UBXN4_CAEEL
ID UBXN4_CAEEL Reviewed; 469 AA.
AC P34631;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=UBX domain-containing protein 4 {ECO:0000305};
DE AltName: Full=Erasin {ECO:0000305|PubMed:19822669};
GN Name=ubxn-4 {ECO:0000312|WormBase:ZK353.8};
GN ORFNames=ZK353.8 {ECO:0000312|WormBase:ZK353.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17498661; DOI=10.1016/j.bbrc.2007.04.163;
RA Yamauchi S., Sasagawa Y., Ogura T., Yamanaka K.;
RT "Differential expression pattern of UBX family genes in Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 358:545-552(2007).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19822669; DOI=10.1083/jcb.200903024;
RA Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
RA Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
RT "Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD.";
RL J. Cell Biol. 187:201-217(2009).
RN [5]
RP INTERACTION WITH CDC-48.1 AND CDC-48.2.
RX PubMed=20977550; DOI=10.1111/j.1365-2443.2010.01454.x;
RA Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T.;
RT "Caenorhabditis elegans UBX cofactors for CDC-48/p97 control
RT spermatogenesis.";
RL Genes Cells 15:1201-1215(2010).
CC -!- FUNCTION: Probably acts as an adapter for ATPase cdc-48.1 and/or cdc-
CC 48.2, conferring substrate specificity. May play a role in the ER-
CC associated protein degradation pathway (ERAD) possibly acting as a
CC platform to recruit both ubql-1 and cdc-48.1 and/or cdc-48.2 to the ER
CC during ERAD. {ECO:0000269|PubMed:19822669, ECO:0000305}.
CC -!- SUBUNIT: Interacts with cdc-48.1 (via N-terminus) and cdc-48.2 (via N-
CC terminus). {ECO:0000269|PubMed:20977550}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92575}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q92575}. Note=Both the N- and the C-terminus
CC face the cytosol. {ECO:0000250|UniProtKB:Q92575}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:17498661}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, L4 larvae and adults.
CC Expressed to a lesser extent between L1 and L3 larval stages.
CC {ECO:0000269|PubMed:17498661}.
CC -!- INDUCTION: Induced upon ER stress (PubMed:19822669, PubMed:17498661).
CC Down-regulated upon heat stress (PubMed:17498661).
CC {ECO:0000269|PubMed:17498661, ECO:0000269|PubMed:19822669}.
CC -!- DOMAIN: The intramembrane domain also contains the signal for ER
CC targeting. {ECO:0000250|UniProtKB:Q92575}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC lifespan. Induces ER stress characterized by the expression of hsp-4,
CC the accumulation of ubiquitinated proteins and an increase in ubql-1
CC expression. {ECO:0000269|PubMed:19822669}.
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DR EMBL; FO081668; CCD73207.1; -; Genomic_DNA.
DR PIR; S44655; S44655.
DR RefSeq; NP_498856.1; NM_066455.4.
DR AlphaFoldDB; P34631; -.
DR SMR; P34631; -.
DR BioGRID; 41391; 3.
DR IntAct; P34631; 1.
DR STRING; 6239.ZK353.8.1; -.
DR EPD; P34631; -.
DR PaxDb; P34631; -.
DR PeptideAtlas; P34631; -.
DR PRIDE; P34631; -.
DR EnsemblMetazoa; ZK353.8.1; ZK353.8.1; WBGene00022703.
DR EnsemblMetazoa; ZK353.8.2; ZK353.8.2; WBGene00022703.
DR GeneID; 176187; -.
DR UCSC; ZK353.8.1; c. elegans.
DR CTD; 176187; -.
DR WormBase; ZK353.8; CE00392; WBGene00022703; ubxn-4.
DR eggNOG; KOG2507; Eukaryota.
DR GeneTree; ENSGT00940000160205; -.
DR HOGENOM; CLU_600254_0_0_1; -.
DR InParanoid; P34631; -.
DR OMA; HNNTSEN; -.
DR OrthoDB; 1334491at2759; -.
DR PhylomeDB; P34631; -.
DR PRO; PR:P34631; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022703; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Reference proteome;
KW Unfolded protein response.
FT CHAIN 1..469
FT /note="UBX domain-containing protein 4"
FT /id="PRO_0000211007"
FT TOPO_DOM 1..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 278..356
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 181..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..214
FT /evidence="ECO:0000255"
FT COMPBIAS 404..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51631 MW; C8BBF80CAA37A9CD CRC64;
MQWFGGNVAT AIQISRKNKA LLIVYITTDS EDGQIFDGFW QHIDSSNLLC AVVGIKLKAG
ETSAQQFADI YPTPILPAAY LIDQNGKPLE VITPLVGKTY DQFRAKFDKA TAQFVNGMPT
AAANQLSTPS PSPAPVQVPA STDAPIPAPT PVTAPIQSSS TSQEMTRELA EKVARAKALL
EQKKQKDAEK KREADKHVKE EMTKAREAKQ ERDAEALVKA AKQRKMEKLA AESDKKRILA
QIKADREAAQ KKFGKLVNTE NASENTEKKQ ETTVGKAVPS DRCRLQVRLP DGSTFVEEFP
SNDVLNSLVE IIRQKPSIAG TTFEIQQPYP RRIFTNDDYS KTFLENQLTP STALVVIQKS
SGSSSNYGSF SLSTQTVSFV TWVLYPLTAF WNIFCGMIGW NSTGKQQDSK SKKNDGPSTS
GQSGSQPQRR GMPRSAEVRR RGNVAGLENP NEDDPEERAS FNGNSTQFM
