ADM1A_XENLA
ID ADM1A_XENLA Reviewed; 404 AA.
AC Q6GN67; Q05AY8; Q9PVQ2;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1-A;
DE AltName: Full=Oocyte membrane protein {ECO:0000303|PubMed:11148449};
GN Name=adrm1-a; Synonyms=xoom {ECO:0000303|PubMed:11148449};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10610020;
RA Hasegawa K., Shiraishi T., Kinoshita T.;
RT "Xoom: a novel oocyte membrane protein maternally expressed and involved in
RT the gastrulation movement of Xenopus embryos.";
RL Int. J. Dev. Biol. 43:479-485(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=10969733; DOI=10.1046/j.1440-169x.2000.00516.x;
RA Hasegawa K., Kinoshita T.;
RT "Xoom is required for epibolic movement of animal ectodermal cells in
RT Xenopus laevis gastrulation.";
RL Dev. Growth Differ. 42:337-346(2000).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11148449; DOI=10.1046/j.1440-169x.2001.00549.x;
RA Hasegawa K., Sakurai N., Kinoshita T.;
RT "Xoom is maternally stored and functions as a transmembrane protein for
RT gastrulation movement in Xenopus embryos.";
RL Dev. Growth Differ. 43:25-31(2001).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. Within the complex, functions as a proteasomal ubiquitin
CC receptor. {ECO:0000250|UniProtKB:Q16186}.
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). {ECO:0000250|UniProtKB:Q16186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11148449}. Nucleus
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR EMBL; AB026995; BAA86033.1; -; mRNA.
DR EMBL; BC073651; AAH73651.2; -; mRNA.
DR EMBL; BC123105; AAI23106.1; -; mRNA.
DR RefSeq; NP_001081367.1; NM_001087898.2.
DR AlphaFoldDB; Q6GN67; -.
DR SMR; Q6GN67; -.
DR BioGRID; 99136; 1.
DR DNASU; 397797; -.
DR GeneID; 397797; -.
DR KEGG; xla:397797; -.
DR CTD; 397797; -.
DR Xenbase; XB-GENE-6252580; adrm1.S.
DR OrthoDB; 1479349at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 397797; Expressed in oocyte and 20 other tissues.
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 Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; -; 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; PTHR12225; 1.
DR Pfam; PF04683; Proteasom_Rpn13; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..404
FT /note="Proteasomal ubiquitin receptor ADRM1-A"
FT /id="PRO_0000286072"
FT DOMAIN 17..130
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 278..390
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 195..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 340
FT /note="G -> S (in Ref. 1; BAA86033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 42125 MW; 255B0EAEAF087C99 CRC64;
MSSGALFPSL VPGSRGSSSK YLVEFRAGKM SLKGSTVTPD KRKGLVYIQQ TDDSLIHFCW
KDRTSGSVED DLIIFPDDCE FKRVSQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDEEYC
RKLNEYLNNP PMPGALGGSG SGSHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
GLGALTGPGL ASLLGSGGPT TSSSSSSSRS QSAAVTPSST TSSTRTTSAP VAPAAAPATT
PSPAVSSNDG ASEATSPTQP IQLSDLQNIL ATMNVPATGE GGQQVDLASV LTPEIMAPIL
ANAEVQERLT PYLPSGESLP QTADEIQNTL TSPQFQQALG MFSAALASGQ LGPLMSQFGL
PADAVDAANK GDIEAFAKAM QSTSSQKERE SSEKKEEEED MSLD
