TUL1_YEAST
ID TUL1_YEAST Reviewed; 758 AA.
AC P36096; D6VXQ1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transmembrane E3 ubiquitin-protein ligase 1;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TUL1 {ECO:0000305};
DE Flags: Precursor;
GN Name=TUL1; OrderedLocusNames=YKL034W; ORFNames=YKL247;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8203146; DOI=10.1002/yea.320100112;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "Analysis of an 11.7 kb DNA fragment of chromosome XI reveals a new tRNA
RT gene and four new open reading frames including a leucine zipper protein
RT and a homologue to the yeast mitochondrial regulator ABF2.";
RL Yeast 10:125-130(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-570.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1481573; DOI=10.1002/yea.320081108;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT reveals five new open reading frames, including a zinc finger protein and a
RT homolog of the UDP-glucose pyrophosphorylase from potato.";
RL Yeast 8:977-986(1992).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBC4.
RX PubMed=11788821; DOI=10.1038/ncb743;
RA Reggiori F., Pelham H.R.B.;
RT "A transmembrane ubiquitin ligase required to sort membrane proteins into
RT multivesicular bodies.";
RL Nat. Cell Biol. 4:117-123(2002).
RN [6]
RP FUNCTION.
RX PubMed=15973437; DOI=10.1038/sj.emboj.7600724;
RA Valdez-Taubas J., Pelham H.R.B.;
RT "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its
RT ubiquitination and degradation.";
RL EMBO J. 24:2524-2532(2005).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE DSC E3 UBIQUITIN LIGASE COMPLEX.
RX PubMed=25078903; DOI=10.1074/mcp.m114.040774;
RA Tong Z., Kim M.S., Pandey A., Espenshade P.J.;
RT "Identification of candidate substrates for the Golgi Tul1 E3 ligase using
RT quantitative diGly proteomics in yeast.";
RL Mol. Cell. Proteomics 13:2871-2882(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=29355480; DOI=10.7554/elife.33116;
RA Yang X., Arines F.M., Zhang W., Li M.;
RT "Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome
RT system.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Catalytic component of the DSC E3 ubiquitin ligase complexes
CC that tag proteins present in Golgi, endosome and vacuole membranes and
CC function in protein homeostasis under non-stress conditions and support
CC a role in protein quality control (PubMed:25078903, PubMed:29355480).
CC Mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12
CC and other proteins containing exposed hydrophilic residues within their
CC transmembrane domains, leading to their sorting into internal vesicles
CC in late endosomes (PubMed:11788821). Targets also the unpalmitoylated
CC endosomal SNARE TLG1 to the MVB pathway (PubMed:15973437).
CC {ECO:0000269|PubMed:11788821, ECO:0000269|PubMed:15973437,
CC ECO:0000269|PubMed:25078903, ECO:0000269|PubMed:29355480}.
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: Component of the DSC E3 ligase complexes composed of at least
CC TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized
CC complex or GLD1 for the Golgi/endosome-localized complex
CC (PubMed:25078903, PubMed:29355480). Interacts with UBC4
CC (PubMed:11788821). {ECO:0000269|PubMed:11788821,
CC ECO:0000269|PubMed:25078903, ECO:0000269|PubMed:29355480}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11788821}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11788821}.
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DR EMBL; X71622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X69584; CAA49298.1; -; Genomic_DNA.
DR EMBL; Z28034; CAA81869.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09121.1; -; Genomic_DNA.
DR PIR; S37855; S37855.
DR RefSeq; NP_012890.1; NM_001179600.1.
DR AlphaFoldDB; P36096; -.
DR BioGRID; 34097; 105.
DR ComplexPortal; CPX-1190; TUL1 E3 ubiquitin ligase complex.
DR DIP; DIP-5413N; -.
DR IntAct; P36096; 4.
DR STRING; 4932.YKL034W; -.
DR MaxQB; P36096; -.
DR PaxDb; P36096; -.
DR PRIDE; P36096; -.
DR EnsemblFungi; YKL034W_mRNA; YKL034W; YKL034W.
DR GeneID; 853832; -.
DR KEGG; sce:YKL034W; -.
DR SGD; S000001517; TUL1.
DR VEuPathDB; FungiDB:YKL034W; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_1_0_1; -.
DR InParanoid; P36096; -.
DR OMA; VFSPDCG; -.
DR BioCyc; YEAST:G3O-31837-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P36096; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36096; protein.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
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 Golgi apparatus; Membrane; Metal-binding; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..758
FT /note="Transmembrane E3 ubiquitin-protein ligase 1"
FT /id="PRO_0000056409"
FT TOPO_DOM 27..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..458
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..553
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..635
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 699..752
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 758 AA; 87880 MW; F29A61E994F96628 CRC64;
MEIDGNTLVF IIVILFLFFS SPGGDGVSSQ YEFNQLQRLK QQFRTEHNTF VNMTYTDSFR
NITGLKLSYQ DMLNNPLQNA TYPLPGKDYD RWFPNQNYMV LPNDVIEAIN TEVWNTSNDD
ASNLFPPNIT STLLGKIDLV SNNKYEKIRM PVPRFYEPAT DFSEDIPPEG ETYWSEWPSY
GELHNVSFQH GEIAIQISHM SNLQDNNNYL RRNFINKKND RWKLLNLQID FSDKAEKEKH
SIYSKAVYDI QRGRILSISQ SSKFHSLFAL PHYMSFQNDY NEKIFNDVKE LVDEFWNFTD
YTDVMTMKDV QDAYNNANFK CEYLIFLQLE PWNQYTRDQI KLIDDELNWP LGRPANLSSL
PPINVVSGLL YSPDCGVRLG LHNVKGTRYE LKIMSIRKHL LFGIALFAAQ IYLLLTQMHH
TNTPSMVNKI SFYCFSMINL VDGSLATLYF VAASVVPELY LPLVISAFSC FILASIFEIR
YLISIYASQV NEQNVGIINL LRGNTGTYDE NRPRPAFIPD EGSIGGSLYG RFFFMLIIFT
FLILSSTSWP RQLRMVFEYI LIFILNSYWI PQIFRNAVKG IPSRRERARS SIGGNRSQNK
MPLLWSFVIG TTIIRSLPVV YVFTYSSNVF RHHKDVHFVV FLSLWLLFQI SILYSQDVLG
SRWFLPKHTI PDGYSYFKPL SNEYISEHGG GTAEHTVDCA ICMSDVPIYI EEIPETHKVD
QHSYMVTPCN HVFHTSCLEN WMNYKLQCPV CRSPLPPL
