ID A0A8H5G976_9AGAR Unreviewed; 312 AA.
AC A0A8H5G976;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Adhesion regulating molecule {ECO:0008006|Google:ProtNLM};
GN ORFNames=D9756_004757 {ECO:0000313|EMBL:KAF5360659.1};
OS Leucocoprinus leucothites.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucocoprinus.
OX NCBI_TaxID=201217 {ECO:0000313|EMBL:KAF5360659.1, ECO:0000313|Proteomes:UP000559027};
RN [1] {ECO:0000313|EMBL:KAF5360659.1, ECO:0000313|Proteomes:UP000559027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 146.42 {ECO:0000313|EMBL:KAF5360659.1,
RC ECO:0000313|Proteomes:UP000559027};
RX PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT mushroom-forming fungi.";
RL ISME J. 14:2046-2059(2020).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF5360659.1}.
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DR EMBL; JAACJO010000003; KAF5360659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H5G976; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000559027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000559027}.
FT DOMAIN 2..116
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 191..300
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 123..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..152
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 33463 MW; 794A609003C0541B CRC64;
MSDSDTLLGF KAGRAFRREG SNTIEPSPTK GAILLINGDD GLLHFQWKNR ESGNVEEDLI
LFPSDASFAK VTQSPGRVYV LKFSSSNRRD FFWLQDASSA RDDEFVRNLN GLLEDPDYEV
QWSSSSTSQI QTSSSSVPSS LPTSNPTTSN NNFQVTPEQT AALSNALGQL QGNPILSNVL
QRLQAQNAGG VSALAPPDLA LTDVLSPANV APLFTSHPEL ISTLFPHLPP DLPMPPSAET
LQRVISSPHF RAAVSSLDQG LRTGLLGGFV RSLGLPEEAG TGVLPFLRAI QEQADRERSG
SSSAGGNNME TE
//
