ID A0A504YX15_FASGI Unreviewed; 394 AA.
AC A0A504YX15;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 02-APR-2025, entry version 18.
DE SubName: Full=Adhesion regulating molecule 1 {ECO:0000313|EMBL:TPP62408.1};
GN ORFNames=FGIG_02449 {ECO:0000313|EMBL:TPP62408.1};
OS Fasciola gigantica (Giant liver fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC Fasciola.
OX NCBI_TaxID=46835 {ECO:0000313|EMBL:TPP62408.1, ECO:0000313|Proteomes:UP000316759};
RN [1] {ECO:0000313|EMBL:TPP62408.1, ECO:0000313|Proteomes:UP000316759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uganda_cow_1 {ECO:0000313|EMBL:TPP62408.1};
RA Choi Y.-J.;
RT "Annotation for the trematode Fasciola gigantica.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:TPP62408.1}.
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DR EMBL; SUNJ01006875; TPP62408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A504YX15; -.
DR STRING; 46835.A0A504YX15; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000316759; 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 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:UP000316759}.
FT DOMAIN 14..127
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 241..356
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 186..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..218
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..360
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 42759 MW; 1C413B6F70776592 CRC64;
MIPSAALFER PQVPPPRHLL QFKAGKMTQG SDNWVHADPR KGWVYVYQSG DGKLHFTWID
RKTCLVEDDF VIAPKQAEFR KVLQCTTGRV YLLKLKDSKR FFIWMQEPNA KKDENICTRI
NDYIEFLPAQ TNTPGDWLTS FGGLNQLTNS DILALLSMGV GLGSGLSSES DVSSAQATAE
TIGRHLNTSH LSSQANPTSI LGSGANTTSA GASGGASTTE KRPEGGKIQL QDLRNILSSV
TAKKEPSIDL NSAINVDSLR TLLEKPEVQE RLKPHLPPVD PEATPDSDLA DLTTNIRSAQ
FKSTLKSFSA AFQTGDLAPL LAQFKLGAKA DEAARRGDLV AFSQALQTSS ASKVFGSSSV
KPDEAAKKDE DKNKKPDDST PDKKDHNGTA MDTD
//
