ID   HERP1_PONAB             Reviewed;         391 AA.
AC   Q5R5B0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein;
GN   Name=HERPUD1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858911; CAH91109.1; -; mRNA.
DR   EMBL; CR860953; CAH93056.1; -; mRNA.
DR   RefSeq; NP_001125648.1; NM_001132176.2.
DR   AlphaFoldDB; Q5R5B0; -.
DR   SMR; Q5R5B0; -.
DR   STRING; 9601.ENSPPYP00000008334; -.
DR   GeneID; 100172567; -.
DR   KEGG; pon:100172567; -.
DR   CTD; 9709; -.
DR   eggNOG; KOG4583; Eukaryota.
DR   HOGENOM; CLU_058243_0_0_1; -.
DR   InParanoid; Q5R5B0; -.
DR   OMA; PEVQHNQ; -.
DR   OrthoDB; 1251727at2759; -.
DR   TreeFam; TF324319; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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_0000280633"
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          100..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          318..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Polar 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;  43632 MW;  2E378B3D39DC96F2 CRC64;
     MESETEPEPV TLLVKSPNQR HRDLELSGDR GWSVGHLKAH LSRVYPERPR PEDQRLIYSG
     KLLLDHQCLR DLLPKQEKRH VLHLVCNVKS PSKMPEINAK VAESTEEPAG SNRGQYPEDS
     SSDGLRQREV LRNLSSPGWE NISRPEAAQQ AFQGLGPGFS GYTPYGWLQL SWFQQIYARQ
     YYMQYLAATA ASGAFVPPPS AQEIPVVSAP APAPIHNQFP AENQPANQNA APQVVVNPGA
     NQNLRMNAQG GPIVEEDDEI NRDWLDWTYS AATFSVFLSI LYFYSSLSRF LMVMGATVVM
     YLHHVGWFPF RPRPVQNFPN DGPPPDIVNQ DPNNNLQEGT DPETEDPNHV PPDRGVLDGE
     QTGPSFMSTA WLVFKTFFAS LLPEGPPAIA N