ID A0A072VQ29_MEDTR Unreviewed; 579 AA.
AC A0A072VQ29;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Putative bilirubin oxidase {ECO:0000313|EMBL:RHN82284.1};
DE EC=1.3.3.5 {ECO:0000313|EMBL:RHN82284.1};
DE SubName: Full=Spore coat A-like protein {ECO:0000313|EMBL:KEH44129.1};
GN Name=25485434 {ECO:0000313|EnsemblPlants:KEH44129};
GN OrderedLocusNames=MTR_1g107555 {ECO:0000313|EMBL:KEH44129.1};
GN ORFNames=MtrunA17_Chr1g0208271 {ECO:0000313|EMBL:RHN82284.1};
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 {ECO:0000313|EMBL:KEH44129.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH44129.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH44129.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH44129,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA 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 [2] {ECO:0000313|EMBL:KEH44129.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH44129.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH44129,
RC ECO:0000313|Proteomes:UP000002051};
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 [3] {ECO:0000313|EnsemblPlants:KEH44129}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH44129};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN82284.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN82284.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; CM001217; KEH44129.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN82284.1; -; Genomic_DNA.
DR RefSeq; XP_013470091.1; XM_013614637.1.
DR AlphaFoldDB; A0A072VQ29; -.
DR STRING; 3880.A0A072VQ29; -.
DR EnsemblPlants; KEH44129; KEH44129; MTR_1g107555.
DR GeneID; 25485434; -.
DR Gramene; KEH44129; KEH44129; MTR_1g107555.
DR KEGG; mtr:25485434; -.
DR HOGENOM; CLU_009100_4_0_1; -.
DR OrthoDB; 315590at2759; -.
DR Proteomes; UP000002051; Chromosome 1.
DR Proteomes; UP000265566; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047705; F:bilirubin oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR CDD; cd13844; CuRO_1_BOD_CotA_like; 1.
DR CDD; cd13868; CuRO_2_CotA_like; 1.
DR CDD; cd13891; CuRO_3_CotA_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR48373; MULTICOPPER OXIDASE LPR1-LIKE ISOFORM X1; 1.
DR PANTHER; PTHR48373:SF1; MULTICOPPER OXIDASE LPR1-LIKE ISOFORM X1; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:RHN82284.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..579
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014500890"
FT DOMAIN 144..220
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 272..357
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 433..575
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 579 AA; 65543 MW; 4DEF82FD1A1796BB CRC64;
MEKTVLLKLL TILAHLLCFV SLSSSSAAAT VKLINASKLK MFVDDLPNMP KVYGYKVVDG
VPKSKSLKIG MFKKKWKFHR DLPPTTVYAY GLNKHKATIP GPTIEALNGI STDVTWQNHL
PPNHILPWDP TIPTSLTKTT NGIPTVVHLH GGIHEPESDG NPNSFFTAGF KIKGPTWTKK
SYHYPNNQHP GNLWYHDHAM GLTRVNLLAG LIGTYIIRDP SIESTLKLPH GNEFDLPLML
FDRSFKTDGS IFMNSTGNNP TIHPQWQPEY FGDAIIVNGK AWPRLTVRRR KYRFRIINAS
NARFFRLFFS NGLRFVHVAS DSAYIGKPVT SNETLVGPSE ITDVIVDFSE SKSNVAILRN
DAAYPYPTGD PVDETSGKVM KFVILPDKEV DTSRIPEKLV EYPVVDLSSV TETRYIAMYE
YTSDIDEPIH LYFNAKPYEA QVTEIAKVGS SEVWYVINLT DDNHPLHIHL GLFKVLDQTE
LVKSDEFKDC MTKNNDAVKC HVDEHARGKK VKVPDYEKGW KNVFKMRPGF VTKIVVRFAY
IHTNATYGFD ATKESGYVYH CHILDHEDNA MMRPLKMIK
//
