ID A0AAF6B8S9_MARPO Unreviewed; 342 AA.
AC A0AAF6B8S9;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 6.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BBN08413.1};
GN ORFNames=Mp_4g11400 {ECO:0000313|EMBL:BBN08413.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:BBN08413.1, ECO:0000313|Proteomes:UP001162541};
RN [1] {ECO:0000313|Proteomes:UP001162541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tak-1 {ECO:0000313|Proteomes:UP001162541};
RX PubMed=32004456; DOI=10.1016/j.cub.2019.12.015;
RA Montgomery S.A., Tanizawa Y., Galik B., Wang N., Ito T., Mochizuki T.,
RA Akimcheva S., Bowman J.L., Cognat V., Marechal-Drouard L., Ekker H.,
RA Hong S.F., Kohchi T., Lin S.S., Liu L.D., Nakamura Y., Valeeva L.R.,
RA Shakirov E.V., Shippen D.E., Wei W.L., Yagura M., Yamaoka S., Yamato K.T.,
RA Liu C., Berger F.;
RT "Chromatin organization in early land plants reveals an ancestral
RT association between H3K27me3, transposons, and constitutive
RT heterochromatin.";
RL Curr. Biol. 30:573-588.e7(2020).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AP019869; BBN08413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAF6B8S9; -.
DR Proteomes; UP001162541; Chromosome 4.
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; 1.10.2020.20:FF:000002; 26S proteasome regulatory subunit 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}.
FT DOMAIN 19..131
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 206..313
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 133..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 38683 MW; 73791AA359D32245 CRC64;
MASTKWAQMS PVPTEPMTGT KEILLEFRAG KMHLENSRVH SDPRKGLVRI VRADDSLVHF
QWLDRVLNVV EDDQIVFPEE AIFEKVSQTL GRVYILKFKE DNRKSFFWMQ GPRAEEDEEL
CSLVNIHLNR PLAEMGGDEE PESPLQPVSE TSEGGDTAEV SLRDVNLVSS IGEPSPSSTG
AVQLSELQRI LQGLGQVAVP QDAMETMHRD TGPSFSDILK PDVVIPLLDR SHFEDRLAPY
LPEGVKTPEA IAELMQSPQF QQQLDMFTHV LRSGQLDWAQ FGIDPSNYNF TVSSFLEAFQ
DQFISMPDSA QDENMPESER PREVQKRDQK RGRDNDVMEE GL
//
