HRD1_SCHPO
ID HRD1_SCHPO Reviewed; 677 AA.
AC O74757;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
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; ORFNames=SPBC17D11.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH SRE1.
RX PubMed=19520858; DOI=10.1074/jbc.m109.002436;
RA Hughes B.T., Nwosu C.C., Espenshade P.J.;
RT "Degradation of sterol regulatory element-binding protein precursor
RT requires the endoplasmic reticulum-associated degradation components Ubc7
RT and Hrd1 in fission yeast.";
RL J. Biol. Chem. 284:20512-20521(2009).
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). Together with
CC ubc7, required for the degradation of the transcription factor sre1
CC precursor in the absence of its binding partner scp1. {ECO:0000250,
CC ECO:0000269|PubMed:19520858}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HRD1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21073.1; -; Genomic_DNA.
DR PIR; T39713; T39713.
DR RefSeq; NP_596376.1; NM_001022297.2.
DR AlphaFoldDB; O74757; -.
DR SMR; O74757; -.
DR BioGRID; 276446; 25.
DR STRING; 4896.SPBC17D11.02c.1; -.
DR iPTMnet; O74757; -.
DR PaxDb; O74757; -.
DR PRIDE; O74757; -.
DR EnsemblFungi; SPBC17D11.02c.1; SPBC17D11.02c.1:pep; SPBC17D11.02c.
DR GeneID; 2539900; -.
DR KEGG; spo:SPBC17D11.02c; -.
DR PomBase; SPBC17D11.02c; hrd1.
DR VEuPathDB; FungiDB:SPBC17D11.02c; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_436256_0_0_1; -.
DR InParanoid; O74757; -.
DR OMA; YEQFWIT; -.
DR PhylomeDB; O74757; -.
DR Reactome; R-SPO-5358346; Hedgehog ligand biogenesis.
DR UniPathway; UPA00143; -.
DR PRO; PR:O74757; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0010620; P:negative regulation of transcription by transcription factor catabolism; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..677
FT /note="ERAD-associated E3 ubiquitin-protein ligase hrd1"
FT /id="PRO_0000358324"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..39
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..140
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..225
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ZN_FING 292..351
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 379..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 677 AA; 75657 MW; 9CCC42CF77C66056 CRC64;
MKFILYVLAS LVLFGLSVLL SLYSSANVYS ATVMISQSPV HITIGLNVCL CLFFAIANAL
KTLLFGSLQT FELELLYEQF WITLTEIMLA ITVFREAISI SFFMLLSTLM FARVFHSICS
FRTERLQIQL TDQRFHIFSR LTCAYFVLSI LDASLIYLCF TSEHLGDKST RMLFVCEFSV
LLLNLTIEAS KLCIYLYEAR HLDQVWDEKS TYLFRLEVCR DGLRLLAYSL LFMYQFPYVS
VPIYSIRQMY TCFYSLFRRI REHARFRQAT RDMNAMYPTA TEEQLTNSDR TCTICREEMF
HPDHPPENTD EMEPLPRGLD MTPKRLPCGH ILHFHCLRNW LERQQTCPIC RRSVIGNQSS
PTGIPASPNV RATQIATQVP NPQNTPTTTA VPGITNSSNQ GDPQASTFNG VPNANSSGFA
AHTQDLSSVI PRRIALRDGW TMLPIPGTRR IPTYSQSTST TNPSATPTTG DPSNSTYGGP
QTFPNSGNNP NFNRGIAGIV PPGWRLVSSN TQSLSTNSAM TSLYQNASSA DNNLGSSLPN
VVPLSRGLTQ SNETSNTFPA ASSNISSQLR ELHTKIDELR ETVSNFRADY NSIRTSLNQL
EAASGINERI QTTSADSLLN SNGMSGTEGF ENTQTSITTN DNQSSILTSS DQTSPFATDE
DRQNSRNVQL ETVDENF
