MUD1_SCHPO
ID MUD1_SCHPO Reviewed; 332 AA.
AC Q10256;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=UBA domain-containing protein Mud1 {ECO:0000303|PubMed:11584278};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q5TDH0};
DE AltName: Full=DNA-damage-inducible protein DDI1 homolog {ECO:0000303|PubMed:16138082};
DE AltName: Full=UBA domain-containing protein 1 {ECO:0000303|PubMed:11584278};
GN Name=mud1 {ECO:0000303|PubMed:11584278};
GN Synonyms=ddi1 {ECO:0000303|PubMed:16138082},
GN ucp1 {ECO:0000303|PubMed:11584278};
GN ORFNames=SPAC56F8.08 {ECO:0000312|PomBase:SPAC56F8.08};
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 FUNCTION, AND SUBUNIT.
RX PubMed=11584278; DOI=10.1038/ncb1001-939;
RA Wilkinson C.R.M., Seeger M., Hartmann-Petersen R., Stone M., Wallace M.,
RA Semple C., Gordon C.;
RT "Proteins containing the UBA domain are able to bind to multi-ubiquitin
RT chains.";
RL Nat. Cell Biol. 3:939-943(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 293-332, FUNCTION, SUBUNIT,
RP DOMAIN, SITES, AND MUTAGENESIS OF PHE-330.
RX PubMed=16138082; DOI=10.1038/sj.emboj.7600797;
RA Trempe J.F., Brown N.R., Lowe E.D., Gordon C., Campbell I.D., Noble M.E.,
RA Endicott J.A.;
RT "Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA
RT domain.";
RL EMBO J. 24:3178-3189(2005).
CC -!- FUNCTION: Recognizes and binds polyubiquitin chains (PubMed:11584278,
CC PubMed:16138082). Acts as a linker between the 19S proteasome and
CC polyubiquitinated proteins via UBA domain interactions with ubiquitin
CC for their subsequent degradation. Aspartic protease. Appears to act as
CC negative regulator of constitutive exocytosis. May act at the level of
CC secretory vesicle docking and fusion as a competitive inhibitor of
CC SNARE assembly. Required for S-phase checkpoint control (By
CC similarity). {ECO:0000250|UniProtKB:P40087,
CC ECO:0000269|PubMed:11584278, ECO:0000269|PubMed:16138082}.
CC -!- SUBUNIT: Homodimer (PubMed:16138082). Interacts (via UBA domain) with
CC polyubiquitin (polyUb) chains (via Lys-48-linked polyUbs)
CC (PubMed:11584278, PubMed:16138082). Has weak binding affinity for
CC monoubiquitin (PubMed:16138082). According to another report, has no
CC affinity for monoubiquitin (PubMed:11584278).
CC {ECO:0000269|PubMed:11584278, ECO:0000269|PubMed:16138082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40087}. Cell
CC membrane {ECO:0000250|UniProtKB:P40087}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P40087}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P40087}.
CC -!- DOMAIN: The UBA domain specifically recognizes Lys-48-linked
CC diubiquitin units (Ub2), which is mediated by the two binding sites
CC within a single UBA domain. {ECO:0000269|PubMed:16138082}.
CC -!- SIMILARITY: Belongs to the DDI1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93579.1; -; Genomic_DNA.
DR PIR; T38918; T38918.
DR RefSeq; NP_001018195.1; NM_001018619.2.
DR PDB; 1Z96; X-ray; 1.80 A; A/B=293-332.
DR PDBsum; 1Z96; -.
DR AlphaFoldDB; Q10256; -.
DR SMR; Q10256; -.
DR BioGRID; 280553; 12.
DR MINT; Q10256; -.
DR STRING; 4896.SPAC56F8.08.1; -.
DR MEROPS; A28.A06; -.
DR iPTMnet; Q10256; -.
DR MaxQB; Q10256; -.
DR PaxDb; Q10256; -.
DR EnsemblFungi; SPAC56F8.08.1; SPAC56F8.08.1:pep; SPAC56F8.08.
DR GeneID; 3361477; -.
DR KEGG; spo:SPAC56F8.08; -.
DR PomBase; SPAC56F8.08; mud1.
DR VEuPathDB; FungiDB:SPAC56F8.08; -.
DR eggNOG; KOG0012; Eukaryota.
DR HOGENOM; CLU_020435_2_0_1; -.
DR InParanoid; Q10256; -.
DR OMA; PCRFTVI; -.
DR PhylomeDB; Q10256; -.
DR EvolutionaryTrace; Q10256; -.
DR PRO; PR:Q10256; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:PomBase.
DR GO; GO:0000149; F:SNARE binding; ISO:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:PomBase.
DR CDD; cd05479; RP_DDI; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF09668; Asp_protease; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cell membrane; Cytoplasm; Hydrolase;
KW Membrane; Protease; Protein transport; Reference proteome; Transport.
FT CHAIN 1..332
FT /note="UBA domain-containing protein Mud1"
FT /id="PRO_0000096643"
FT DOMAIN 291..332
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 246..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /evidence="ECO:0000250|UniProtKB:Q5TDH0"
FT SITE 303
FT /note="Involved in interaction with monoubiquitin"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 306
FT /note="Involved in interaction with monoubiquitin"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 307
FT /note="Involved in interaction with monoubiquitin"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 308
FT /note="Involved in interaction with monoubiquitin and Lys-
FT 48-linked diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 316
FT /note="Involved in interaction with monoubiquitin"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 318
FT /note="Involved in interaction with Lys-48-linked
FT diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 319
FT /note="Involved in interaction with Lys-48-linked
FT diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 320
FT /note="Involved in interaction with monoubiquitin and Lys-
FT 48-linked diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 327
FT /note="Involved in interaction with Lys-48-linked
FT diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 328
FT /note="Involved in interaction with Lys-48-linked
FT diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 330
FT /note="Involved in interaction with monoubiquitin"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 331
FT /note="Involved in interaction with monoubiquitin and Lys-
FT 48-linked diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT SITE 332
FT /note="Involved in interaction with monoubiquitin and Lys-
FT 48-linked diubiquitin (Ub2)"
FT /evidence="ECO:0000269|PubMed:16138082"
FT MUTAGEN 330
FT /note="F->A: 20-fold reduction in binding affinity for Lys-
FT 48-linked diubiquitin (Ub2) compared to that of the wild-
FT type. Significantly reduced binding affinity also for Lys-
FT 48-linked triubiquitin (Ub3) and tetraubiquitin (Ub4).
FT Slightly reduced binding affinity for monoubiquitin. No
FT effect on stability or structure of the UBA domain."
FT /evidence="ECO:0000269|PubMed:16138082"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:1Z96"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:1Z96"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:1Z96"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:1Z96"
SQ SEQUENCE 332 AA; 35870 MW; 47E7514CF9DA3502 CRC64;
MNNLTPENIR QTILATPFLL NRIRTEFPQL AAVLNDPNAF ATTWQSINAS QLLQIPSSTY
SMGMPSFSED DLFDVEVQRR IEEQIRQNAV TENMQSAIEN HPEVFGQVYM LFVNVEINGH
KVKAFVDSGA QATILSADCA EKCGLTRLLD TRFQGVAKGV GMAKILGCVH SAPLKIGDLY
LPCRFTVIEG RDVDMLLGLD MLRRYQACID LENNVLRIHG KEIPFLGESE IPKLLANVEP
SANAHGLGIE PASKASASSP NPQSGTRLGT KESVAPNNEG SSNPPSLVNP PTDPGLNSKI
AQLVSMGFDP LEAAQALDAA NGDLDVAASF LL
