BCP1B_MEDTR
ID BCP1B_MEDTR Reviewed; 162 AA.
AC A0A072U307;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Blue copper protein 1b {ECO:0000303|PubMed:20687807};
DE Short=MtBcp1b {ECO:0000303|PubMed:20687807};
DE Flags: Precursor;
GN Name=BCP1B {ECO:0000303|PubMed:20687807};
GN Synonyms=MtC50697 {ECO:0000303|PubMed:20687807};
GN OrderedLocusNames=MTR_7g086160 {ECO:0000312|EMBL:KEH23538.1};
GN ORFNames=MtrunA17_Chr7g0253681 {ECO:0000312|EMBL:RHN47500.1};
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 [MRNA], AND INDUCTION BY GLOMUS INTRARADICES.
RC STRAIN=cv. Jemalong J5; TISSUE=Root;
RX PubMed=20687807; DOI=10.1094/mpmi-23-9-1175;
RA Paradi I., van Tuinen D., Morandi D., Ochatt S., Robert F., Jacas L.,
RA Dumas-Gaudot E.;
RT "Transcription of two blue copper-binding protein isogenes is highly
RT correlated with arbuscular mycorrhizal development in Medicago
RT truncatula.";
RL Mol. Plant Microbe Interact. 23:1175-1183(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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Accumulates in roots, in a RAM1-dependent manner, during
CC colonization by arbuscular mycorrhizal (AM) fungi (e.g. Glomus
CC versiforme and G.intraradices); the expression level correlates tightly
CC with AM development. {ECO:0000269|PubMed:20687807,
CC ECO:0000269|PubMed:26511916}.
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DR EMBL; FN600697; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CM001223; KEH23538.1; -; Genomic_DNA.
DR EMBL; PSQE01000007; RHN47500.1; -; Genomic_DNA.
DR RefSeq; XP_013449510.1; XM_013594056.1.
DR AlphaFoldDB; A0A072U307; -.
DR SMR; A0A072U307; -.
DR EnsemblPlants; KEH23538; KEH23538; MTR_7g086160.
DR GeneID; 25498990; -.
DR Gramene; KEH23538; KEH23538; MTR_7g086160.
DR KEGG; mtr:MTR_7g086160; -.
DR HOGENOM; CLU_058719_4_0_1; -.
DR OrthoDB; 1537588at2759; -.
DR Proteomes; UP000002051; Chromosome 7.
DR Proteomes; UP000265566; Chromosome 7.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR039391; Phytocyanin.
DR InterPro; IPR003245; Phytocyanin_dom.
DR PANTHER; PTHR33021; PTHR33021; 1.
DR Pfam; PF02298; Cu_bind_like; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS51485; PHYTOCYANIN; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Electron transport; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..162
FT /note="Blue copper protein 1b"
FT /id="PRO_5014499234"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 25..125
FT /note="Phytocyanin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 111
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 78..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00818"
SQ SEQUENCE 162 AA; 17542 MW; C3C88D6D217EEC72 CRC64;
MASSRVVLIL SISMVLLSSV AIAATDYIVG DDKGWTVDFD YTQWAQDKVF RVGDNLVFNY
DPSRHNVFKV NGTLFQSCTF PPKNEALSTG KDIIQLKTEG RKWYVCGVAD HCSARQMKLV
ITVLAEGAPA PSPPPSSDAH SVVSSLFGVV MAIMVAIAVI FA