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Database: UniProt
Entry: A0A1D5NTD3_CHICK
LinkDB: A0A1D5NTD3_CHICK
Original site: A0A1D5NTD3_CHICK 
ID   A0A1D5NTD3_CHICK        Unreviewed;       405 AA.
AC   A0A1D5NTD3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   28-JAN-2026, entry version 39.
DE   SubName: Full=Adhesion regulating molecule 1 {ECO:0000313|Ensembl:ENSGALP00010033839.1};
GN   Name=ADRM1 {ECO:0000313|Ensembl:ENSGALP00010033839.1};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010033839.1, ECO:0000313|Proteomes:UP000000539};
RN   [1] {ECO:0000313|Ensembl:ENSGALP00010033839.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Broiler {ECO:0000313|Ensembl:ENSGALP00010033839.1};
RA   Warren W., Formenti G., Fedrigo O., Haase B., Mountcastle J., Balacco J.,
RA   Tracey A., Schneider V., Okimoto R., Cheng H., Hawken R., Howe K.,
RA   Jarvis E.D.;
RT   "Gallus gallus (Chicken) genome, bGalGal1, GRCg7b, maternal haplotype
RT   autosomes + Z & W.";
RL   Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGALP00010033839.1}
RP   IDENTIFICATION.
RC   STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010033839.1};
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGALP00010033839.1}
RP   IDENTIFICATION.
RC   STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010033839.1};
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   RefSeq; NP_989982.2; NM_204651.2.
DR   AlphaFoldDB; A0A1D5NTD3; -.
DR   SMR; A0A1D5NTD3; -.
DR   Ensembl; ENSGALT00010055901.1; ENSGALP00010033839.1; ENSGALG00010022954.1.
DR   GeneID; 395365; -.
DR   KEGG; gga:395365; -.
DR   CTD; 11047; -.
DR   VEuPathDB; HostDB:geneid_395365; -.
DR   GeneTree; ENSGT00390000013839; -.
DR   InParanoid; A0A1D5NTD3; -.
DR   OMA; SNQRHFF; -.
DR   OrthoDB; 340431at2759; -.
DR   Reactome; R-GGA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-GGA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-GGA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-GGA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-GGA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-GGA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-GGA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-GGA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-GGA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-GGA-202424; Downstream TCR signaling.
DR   Reactome; R-GGA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-GGA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-GGA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-GGA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-GGA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-GGA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-GGA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-GGA-4641257; Degradation of AXIN.
DR   Reactome; R-GGA-4641258; Degradation of DVL.
DR   Reactome; R-GGA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-GGA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-GGA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-GGA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-GGA-5632684; Hedgehog 'on' state.
DR   Reactome; R-GGA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-GGA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-GGA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-GGA-5689603; UCH proteinases.
DR   Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR   Reactome; R-GGA-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-GGA-68949; Orc1 removal from chromatin.
DR   Reactome; R-GGA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-GGA-69601; Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-GGA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-GGA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-GGA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-GGA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-GGA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-GGA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-GGA-8951664; Neddylation.
DR   Reactome; R-GGA-9020702; Interleukin-1 signaling.
DR   Reactome; R-GGA-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-GGA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-GGA-9766229; Degradation of CDH1.
DR   Reactome; R-GGA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Reactome; R-GGA-9907900; Proteasome assembly.
DR   Reactome; R-GGA-9932298; Degradation of CRY and PER proteins.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000005200; Expressed in muscle tissue and 14 other cell types or 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   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:A0A1D5NTD3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT   REGION          193..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..247
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  42224 MW;  14EA59C51AA1783D CRC64;
     MSSGALFPSL VPGSRGSSSK YLVEFRAGKM SLKGSTVTPD KRKGLVYIQQ TDDSLIHFCW
     KDRTSGNVED DLIIFPDDCE FKRVPQCTTG RVYVLKFKAG SKRLFFWMQE PKTDKDEEHC
     RKVNEYLNNP PMPGALGGNA SGGHELSALG GEGGLQSLLG NMSHNQLMQL IGPTGLGGLG
     GLGALTGPGL ASLLGSGGPP TSSSSSSSRS QSAAVTPSST TSSTRVTPAP AVPAAASVTS
     PSPVPSSGNG TSSATSPTQP IQLSDLQNIL ATMNVPSGAG GQQVDLATVL TPEIMAPILA
     NAEVQERLMP YLPSGESLPQ TAEEIQNTLT SPQFQQALSM FSAALASGQL GPLMSQFGLP
     AEAIDAANKG DVEAFAKAMQ NSVKSDQKEG DSKDKKDEEE DMSLD
//
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