(data stored in ACNUC7421 zone)

SWISSPROT: HRD1_ASHGO

ID   HRD1_ASHGO              Reviewed;         575 AA.
AC   Q75CC8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=ERAD-associated E3 ubiquitin-protein ligase HRD1;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase HRD1 {ECO:0000305};
GN   Name=HRD1; OrderedLocusNames=ACL019C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 179.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin
CC       specifically from endoplasmic reticulum-associated E2 ligases, and
CC       transfers it to substrates promoting their degradation. Mediates the
CC       degradation of endoplasmic reticulum proteins (ERQC), also called ER-
CC       associated degradation (ERAD). Component of the HRD1 ubiquitin ligase
CC       complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC       for the rapid degradation of soluble lumenal and membrane proteins with
CC       misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC       misfolded transmembrane domains (ERAD-M) (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with HRD3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
DR   EMBL; AE016816; AAS51209.2; -; Genomic_DNA.
DR   RefSeq; NP_983385.2; NM_208738.2.
DR   STRING; 33169.AAS51209; -.
DR   PRIDE; Q75CC8; -.
DR   EnsemblFungi; AAS51209; AAS51209; AGOS_ACL019C.
DR   GeneID; 4619510; -.
DR   KEGG; ago:AGOS_ACL019C; -.
DR   InParanoid; Q75CC8; -.
DR   KO; K10601; -.
DR   OMA; ICREDMH; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CC8.
DR   SWISS-2DPAGE; Q75CC8.
KW   Endoplasmic reticulum; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..575
FT                   /note="ERAD-associated E3 ubiquitin-protein ligase HRD1"
FT                   /id="PRO_0000240366"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        5..25
FT                   /note="Helical; Name=1"
FT   TOPO_DOM        26..46
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        47..67
FT                   /note="Helical; Name=2"
FT   TOPO_DOM        68..79
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        80..100
FT                   /note="Helical; Name=3"
FT   TOPO_DOM        101..103
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        104..124
FT                   /note="Helical; Name=4"
FT   TOPO_DOM        125..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=5"
FT   TOPO_DOM        160..179
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        180..200
FT                   /note="Helical; Name=6"
FT   TOPO_DOM        201..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   ZN_FING         320..368
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   575 AA;  65420 MW;  C4B3C901EBFA5F74 CRC64;
     MPREVSWPMW AMFITATYAL AGWSAYSCAT SFDDPLSALF MASSGVHFVI WGNFLIVHYC
     LFVWAIIRVL FGQLTAIEYD HIFERLHVVL VTLASIVITM RKTYMAGHMT ILFYTLCLVA
     HWVLRDRMDF VFQVHGTDSS LLGILCSRFM FSLLVLGMVD YKMLKFCVQN TNVDGKRHDL
     YLMLALSFAQ LILDVLHVVL LTSLNLFEMV RSRRTRSANL VYEGGTTDDD ADDEVFILEG
     KYIYETVFDL TITVLKVILD IIQEVFVPWS ITVVYSIFVR SIKAGESFLL VYNYWKNNKK
     LYEKLSDVSE EQLDDTDSMC IICMDDMLPT TETTKMNRRA KMLPCGHMLH FGCLKSWMER
     SQTCPICRLS VFANDSNSHA TTQAREQTPP DLLQERGIDE HIDVIGMQDM SVQSISLHEG
     TAVRRGTTGN CMNQAYDGGL LSHEERDQAG WVAFPIEFRA DNKVFFNLND SQGDRQWMAS
     YTSYPRQNMV NSDDPDNASE SHSRIPSPSL PGSLEGTSSQ VDVTVSAKDA PANACFVIAT
     SKLEQTKEVE HLKRKVEELE SRVEELSKRI KTDQV
//

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