CUPR1_ARTBC
ID CUPR1_ARTBC Reviewed; 186 AA.
AC P0DN32; D4ANC7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Probable GPI-anchored cupredoxin ARB_05732-1 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_05732-1;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Probable electron transfer copper protein that serves as a
CC direct electron donor (By similarity). {ECO:0000250|UniProtKB:P04377}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P04377};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P04377};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}. Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFE35688.1; Type=Erroneous gene model prediction; Note=The predicted gene ARB_05732 has been split into 2 genes: ARB_05732-1 and ARB_05732-2.; Evidence={ECO:0000305};
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DR EMBL; ABSU01000003; EFE35688.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0DN32; -.
DR SMR; P0DN32; -.
DR STRING; 663331.P0DN32; -.
DR EnsemblFungi; EFE35688; EFE35688; ARB_05732.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR SUPFAM; SSF49503; SSF49503; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Disulfide bond; Electron transport; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..153
FT /note="Probable GPI-anchored cupredoxin ARB_05732-1"
FT /id="PRO_0000434777"
FT PROPEP 154..186
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434778"
FT REGION 130..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P42849"
FT BINDING 98
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P42849"
FT BINDING 103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P42849"
FT LIPID 153
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 66..104
FT /evidence="ECO:0000250|UniProtKB:P42849"
SQ SEQUENCE 186 AA; 18699 MW; 2C8C9EF0B3B63A8B CRC64;
MVNMNILTTV ALAGLAAAKT VEVVVAENGG LTFTPNQIKA DVNDIVHFKL AKSGHDISSG
PFDMPCKPSD NSLYSGKLNE GDEFSVNITN TDPIWLYCSV SKHCSKGMVA VINPPSSGNT
IEAYKQAAAG AGNGQAPSRV NNGSSGSGTP TSGGAPAATS PNAASSLTFS GAAALVAMGG
AWIGLL
