ID   HRD3_SCHPO              Reviewed;         713 AA.
AC   Q9USV0; P78930; P78931;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative ERAD-associated E3 ubiquitin-protein ligase component;
DE   Flags: Precursor;
GN   ORFNames=SPBC28F2.08c;
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 [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RA   Kohnosu A., Niwa O., Yano M., Saitoh S., Katayama T., Nagao K.,
RA   Yanagida M.;
RT   "S.pombe chromosome II cosmid 1228 sequence.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: Component of the endoplasmic reticulum quality control (ERQC)
CC       system involved in ubiquitin-dependent degradation of missfolded
CC       endoplasmic reticulum proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sel-1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12178.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA12179.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D83992; BAA12178.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; D83992; BAA12179.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CU329671; CAB57937.1; -; Genomic_DNA.
DR   PIR; T40051; T40051.
DR   RefSeq; NP_595669.1; NM_001021564.2.
DR   AlphaFoldDB; Q9USV0; -.
DR   SMR; Q9USV0; -.
DR   BioGRID; 277095; 12.
DR   STRING; 4896.SPBC28F2.08c.1; -.
DR   MaxQB; Q9USV0; -.
DR   PaxDb; Q9USV0; -.
DR   PRIDE; Q9USV0; -.
DR   EnsemblFungi; SPBC28F2.08c.1; SPBC28F2.08c.1:pep; SPBC28F2.08c.
DR   GeneID; 2540568; -.
DR   KEGG; spo:SPBC28F2.08c; -.
DR   PomBase; SPBC28F2.08c; -.
DR   VEuPathDB; FungiDB:SPBC28F2.08c; -.
DR   eggNOG; KOG1550; Eukaryota.
DR   HOGENOM; CLU_386442_0_0_1; -.
DR   InParanoid; Q9USV0; -.
DR   OMA; SLAYWRL; -.
DR   PhylomeDB; Q9USV0; -.
DR   PRO; PR:Q9USV0; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
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:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR   Gene3D; 1.25.40.10; -; 2.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF08238; Sel1; 7.
DR   SMART; SM00671; SEL1; 6.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..713
FT                   /note="Putative ERAD-associated E3 ubiquitin-protein ligase
FT                   component"
FT                   /id="PRO_0000350745"
FT   TRANSMEM        671..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          83..124
FT                   /note="Sel1-like 1"
FT   REPEAT          125..160
FT                   /note="Sel1-like 2"
FT   REPEAT          212..248
FT                   /note="Sel1-like 3"
FT   REPEAT          280..315
FT                   /note="Sel1-like 4"
FT   REPEAT          490..525
FT                   /note="Sel1-like 5"
FT   REPEAT          527..562
FT                   /note="Sel1-like 6"
FT   REGION          621..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        149
FT                   /note="V -> G (in Ref. 1; BAA12178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        317
FT                   /note="S -> P (in Ref. 1; BAA12178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="I -> L (in Ref. 1; BAA12178)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   713 AA;  80260 MW;  58ADF7EDE319E6F8 CRC64;
     MQLLNFLICL FFIFKRCVFT VIGGEFSYDN IDKKPILVAS YPEGSRFNVS ASIKTLPDLV
     TLTFPKLVKD PGYVYEEAEK GDPESQFLIA MLYAMGPDER LGLSFPRNEP LSRIFLELSA
     TQNYTYALLA LAYKHLNGLS TPMSVDKGVE LYKQVAHQIS CLVQPLSHFA PDIAAEYPVD
     LYDLSRTSSY SVQKKDDIVE YLKDYALRGN NISAHISLAT IYQYGTPGKL KDIKLAVKHY
     LAAIRLVNSG IPDSPSEAIK SIHNNPRHAP TTKETANSLS IAAFRLGCMA LHGELGKPDP
     SLAYAWFEYG VSLNHSSSKA AIAYMYFMGY PVAENTESIT KLLENALASN DPLAFAVAGK
     VSLANGQIDE ATVHLIRAVS NGHLESVLHI ADIYYGSNNQ LSIAYYENFI SRVLELFDVK
     TISFDPLTRH FAHRLSAELG NLMSQILAAK DRDPSTSYLK TVIFPTNEQT HRNARIAMNY
     YSRAAARNHI HSLIKIGDFY RMGLGTSAKP ELAFSYYSQA AAIHPSALAY WRLGWMHEYG
     VGVPVDFEMA KKNYDNALMH DTRAFLAVTL ARLRMRLSSP DSWFSNIYRI LGKVTYKFLK
     LVQYFIINIF DILSPAGPDS QLPPEPPTLQ VDRTPQQPDP QETSESLPSP NTEEMGESYN
     DIRFTYDYID GRFLETACVT LIVVVVGLVL MRRHQQHRLQ ERRERIIRRQ NRA