ID   UBXN4_BOVIN             Reviewed;         508 AA.
AC   Q3ZBU9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=UBX domain-containing protein 4;
DE   AltName: Full=UBX domain-containing protein 2;
GN   Name=UBXN4; Synonyms=UBXD2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI03097.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC103096; AAI03097.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001030491.2; NM_001035414.2.
DR   AlphaFoldDB; Q3ZBU9; -.
DR   SMR; Q3ZBU9; -.
DR   STRING; 9913.ENSBTAP00000020184; -.
DR   PaxDb; Q3ZBU9; -.
DR   PeptideAtlas; Q3ZBU9; -.
DR   PRIDE; Q3ZBU9; -.
DR   Ensembl; ENSBTAT00000020184; ENSBTAP00000020184; ENSBTAG00000015169.
DR   GeneID; 536181; -.
DR   KEGG; bta:536181; -.
DR   CTD; 23190; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015169; -.
DR   VGNC; VGNC:36627; UBXN4.
DR   eggNOG; KOG2507; Eukaryota.
DR   GeneTree; ENSGT00940000160205; -.
DR   HOGENOM; CLU_039222_1_1_1; -.
DR   InParanoid; Q3ZBU9; -.
DR   OMA; HNNTSEN; -.
DR   OrthoDB; 1334491at2759; -.
DR   TreeFam; TF317466; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000015169; Expressed in spermatid and 108 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Unfolded protein response.
FT   CHAIN           1..508
FT                   /note="UBX domain-containing protein 4"
FT                   /id="PRO_0000317474"
FT   TOPO_DOM        1..413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        414..434
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        435..508
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          315..393
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          1..200
FT                   /note="Interaction with UBQLN1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92575"
FT   REGION          117..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         489
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92575"
SQ   SEQUENCE   508 AA;  56784 MW;  27DB33631FB9621A CRC64;
     MLWFQGAIPA AIASAKRSGA VFVVFVAGDD EQSTQMAASW EDEKVTEASS NSFVAIKIDT
     RSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSISAD ELVTRIHKVR QMHSLKGEAS
     LANGSQSEGS VSTPSASFEH NNTSENCQSR NVELCETPST SDTKSDSATG GESSGQTTVS
     QEPSGCSNQR PTEDLTVRVE RLTKKLEERR EEKRKEEEQR EIKKEIERRK TGKEMLDYKR
     KQEEELTKRM LEERNREKAE DRAARERIKQ QIALDRAERA ARFAKTKEEV EAAKAAALLA
     KQAEMEIKRE TSTKERSTVA RIQFRLPDGS SFTNQFPSDA PLEEARQFAA QTVGNTYGNF
     SLATMFPRRE FTKEDYKKKL LDLELAPSAS VVLLPAGRPT TSMVHSSSGD FWTLLGTVLY
     PFLAIWRLIS NFLFSNPPPA QTSVRAASLE TSNLASSSNS EKREPVRKRV LEKRGEDFKK
     EGKIYRLRTQ DDGEDENNTW NGNSTQQM