ID UBQL1_RAT Reviewed; 582 AA.
AC Q9JJP9; Q6IN34;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 16-APR-2014, entry version 96.
DE RecName: Full=Ubiquilin-1;
DE AltName: Full=Protein linking IAP with cytoskeleton 1;
DE Short=PLIC-1;
GN Name=Ubqln1; Synonyms=Da41, Plic1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NBL1.
RX PubMed=9303440; DOI=10.1089/dna.1997.16.985;
RA Ozaki T., Hishiki T., Toyama Y., Yuasa S., Nakagawara A., Sakiyama S.;
RT "Identification of a new cellular protein that can interact
RT specifically with DAN.";
RL DNA Cell Biol. 16:985-991(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 37-53; 62-74; 198-212; 245-263 AND 540-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH GABRA1; GABRA2; GABRA3; GABRA6; GABRB1; GABRB2 AND
RP GABRB3, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11528422; DOI=10.1038/nn0901-908;
RA Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA Wisden W., Triller A., Smart T.G., Moss S.J.;
RT "GABA(A) receptor cell surface number and subunit stability are
RT regulated by the ubiquitin-like protein Plic-1.";
RL Nat. Neurosci. 4:908-916(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 450-458 IN COMPLEX WITH MHC
RP I.
RX PubMed=12470953; DOI=10.1016/S0022-2836(02)01095-1;
RA Rudolph M.G., Stevens J., Speir J.A., Trowsdale J., Butcher G.W.,
RA Joly E., Wilson I.A.;
RT "Crystal structures of two rat MHC class Ia (RT1-A) molecules that are
RT associated differentially with peptide transporter alleles TAP-A and
RT TAP-B.";
RL J. Mol. Biol. 324:975-990(2002).
CC -!- FUNCTION: Links CD47 to the cytoskeleton. Promotes the surface
CC expression of GABA-A receptors. Promotes the accumulation of
CC uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has
CC no effect on PSEN1 and PSEN2 degradation (By similarity).
CC -!- SUBUNIT: Binds CD47, UBE3A, BTRC, P4HB, MTOR, PSEN1 and PSEN2.
CC Interacts with the proteasome 19S subunit (By similarity). Binds
CC NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm.
CC Note=Detected in neuronal processes and at synapses.
CC -!- DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It
CC also binds ubiquitin with micromolar affinity, independently of
CC polyubiquitin linkage type (By similarity).
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR EMBL; D87950; BAA92267.1; -; mRNA.
DR EMBL; BC072477; AAH72477.1; -; mRNA.
DR RefSeq; NP_446199.2; NM_053747.2.
DR UniGene; Rn.94864; -.
DR PDB; 1KJV; X-ray; 1.48 A; P=450-458.
DR PDBsum; 1KJV; -.
DR ProteinModelPortal; Q9JJP9; -.
DR SMR; Q9JJP9; 1-98, 530-579.
DR BioGrid; 250384; 3.
DR PaxDb; Q9JJP9; -.
DR PRIDE; Q9JJP9; -.
DR Ensembl; ENSRNOT00000061233; ENSRNOP00000057944; ENSRNOG00000019282.
DR GeneID; 114590; -.
DR KEGG; rno:114590; -.
DR UCSC; RGD:620745; rat.
DR CTD; 29979; -.
DR RGD; 620745; Ubqln1.
DR eggNOG; COG5272; -.
DR GeneTree; ENSGT00390000005720; -.
DR HOGENOM; HOG000234878; -.
DR HOVERGEN; HBG064537; -.
DR KO; K04523; -.
DR OrthoDB; EOG7HF1J8; -.
DR PhylomeDB; Q9JJP9; -.
DR EvolutionaryTrace; Q9JJP9; -.
DR NextBio; 618741; -.
DR PRO; PR:Q9JJP9; -.
DR Genevestigator; Q9JJP9; -.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:BHF-UCL.
DR GO; GO:0097194; P:execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:1902175; P:regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; ISS:BHF-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISS:HGNC.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin-like.
DR InterPro; IPR028799; UBQLN1.
DR PANTHER; PTHR10677; PTHR10677; 1.
DR PANTHER; PTHR10677:SF8; PTHR10677:SF8; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Nucleus; Proteasome; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 582 Ubiquilin-1.
FT /FTId=PRO_0000211010.
FT DOMAIN 28 102 Ubiquitin-like.
FT DOMAIN 539 579 UBA.
FT COMPBIAS 372 546 Gln-rich.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT CONFLICT 63 64 HI -> QT (in Ref. 3; AA sequence).
FT CONFLICT 224 224 N -> D (in Ref. 2; AAH72477).
FT CONFLICT 247 249 ERD -> DRA (in Ref. 2; AAH72477).
SQ SEQUENCE 582 AA; 62072 MW; 6651E95B09071E5B CRC64;
MAESAESGGP PGAQDSAADS GPAEPKIMKV TVKTPKEKEE FAVPENSSVQ QFKEEISKRF
KSHIDQLVLI FAGKILKDQD TLSQHGIHDG LTVHLVIKTQ NRPQDNSAQQ TNTTGNSVTS
SPAPDSNPTS GPAANSSFGL GGLGGLAGLS SLGLNTTNFS ELQSQMQRQL LSNPEMMVQI
MENPFVQSML SNPDLMRQLI MANPQMQQLI QRNPEISHML NNPNIMRQTL ELARNPAMMQ
EMMRNQERDL SNLESIPGGY NALRRMYTDI QEPMLNAAQE QFGGNPFASL VSSPSSAEGT
QPSRTENRDP LPNPWAPQTP QSSPASGSTG STTNTVSTSA GNATSTPAGQ GTSGPNLVPG
AGASMFNTPG MQSLLQQITE NPQLMQNMLS APYMRSMMQS LSQNPDLAAQ MMLNNPLFAG
NPQLQEQMRQ QLPTFLQQMQ NPDTLSAMSN PRAMQALLQI QQGLQTLATE APGLIPGFTP
GLAAGNSGGP AGTTAPSTAP GEDTNPQGGA AEPGHQQFIQ QMLQALAGVN PQLQSPEVRF
QQQLEQLSAM GFLNREANLQ ALIATGGDIN AAIERLLGSQ PS
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