL HDISGQAIKG EIMAIMGPSG AGKSTFLDAL AGRIAKGSLQ GSVRIDGKPV
     TTSYMKMVSS YVMQDDQLFP MLTVFETFMF AAEVRLPPSI SRDEKKKRVH ELLNKLGLQS
     ATHTYIGDEG RRGVSGGERR RVSIGIEIIH KPSLLFLDEP TSGLDSTSAY SVVEKIKDIA
     QGGSIVLMTI HQPSFRIQML LDKITILARG RLIYMGRPDA LHTHLSGFGR PVPDGENNIE
     YLLDVITEYD QATVGLDPLV QYQHDGHKPD PAAMTPVPKP PRTPYRRNTP ASKHMISLRS
     QGFTAGTPQP DSSQFGLDDD DNDDDENFDN SLERRSVQTS RNIVTSGVYP RLASQFYQDF
     SAKDFSVWLY NGVVGTPRRP PSWTPARTPG WTPGKTPLSG PRSFVSNQHS ASYQDPYYIQ
     KTNTVVGQSM DYSATSYAPS YEEFEIEEVL DEPDLGPKYA NPWLREVAVL SWRTVLNVIR
     TPELFASREI VLTVMALVLS TIFKNLGDTT FIDINRLLNF YIFAVCLVFF SSNDAVPSFI
     MERFIFIRET SHNAYRASSY VISSLIVYLP FFAVQGLTFA VITKLMLHLK SNLFNFWMIL
     FASLITTNAY VMLVSALVPS YITGYAVVIA TTALFFLTCG FFLKRTQIPA YWKWLHYISA
     IKYPFEGLLI NEFKNNRGCY SGNKADLSPG PLGDVKPSKH HNASLPLNCL LGEDVLSTMD
     ITMESLWYDI LILLAWGVLY RFFFYLVLRF YSKNERK
 
 
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