HERP1_MOUSE
ID HERP1_MOUSE Reviewed; 391 AA.
AC Q9JJK5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein;
GN Name=Herpud1;
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].
RX PubMed=10922362; DOI=10.1074/jbc.m002063200;
RA Kokame K., Agarwala K.L., Kato H., Miyata T.;
RT "Herp, a new ubiquitin-like membrane protein induced by endoplasmic
RT reticulum stress.";
RL J. Biol. Chem. 275:32846-32853(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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).
CC -!- FUNCTION: Component of the endoplasmic reticulum quality control (ERQC)
CC system also called ER-associated degradation (ERAD) involved in
CC ubiquitin-dependent degradation of misfolded endoplasmic reticulum
CC proteins. Binds to ubiquilins and this interaction is required for
CC efficient degradation of CD3D via the ERAD pathway.
CC {ECO:0000250|UniProtKB:Q15011}.
CC -!- SUBUNIT: Interacts with PSEN1 and PSEN2 (By similarity). Interacts with
CC UBXN6 (By similarity). Interacts with UBQLN1, UBQLN2 and UBQLN4 (By
CC similarity). Component of the HRD1 complex, which comprises at least
CC SYNV1/HRD1, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1. FAM8A1 binding
CC to SYNV1 may promote recruitment of HERPUD1 to the HRD1 complex (By
CC similarity). {ECO:0000250|UniProtKB:Q15011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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DR EMBL; AB034991; BAB07892.1; -; mRNA.
DR CCDS; CCDS22541.1; -.
DR RefSeq; NP_071726.1; NM_022331.1.
DR AlphaFoldDB; Q9JJK5; -.
DR SMR; Q9JJK5; -.
DR BioGRID; 211038; 3.
DR STRING; 10090.ENSMUSP00000124201; -.
DR iPTMnet; Q9JJK5; -.
DR PhosphoSitePlus; Q9JJK5; -.
DR EPD; Q9JJK5; -.
DR MaxQB; Q9JJK5; -.
DR PaxDb; Q9JJK5; -.
DR PRIDE; Q9JJK5; -.
DR ProteomicsDB; 269826; -.
DR Antibodypedia; 28691; 293 antibodies from 33 providers.
DR DNASU; 64209; -.
DR Ensembl; ENSMUST00000161576; ENSMUSP00000124201; ENSMUSG00000031770.
DR GeneID; 64209; -.
DR KEGG; mmu:64209; -.
DR UCSC; uc009mwg.1; mouse.
DR CTD; 9709; -.
DR MGI; MGI:1927406; Herpud1.
DR VEuPathDB; HostDB:ENSMUSG00000031770; -.
DR eggNOG; KOG4583; Eukaryota.
DR GeneTree; ENSGT00390000017671; -.
DR HOGENOM; CLU_058243_0_0_1; -.
DR InParanoid; Q9JJK5; -.
DR OMA; PEVQHNQ; -.
DR OrthoDB; 1251727at2759; -.
DR PhylomeDB; Q9JJK5; -.
DR TreeFam; TF324319; -.
DR BioGRID-ORCS; 64209; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Herpud1; mouse.
DR PRO; PR:Q9JJK5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JJK5; protein.
DR Bgee; ENSMUSG00000031770; Expressed in lacrimal gland and 266 other tissues.
DR ExpressionAtlas; Q9JJK5; baseline and differential.
DR Genevisible; Q9JJK5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:1990037; C:Lewy body core; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IMP:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
DR GO; GO:1902235; P:regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903069; P:regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031396; P:regulation of protein ubiquitination; IMP:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR InterPro; IPR039751; HERPUD1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12943; PTHR12943; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Unfolded protein response.
FT CHAIN 1..391
FT /note="Homocysteine-responsive endoplasmic reticulum-
FT resident ubiquitin-like domain member 1 protein"
FT /id="PRO_0000114921"
FT TOPO_DOM 1..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..289
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 10..72
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 90..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..200
FT /note="Interaction with UBQLN1"
FT /evidence="ECO:0000250|UniProtKB:Q15011"
FT REGION 317..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q15011"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15011"
SQ SEQUENCE 391 AA; 43907 MW; 7F707DBF9B1A3A12 CRC64;
MEPEPQPEPV TLLVKSPNQR HRDLELSGDR SWSVSRLKAH LSRVYPERPR PEDQRLIYSG
KLLLDHQCLQ DLLPKQEKRH VLHLVCNVKN PSKMPETSTK GAESTEQPDN SNQTQHPGDS
SSDGLRQREV LRNLSPSGWE NISRPEAVQQ TFQGLGPGFS GYTTYGWLQL SWFQQIYARQ
YYMQYLAATA ASGTFVPTPS AQEIPVVSTP APAPIHNQFP AENQPANQNA AAQAVVNPGA
NQNLRMNAQG GPLVEEDDEI NRDWLDWTYS AATFSVFLSI LYFYSSLSRF LMVMGATVVM
YLHHVGWFPF RQRPVQNFPD DGGPRDAANQ DPNNNLQGGM DPEMEDPNRL PPDREVLDPE
HTSPSFMSTA WLVFKTFFAS LLPEGPPALA N
