UBXN4_MOUSE
ID UBXN4_MOUSE Reviewed; 506 AA.
AC Q8VCH8; Q3UGR4; Q8BW17;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Melanocyte;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=16968747; DOI=10.1242/jcs.03163;
RA Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A.,
RA Monteiro M.J.;
RT "Characterization of erasin (UBXD2): a new ER protein that promotes ER-
RT associated protein degradation.";
RL J. Cell Sci. 119:4011-4024(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 309-409.
RG RIKEN structural genomics initiative (RSGI);
RT "Structure of the UBX domain in mouse UBX domain-containing protein 2.";
RL Submitted (MAR-2007) to the PDB data bank.
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 -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain, heart,
CC kidney, liver, muscle and spleen (at protein level).
CC {ECO:0000269|PubMed:16968747}.
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; AK075716; BAC35906.1; -; mRNA.
DR EMBL; AK147795; BAE28143.1; -; mRNA.
DR EMBL; BC019795; AAH19795.1; -; mRNA.
DR CCDS; CCDS15251.1; -.
DR RefSeq; NP_080666.2; NM_026390.2.
DR PDB; 2DZK; NMR; -; A=312-409.
DR PDBsum; 2DZK; -.
DR AlphaFoldDB; Q8VCH8; -.
DR SMR; Q8VCH8; -.
DR BioGRID; 212456; 5.
DR STRING; 10090.ENSMUSP00000027592; -.
DR iPTMnet; Q8VCH8; -.
DR PhosphoSitePlus; Q8VCH8; -.
DR SwissPalm; Q8VCH8; -.
DR EPD; Q8VCH8; -.
DR jPOST; Q8VCH8; -.
DR MaxQB; Q8VCH8; -.
DR PaxDb; Q8VCH8; -.
DR PeptideAtlas; Q8VCH8; -.
DR PRIDE; Q8VCH8; -.
DR ProteomicsDB; 298379; -.
DR GeneID; 67812; -.
DR KEGG; mmu:67812; -.
DR UCSC; uc007cll.1; mouse.
DR CTD; 23190; -.
DR MGI; MGI:1915062; Ubxn4.
DR eggNOG; KOG2507; Eukaryota.
DR InParanoid; Q8VCH8; -.
DR OrthoDB; 1334491at2759; -.
DR PhylomeDB; Q8VCH8; -.
DR TreeFam; TF317466; -.
DR BioGRID-ORCS; 67812; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ubxn4; mouse.
DR EvolutionaryTrace; Q8VCH8; -.
DR PRO; PR:Q8VCH8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VCH8; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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 3D-structure; 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_0000211028"
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 110..194
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 110..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..186
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:17242355"
FT CONFLICT 65
FT /note="C -> R (in Ref. 1; BAC35906)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="I -> T (in Ref. 1; BAE28143)"
FT /evidence="ECO:0000305"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:2DZK"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2DZK"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2DZK"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:2DZK"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2DZK"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2DZK"
FT TURN 371..375
FT /evidence="ECO:0007829|PDB:2DZK"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:2DZK"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:2DZK"
SQ SEQUENCE 506 AA; 56472 MW; DD9CCC380F29C80F CRC64;
MLWFQGAIPA AIASAKRSGA VFVVFVAGDD EQSIQMAASW EDEKVTQASS NNFVAIKIDT
KSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSVSAD ELVTRIHKVQ QMHSSKGEAS
VTNDNQSESS VSTPSASFEP DVCENPESKN TELCETPATS DIKSDTATGG ECTGHDSHSQ
EPHGCSNQRP AEDLTVRVER LTKKLEERRE EKRKEEAQRE IKKEIERRKT GKEMLDYKRK
QEEELTKRML EERSREKAED RAARERIKQQ IALDRAERAA RFAKTKEAEA AKAAALLTKQ
AGTEVKREST ARDRSTIARI QFRLPDGSSF TNQFPSDAPL EEARQFAAQT VGNTYGNFSL
ATMFPRREFT REDYKRRLLD LELAPSASVV LLPAGRPATS IVHSSSGDIW TLLGTVLYPF
LAIWRLISNF LFSNPPPAQT SARATSTEPS NSASSSKSEK REPVRKRMLE KRGEDFKKEG
KIYRLRTQDD GEDENNTWNG NSTQQM
