ID A0A663MSH9_ATHCN Unreviewed; 424 AA.
AC A0A663MSH9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Adhesion regulating molecule 1 {ECO:0000313|Ensembl:ENSACUP00000015430.1};
GN Name=ADRM1 {ECO:0000313|Ensembl:ENSACUP00000015430.1};
OS Athene cunicularia (Burrowing owl) (Speotyto cunicularia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Strigiformes;
OC Strigidae; Athene.
OX NCBI_TaxID=194338 {ECO:0000313|Ensembl:ENSACUP00000015430.1, ECO:0000313|Proteomes:UP000472269};
RN [1] {ECO:0000313|Ensembl:ENSACUP00000015430.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSACUP00000015430.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ADRM1 family.
CC {ECO:0000256|ARBA:ARBA00009216}.
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DR AlphaFoldDB; A0A663MSH9; -.
DR Ensembl; ENSACUT00000016469.1; ENSACUP00000015430.1; ENSACUG00000010378.1.
DR OMA; SNQRHFF; -.
DR Proteomes; UP000472269; Unplaced.
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:000001; Proteasomal ubiquitin receptor ADRM1; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000472269}.
FT DOMAIN 37..150
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 295..408
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 213..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..266
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 44407 MW; 7F1E60B06C8D4D83 CRC64;
MKQKKEALGP GGFIFEYLSR MSSGALFPSL VPGSRGSSSK YLVEFRAGKM SLKGSTVTPD
KRKGLVYIQQ TDDSLIHFCW KDRTSGNVED DLIIFPDDCE FKRVPQCTTG RVYVLKFKAG
SKRLFFWMQE PKTDKDEEHC RKVNEYLNNP PMPGALGGNA SGGHELSALG GEGGLQSLLG
NMSHNQLMQL IGPTGLGGLG GLGALTGPGL ASLLGSGGPP TSSSSSSSRS QSAAVTPSST
SSTRVTPAPS VPAAASVTSP SPVPSSGNGT SSATSPTQPI QLSDLQNILA TMNVPSGAGG
QQVDLATVLT PEIMAPILAN AEVQERLMPY LPSGESLPQT AEEIQNTLTS PQFQQALSMF
SAALASGQLG PLMSQFGLPA EAVDAANKGD VEAFAKAMQN SVKSDQKEGD SKDKKDEEED
MSLD
//