STR2_MEDTR
ID STR2_MEDTR Reviewed; 727 AA.
AC A9YWR6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=ABC transporter G family member STR2 {ECO:0000303|PubMed:20453115};
DE EC=7.6.2.-;
DE AltName: Full=Protein STUNTED ARBUSCULE 2 {ECO:0000303|PubMed:20453115};
GN Name=STR2 {ECO:0000303|PubMed:20453115};
GN OrderedLocusNames=MTR_5g030910 {ECO:0000312|EMBL:AES95907.1};
GN ORFNames=MtrunA17_Chr5g0411621 {ECO:0000312|EMBL:RHN54875.1};
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].
RC STRAIN=cv. Jemalong A17;
RX PubMed=16273388; DOI=10.1007/s00438-005-0057-9;
RA Kevei Z., Seres A., Kereszt A., Kalo P., Kiss P., Toth G., Endre G.,
RA Kiss G.B.;
RT "Significant microsynteny with new evolutionary highlights is detected
RT between Arabidopsis and legume model plants despite the lack of
RT macrosynteny.";
RL Mol. Genet. Genomics 274:644-657(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, INDUCTION BY GLOMUS VERSIFORME, INTERACTION WITH STR,
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 [3]
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 [4]
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 [5]
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).
CC -!- FUNCTION: Together with STR, required for arbuscule development in
CC arbuscular mycorrhizal symbiosis. {ECO:0000269|PubMed:20453115}.
CC -!- SUBUNIT: Heterodimerizes with STR; the resulting transporter is located
CC 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 root cortical cells containing arbuscules
CC upon arbuscular mycorrhizal (AM) symbiosis with Glomus versiforme.
CC {ECO:0000269|PubMed:20453115}.
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; EU306659; ABY48138.1; -; Genomic_DNA.
DR EMBL; FJ659116; ACV73543.1; -; Genomic_DNA.
DR EMBL; FJ659117; ACV73544.1; -; mRNA.
DR EMBL; CM001221; AES95907.1; -; Genomic_DNA.
DR EMBL; PSQE01000005; RHN54875.1; -; Genomic_DNA.
DR RefSeq; XP_003612949.1; XM_003612901.2.
DR AlphaFoldDB; A9YWR6; -.
DR SMR; A9YWR6; -.
DR STRING; 3880.AES95907; -.
DR TCDB; 3.A.1.204.22; the atp-binding cassette (abc) superfamily.
DR EnsemblPlants; AES95907; AES95907; MTR_5g030910.
DR GeneID; 11407838; -.
DR Gramene; AES95907; AES95907; MTR_5g030910.
DR KEGG; mtr:MTR_5g030910; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_8_1; -.
DR OMA; CGYFLDS; -.
DR OrthoDB; 1022017at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
DR Proteomes; UP000265566; Chromosome 5.
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:0140359; F:ABC-type transporter activity; IEA:InterPro.
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; 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 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..727
FT /note="ABC transporter G family member STR2"
FT /id="PRO_0000450019"
FT TOPO_DOM 1..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 476..496
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..510
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 511..531
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 560..580
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..583
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 584..604
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 613..633
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..699
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 700..720
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 25..275
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 727 AA; 81603 MW; 7ADAA1DFD22DF2A2 CRC64;
MKTQGLELET VIDIKHKPVS FTGGLEFESL TYTVTKKKKV DGKWSNEDVD LLHDITGYAP
KGCITAVMGP SGAGKSTLLD GLAGRIASGS LKGKVSLDGN SVNASLIKRT SAYIMQEDRL
FPMLTVYETL MFAADFRLGP LSAVDKRQRV EKLIEQLGLS SSRNTYIGDE GTRGVSGGER
RRVSIGVDII HGPSLLFLDE PTSGLDSTSA LSVIEKLHDI ARNGSTVILT IHQPSSRIQL
LLDHLIILAR GQLMFQGSLK DVGHHLNRMG RKIPKGENPI ENLIDVIQEY DQCDFVGVEV
LAEFARTGMK PPLLSDMEEI ISYTNSIAPS PSPLHRGSKY EEKSQDFSYS SQISRRSLND
EFDHSIRSPY NNTPMSWSAS NSAAFLKFTP SRLKNENKVQ KPPSHASPGI YTYSSEILPA
TPTPHSSDYV VDENDYLTPT NSSQEHLGPK FANSYIGETW ILMRRNFTNI RRTPELFLSR
LMVLTFMGVM MATMFHNPKN TLQGITNRLS FFIFTVCLFF FSSNDAVPAF IQERFIFIRE
TSHNAYRASC YTIASLITHM PFLALQALAY AAIVWFALEL RGPFIYFFLV LFISLLSTNS
FVVFVSSIVP NYILGYAAVI AFTALFFLFC GYFLSSEDIP LYWRWMNKVS TMTYPYEGLL
MNEYQTNETF GSNDGVSITG FDILKSLHIG TEEIKKRNNV LIMLGWAVLY RILFYIILRF
ASKNQRS
