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Database: UniProt
Entry: A0A8W4FAK7_PIG
LinkDB: A0A8W4FAK7_PIG
Original site: A0A8W4FAK7_PIG 
ID   A0A8W4FAK7_PIG          Unreviewed;       418 AA.
AC   A0A8W4FAK7;
DT   14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2022, sequence version 1.
DT   28-JAN-2026, entry version 17.
DE   RecName: Full=Proteasomal ubiquitin receptor ADRM1 {ECO:0000256|ARBA:ARBA00068549};
DE   AltName: Full=Rpn13 homolog {ECO:0000256|ARBA:ARBA00079688};
GN   Name=ADRM1 {ECO:0000313|Ensembl:ENSSSCP00000076431.1};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000076431.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000076431.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000076431.1};
RX   PubMed=32543654;
RA   Warr A., Affara N., Aken B., Beiki H., Bickhart D.M., Billis K., Chow W.,
RA   Eory L., Finlayson H.A., Flicek P., Giron C.G., Griffin D.K., Hall R.,
RA   Hannum G., Hourlier T., Howe K., Hume D.A., Izuogu O., Kim K., Koren S.,
RA   Liu H., Manchanda N., Martin F.J., Nonneman D.J., O'Connor R.E.,
RA   Phillippy A.M., Rohrer G.A., Rosen B.D., Rund L.A., Sargent C.A.,
RA   Schook L.B., Schroeder S.G., Schwartz A.S., Skinner B.M., Talbot R.,
RA   Tseng E., Tuggle C.K., Watson M., Smith T.P.L., Archibald A.L.;
RT   "An improved pig reference genome sequence to enable pig genetics and
RT   genomics research.";
RL   Gigascience 9:giaa051-giaa051(2020).
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000076431.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000076431.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). Interacts with the proteasomal scaffolding
CC       protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction
CC       activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts
CC       with UBQLN2 and ubiquitin. {ECO:0000256|ARBA:ARBA00061738}.
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; A0A8W4FAK7; -.
DR   Ensembl; ENSSSCT00000099242.1; ENSSSCP00000076431.1; ENSSSCG00000038718.3.
DR   GeneTree; ENSGT00390000013839; -.
DR   Proteomes; UP000008227; Chromosome 17.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A8W4FAK7};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          18..131
FT                   /note="Pru"
FT                   /evidence="ECO:0000259|PROSITE:PS51917"
FT   DOMAIN          291..402
FT                   /note="DEUBAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51916"
FT   REGION          212..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..262
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  43217 MW;  38D72EE0C362DAAB CRC64;
     MTTSGALFPS LVPGSRGSSN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
     WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
     CRKVNEYLNN PPMPGALGAS GSGGHELSAL GGNRPLPGCA GRSRWVSGEG GLQSLLGNMS
     HSQLMQLIGP AGLGGLGGLG ALTGPGLASL LGSGGPPASS SSSRSQSAAV TPSSTTSSTR
     ATPAPAAPAA ASATSPSPAP SSGNGTSTAA SPTQPIQLSD LQSILATMNV PAGPGGGQQV
     DLASVLTPEI MAPILANADV QERLLPYLPS GESLPQTAEE IQNTLTSPQF QQALGMFSAA
     LASGQLGPLM CQFGLGLARP GALDVEAFAK AMQSSASPEQ QEGDGKDKKD EEEDMSLD
//
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