ID   HUL4_YEAST              Reviewed;         892 AA.
AC   P40985; D6VWK9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HUL4;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT ubiquitin ligase 4;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HUL4;
GN   Name=HUL4; OrderedLocusNames=YJR036C; ORFNames=J1608;
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=7668047; DOI=10.1002/yea.320110809;
RA   Huang M.-E., Chuat J.-C., Galibert F.;
RT   "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT   genes and 14 new open reading frames including a gene most probably
RT   belonging to the family of ubiquitin-protein ligases.";
RL   Yeast 11:775-781(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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 362-892.
RX   PubMed=7957102; DOI=10.1002/j.1460-2075.1994.tb06871.x;
RA   van Gool A.J., Verhage R., Swagemakers S.M.A., van de Putte P., Brouwer J.,
RA   Troelstra C., Bootsma D., Hoeijmakers J.H.J.;
RT   "RAD26, the functional S. cerevisiae homolog of the Cockayne syndrome B
RT   gene ERCC6.";
RL   EMBO J. 13:5361-5369(1994).
RN   [5]
RP   GENE NAME, AND GENE DISRUPTION.
RX   PubMed=9858558; DOI=10.1128/mcb.19.1.342;
RA   Wang G., Yang J., Huibregtse J.M.;
RT   "Functional domains of the rsp5 ubiquitin-protein ligase.";
RL   Mol. Cell. Biol. 19:342-352(1999).
RN   [6]
RP   IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND FUNCTION OF THE TRF4 COMPLEX.
RX   PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
RA   Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
RA   Langen H., Keith G., Keller W.;
RT   "A new yeast poly(A) polymerase complex involved in RNA quality control.";
RL   PLoS Biol. 3:986-997(2005).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase, component of the TRAMP
CC       (TRF4) complex which has a poly(A) RNA polymerase activity and is
CC       involved in a post-transcriptional quality control mechanism limiting
CC       inappropriate expression of genetic information. Polyadenylation is
CC       required for the degradative activity of the exosome on several of its
CC       nuclear RNA substrates. {ECO:0000269|PubMed:15828860}.
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=2.3.2.26;
CC   -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC       composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
CC       {ECO:0000269|PubMed:15828860}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the HUL4 family. {ECO:0000305}.
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DR   EMBL; L36344; AAA88738.1; -; Genomic_DNA.
DR   EMBL; Z49536; CAA89563.1; -; Genomic_DNA.
DR   EMBL; X81635; CAA57291.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08825.1; -; Genomic_DNA.
DR   PIR; S57055; S57055.
DR   RefSeq; NP_012570.3; NM_001181694.3.
DR   AlphaFoldDB; P40985; -.
DR   SMR; P40985; -.
DR   BioGRID; 33789; 57.
DR   ComplexPortal; CPX-1678; TRAMP complex variant 4-1.
DR   ComplexPortal; CPX-1679; TRAMP complex variant 4-2.
DR   IntAct; P40985; 1.
DR   MINT; P40985; -.
DR   STRING; 4932.YJR036C; -.
DR   PaxDb; 4932-YJR036C; -.
DR   PeptideAtlas; P40985; -.
DR   EnsemblFungi; YJR036C_mRNA; YJR036C; YJR036C.
DR   GeneID; 853494; -.
DR   KEGG; sce:YJR036C; -.
DR   AGR; SGD:S000003797; -.
DR   SGD; S000003797; HUL4.
DR   VEuPathDB; FungiDB:YJR036C; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   GeneTree; ENSGT00940000163989; -.
DR   HOGENOM; CLU_002173_5_1_1; -.
DR   InParanoid; P40985; -.
DR   OMA; YGNDWHI; -.
DR   OrthoDB; 5471864at2759; -.
DR   BioCyc; YEAST:G3O-31673-MONOMER; -.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 853494; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40985; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40985; Protein.
DR   GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR   GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:SGD.
DR   GO; GO:0000292; P:RNA fragment catabolic process; NAS:ComplexPortal.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..892
FT                   /note="Probable E3 ubiquitin-protein ligase HUL4"
FT                   /id="PRO_0000084094"
FT   DOMAIN          792..892
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          31..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        860
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   CONFLICT        362
FT                   /note="H -> Q (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        410
FT                   /note="T -> M (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418
FT                   /note="T -> I (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514..519
FT                   /note="GKSVDV -> RQIRRR (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589..607
FT                   /note="ESSRSWFAIDPPNFDKSKG -> KKAHVHGLPLTLQILTNQR (in Ref.
FT                   4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        705
FT                   /note="V -> A (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723..724
FT                   /note="KH -> ND (in Ref. 4; CAA57291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   892 AA;  103457 MW;  35EF9A8DDA92BD84 CRC64;
     MVSLFDKLNA KKDGRDGSVS KELLSHSVAH TKNRLPKSGR RTSERSLAAS VKDGSCSNSK
     SNKRNSSASV SGEEDKSCLI SLNCLCCGVP LRFPASITKF RCSACQVTVI VKEPEINSNL
     ESSTHISCTL EGLQMVVRRC HDDLQRLKKT GILDKERKGL IFQPVITYLL DRFHDVSILN
     RSFLVHDGGK NIKMLNYEVL QRFYSILSNL PTRKPYYSML CCCNDLLKRI TINKGENLQI
     LQYRWLLIIL NIPTIRTCLI RDRKSKNVFE TQQIRAVSYE LAKRCIGYLS NLSTKTSQQL
     IQSLRRTPTD NFSYQVEILN LYINFQFSRL LSNELSNRTA KNNVKPEDEM RSRLRRHHTT
     GHEFLSTRPI SAQSNDKQGS GFTHPVNNKM KFKFFQYEED WHIHSAAKLT FIYYVANTRR
     NGRGALSIQS FYNITLDFID YKQDFDHWRG VAQKTKMNQL IEEWGNSTTK KCFSFCKYPF
     ILSLGIKISI MEYEIRRIME HEAEQAFLIS LDKGKSVDVY FKIKVRRDVI SHDSLRCIKE
     HQGDLLKSLR IEFVNEPGID AGGLRKEWFF LLTKSLFNPM NGLFIYIKES SRSWFAIDPP
     NFDKSKGKNS QLELYYLFGV VMGLAIFNST ILDLQFPKAL YKKLCSEPLS FEDYSELFPE
     TSRNLIKMLN YTEDNFEDVF SLTFETTYRN NNWILNDSKS SKEYVTVELC ENGRNVPITQ
     SNKHEFVMKW VEFYLEKSIE PQYNKFVSGF KRVFAECNSI KLFNSEELER LVCGDEEQTK
     FDFKSLRSVT KYVGGFSDDS RAVCWFWEII ESWDYPLQKK LLQFVTASDR IPATGISTIP
     FKISLLGSHD SDDLPLAHTC FNEICLWNYS SKKKLELKLL WAINESEGYG FR
//