UBXN4_RAT
ID UBXN4_RAT Reviewed; 506 AA.
AC Q5HZY0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=UBX domain-containing protein 4;
DE AltName: Full=Erasin;
DE AltName: Full=UBX domain-containing protein 2;
GN Name=Ubxn4; Synonyms=Ubxd2, Ubxdc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in endoplasmic reticulum-associated protein
CC degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP
CC to the ER during ERAD. {ECO:0000250|UniProtKB:Q92575}.
CC -!- SUBUNIT: Directly interacts with VCP. Interacts with UBQLN1. Forms a
CC complex with VCP and UBQLN1. {ECO:0000250|UniProtKB:Q92575}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q92575}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus
CC face the cytosol. Also found in the nucleus envelope contiguous to the
CC ER. {ECO:0000250|UniProtKB:Q92575}.
CC -!- DOMAIN: The UBX domain is required for interaction with VCP.
CC {ECO:0000250|UniProtKB:Q92575}.
CC -!- DOMAIN: The intramembrane domain also contains the signal for ER
CC targeting. {ECO:0000250|UniProtKB:Q92575}.
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DR EMBL; BC088845; AAH88845.1; -; mRNA.
DR RefSeq; NP_001012025.1; NM_001012025.1.
DR AlphaFoldDB; Q5HZY0; -.
DR SMR; Q5HZY0; -.
DR STRING; 10116.ENSRNOP00000004878; -.
DR iPTMnet; Q5HZY0; -.
DR PhosphoSitePlus; Q5HZY0; -.
DR jPOST; Q5HZY0; -.
DR PaxDb; Q5HZY0; -.
DR PRIDE; Q5HZY0; -.
DR GeneID; 304766; -.
DR KEGG; rno:304766; -.
DR UCSC; RGD:1307451; rat.
DR CTD; 23190; -.
DR RGD; 1307451; Ubxn4.
DR VEuPathDB; HostDB:ENSRNOG00000003625; -.
DR eggNOG; KOG2507; Eukaryota.
DR HOGENOM; CLU_039222_1_1_1; -.
DR InParanoid; Q5HZY0; -.
DR OMA; HNNTSEN; -.
DR OrthoDB; 1334491at2759; -.
DR PhylomeDB; Q5HZY0; -.
DR TreeFam; TF317466; -.
DR PRO; PR:Q5HZY0; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003625; Expressed in ovary and 20 other tissues.
DR Genevisible; Q5HZY0; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Unfolded protein response.
FT CHAIN 1..506
FT /note="UBX domain-containing protein 4"
FT /id="PRO_0000317476"
FT TOPO_DOM 1..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 412..432
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 313..391
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..199
FT /note="Interaction with UBQLN1"
FT /evidence="ECO:0000250|UniProtKB:Q92575"
FT REGION 114..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 506 AA; 56394 MW; 58E7485D6380A73D CRC64;
MLWFQGAIPA AIASAKRSGA VFVVFVAGDD EQSTQMAASW EDEKVREASS DNFVAIKIDT
KSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSVSAD ELVTRIHKVQ QMHSLKGETS
VTNDKQSESS VSTPSASFEP DICESAESRN TELCETPTTS DPKSDTAAGG ECAGHDSLSQ
EPPGCSNQRP AEDLTVRVER LTKKLEERRE EKRKEEAQRE IKKEIERRKT GKEMLDYKRK
QEEELTKRML EERSREKAED RAARERIKQQ IALDRAERAA RFAKTKEAEA AKAAALLAKQ
AEAEVKRESS TRDRSTIARI QFRLPDGSSF TNQFPSDAPL EEARQFAAQT VGNTYGNFSL
ATMFPRREFT REDYKRKLLD LELAPSASVV LLPAGRPATS IVPSSSGDIW TLLGTVLYPF
LAIWRLISNF LFSNPPPAQT SARATSTEPS NSASSSKSEK REPVRKRVLE KRGEDFKKEG
KIYRLRTQDD GEDENNTWNG NSTQQM
