UBXN8_MOUSE
ID UBXN8_MOUSE Reviewed; 277 AA.
AC Q9QZ49;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=UBX domain-containing protein 8;
DE AltName: Full=Reproduction 8 protein;
DE Short=Rep-8 protein;
DE AltName: Full=UBX domain-containing protein 6;
GN Name=Ubxn8; Synonyms=D0H8S2298E, Rep8, Ubxd6;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=9931425; DOI=10.1016/s0378-1119(98)00598-8;
RA Yamabe Y., Yokoi A., Imamura O., Matsui M., Matsunaga A., Taketo M.,
RA Sugawara M., Furuichi Y.;
RT "Structures of mouse Rep-8 cDNA and genomic clones.";
RL Gene 227:39-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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=21949850; DOI=10.1371/journal.pone.0025061;
RA Madsen L., Kriegenburg F., Vala A., Best D., Prag S., Hofmann K.,
RA Seeger M., Adams I.R., Hartmann-Petersen R.;
RT "The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum
RT membrane for degradation of misfolded proteins.";
RL PLoS ONE 6:E25061-E25061(2011).
RN [4]
RP STRUCTURE BY NMR OF 182-277.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UBX domain of D0H8S2298E protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in endoplasmic reticulum-associated degradation
CC (ERAD) for misfolded lumenal proteins, possibly by tethering VCP to the
CC endoplasmic reticulum membrane. May play a role in reproduction (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SYVN1 and VCP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in gonads. In testis, expressed in
CC post-meiotic round spermatids, while in ovaries it is expressed in
CC granulosa cells. {ECO:0000269|PubMed:21949850}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both the early and late embryonic
CC stages of development. {ECO:0000269|PubMed:9931425}.
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DR EMBL; D88447; BAA84495.1; -; mRNA.
DR EMBL; BC024492; AAH24492.1; -; mRNA.
DR CCDS; CCDS22234.1; -.
DR PDB; 2CR5; NMR; -; A=182-277.
DR PDBsum; 2CR5; -.
DR AlphaFoldDB; Q9QZ49; -.
DR SMR; Q9QZ49; -.
DR STRING; 10090.ENSMUSP00000092992; -.
DR iPTMnet; Q9QZ49; -.
DR PhosphoSitePlus; Q9QZ49; -.
DR EPD; Q9QZ49; -.
DR MaxQB; Q9QZ49; -.
DR PaxDb; Q9QZ49; -.
DR PRIDE; Q9QZ49; -.
DR ProteomicsDB; 298380; -.
DR MGI; MGI:1337129; Ubxn8.
DR eggNOG; KOG1363; Eukaryota.
DR InParanoid; Q9QZ49; -.
DR PhylomeDB; Q9QZ49; -.
DR ChiTaRS; Ubxn8; mouse.
DR EvolutionaryTrace; Q9QZ49; -.
DR PRO; PR:Q9QZ49; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QZ49; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR017247; UBXN8.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037632; UBX_Rep6; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..277
FT /note="UBX domain-containing protein 8"
FT /id="PRO_0000211034"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..33
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 193..269
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 64..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:2CR5"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:2CR5"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:2CR5"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2CR5"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2CR5"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2CR5"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2CR5"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2CR5"
SQ SEQUENCE 277 AA; 31555 MW; 0AC63ACC5C4F5FF9 CRC64;
MASRGVVGLF LLSALPLLCL ELRRGIPSLG IKDLILLSGR IFLLLALLTL VISVTTSWFN
SLKPSQGHLK EGEKENEKRR RLVRERQQEA QGEKASRYIE NVLKPQQEMK LKKLEERFYQ
MTGETWKLTA GHRLLEGDED SEFENSSQAS FETINGEAAR RQNLPKFSTE ISPAARPLLR
KEVPDLPEEP SETAEEVVTV ALRCPNGRVL RRRFFKSWNS QVLLDWMMKV GYHKSLYRLS
TSFPRRALEV EGGSSLEDIG ITVDTVLNVE EKEQSSQ
