DOA10_SCHPO
ID DOA10_SCHPO Reviewed; 1242 AA.
AC O60103;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase doa10;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase doa10 {ECO:0000305};
GN Name=doa10; Synonyms=ssm4; ORFNames=SPBC14F5.07;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, 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).
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 a broad range of substrates, including endoplasmic
CC reticulum membrane proteins (ERQC), soluble nuclear proteins and
CC soluble cytoplasmic proteins (CytoQC). Component of the doa10 ubiquitin
CC ligase complex, which is part of the ERAD-C pathway responsible for the
CC rapid degradation of membrane proteins with misfolded cytoplasmic
CC domains. Also recognizes the N-terminally acetylated residue of
CC proteins as degradation signal (degron).
CC {ECO:0000250|UniProtKB:P40318}.
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
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- SIMILARITY: Belongs to the DOA10/MARCH6 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19325.1; -; Genomic_DNA.
DR PIR; T39453; T39453.
DR RefSeq; NP_596733.1; NM_001022659.2.
DR AlphaFoldDB; O60103; -.
DR SMR; O60103; -.
DR BioGRID; 276403; 8.
DR STRING; 4896.SPBC14F5.07.1; -.
DR iPTMnet; O60103; -.
DR MaxQB; O60103; -.
DR PaxDb; O60103; -.
DR PRIDE; O60103; -.
DR EnsemblFungi; SPBC14F5.07.1; SPBC14F5.07.1:pep; SPBC14F5.07.
DR GeneID; 2539855; -.
DR KEGG; spo:SPBC14F5.07; -.
DR PomBase; SPBC14F5.07; doa10.
DR VEuPathDB; FungiDB:SPBC14F5.07; -.
DR eggNOG; KOG1609; Eukaryota.
DR HOGENOM; CLU_001266_1_0_1; -.
DR InParanoid; O60103; -.
DR OMA; ALYFQYD; -.
DR PhylomeDB; O60103; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O60103; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM: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; ISO:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 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..1242
FT /note="ERAD-associated E3 ubiquitin-protein ligase doa10"
FT /id="PRO_0000310692"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..165
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..495
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..612
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..710
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..806
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 828..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..1002
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1024..1054
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1055..1075
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1076..1089
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1090..1110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1111..1143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1179
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1180..1200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1201..1242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT ZN_FING 1..61
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1242 AA; 142366 MW; B9BD14AD2D476008 CRC64;
MNADDEICRV CRCEGAPDSP LFHPCKCTGS IRYVHQECLV EWLGHSKKTH CELCKAKFEF
TKVYSESMPR TIPFTILCRK LASTLKQRVI FFTRVLLTFF CWTVLLPLIF KHVWNLNFKI
GDTYTIHARN KTFTAPQKPG YFESISQITS SPRLNTLIAN TAEGQVLTFV VTFILITAFL
VREWVLQNAV QVADELQGQQ FENVNQNNQA QAAAAAAQNL REVREARQRL AMVMEHLRER
QEQRNLELQR NGSFEEIERA RQRFALLGDN IREPQEEEND VDVDEIFNRQ QLNQPALDLN
DANSSNSVPV EFNSLHSQNV DYRDEVDSLR PQFNVDEQSS ISHSSNASEN IVDGAVTQAN
GIESDFTRVD HEPIIVNNDD ENGNNESENE EVIEEDNLNR NVIAEAQNQV VADEERNAVA
RAAQIAEADD ADDFDGILEF LGLRGPITGF LQNCLVIAFV VSVFLTTAVG IPYMSGRLMV
EWILFIIHRP TFILRFILSF VNILFDWTVG GAFNIVKILT KLPLLSTVFV KLKLQGIFSS
SFQQVSNNMY SWIYDHVFSS SDHAYESLIY YMKTGHKQVV QSFSIFPVFR VCQMFAVILK
DFVENYSNRP VDRVFTTLIG YCMFTFLGIS YLNRKQFLFN DPQIRNVELA FREVLRQCGS
IAKFGIIFSI ELVVFPIFCG ILLSMCLIGT FKKLAAENLL NVMTVYPAQS IFLAWFIGIT
FMFEFAVFIS MVRKIVRPGV LYFLRDPNDP QFHPIREILE KPMLFQLKKI GFSAILYFAF
IIGCVGSVIH LLKSTGIIFP IEFTTKPAVF EAPIDLLALE ILIFLSIKLF KPLELTRSFW
RTLVSTFCRC LRLSSYVMGQ RYSDEEGYYP KQYFSFLRRI ISKPSDTENQ DDGDKQKAKK
DFVQDGFFLW CPSKDVVPVR QGAMLIPVTE NGYEIFGEKK KVEENADYTI TYAPSNFYKR
LIALLLFCWI CSTLVTVLLV FVPLSLGRAI YAWCFPNVVK HDFYAYAIGF YSISFPMYAI
HASVKFLKLD YLRSLMNKLN LKIVMRSLVM ALKYLLLAFL GIFILPLLLG AIWELYVAIP
FRTIFNRGTL ALDAFQNWVI GLFMLRMIYF TVTSNEERFV SRLFQDAFRD RWTNPQILPL
LKNVLIPFTS ALIAAVVLPS VFTYVTYPFL SSIFPSASKT LMYRLMHPIF LALLGLALLG
RRFVETSSKW SQGIRDDLYL VGTRLHNFGE SAPPAISESA EK
