UBR1_CAEEL
ID UBR1_CAEEL Reviewed; 2058 AA.
AC P91133;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=E3 ubiquitin-protein ligase ubr-1;
DE EC=2.3.2.27;
DE AltName: Full=N-recognin-1;
DE AltName: Full=RING-type E3 ubiquitin transferase ubr-1;
DE AltName: Full=Ubiquitin-protein ligase E3-alpha;
GN Name=ubr-1 {ECO:0000312|WormBase:C32E8.11};
GN ORFNames=C32E8.11 {ECO:0000312|WormBase:C32E8.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP INTERACTION WITH UBC-1.
RX PubMed=14732404; DOI=10.1016/j.ydbio.2003.09.037;
RA Crowe E., Candido E.P.M.;
RT "Characterization of C. elegans RING finger protein 1, a binding partner of
RT ubiquitin-conjugating enzyme 1.";
RL Dev. Biol. 265:446-459(2004).
RN [3]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH CED-3 AND ATE-1, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 136-MET--GLU-163.
RX PubMed=28602583; DOI=10.1016/j.devcel.2017.05.013;
RA Weaver B.P., Weaver Y.M., Mitani S., Han M.;
RT "Coupled Caspase and N-End Rule Ligase Activities Allow Recognition and
RT Degradation of Pluripotency Factor LIN-28 during Non-Apoptotic
RT Development.";
RL Dev. Cell 41:665-673(2017).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 18-ARG--TRP-25;
RP 821-GLU--PHE-2058 AND 1864-GLN--PHE-2058.
RX PubMed=29649217; DOI=10.1371/journal.pgen.1007303;
RA Chitturi J., Hung W., Rahman A.M.A., Wu M., Lim M.A., Calarco J., Baran R.,
RA Huang X., Dennis J.W., Zhen M.;
RT "The UBR-1 ubiquitin ligase regulates glutamate metabolism to generate
RT coordinated motor pattern in Caenorhabditis elegans.";
RL PLoS Genet. 14:E1007303-E1007303(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end
CC rule pathway (By similarity). Recognizes and binds to proteins bearing
CC specific N-terminal residues that are destabilizing according to the N-
CC end rule, leading to their ubiquitination and subsequent degradation
CC (By similarity). In complex with ced-3, required for the ced-3-mediated
CC cleavage and subsequent degradation of the heterochronic protein lin-28
CC to regulate seam cell fate patterning during larval development
CC (PubMed:28602583). Negatively regulates glutamate metabolism through
CC the aspartate aminotransferase got-1.2 (PubMed:29649217). Modulation of
CC glutamate levels most likely controls locomotory behavior, in
CC particular backwards locomotion or 'reversals' (PubMed:29649217).
CC {ECO:0000250|UniProtKB:Q8IWV7, ECO:0000269|PubMed:28602583,
CC ECO:0000269|PubMed:29649217}.
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: Interacts with ubc-1 (Probable). Component of a complex
CC containing at least ced-3, ubr-1 and possibly ate-1 (PubMed:28602583).
CC Within complex interacts with ced-3 (via the p17 subunit); this
CC interaction is required for the ced-3-mediated cleavage and subsequent
CC degradation of the heterochronic protein lin-28 (PubMed:28602583).
CC {ECO:0000269|PubMed:28602583, ECO:0000305|PubMed:14732404}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal muscles, body wall muscles
CC and a subset of neurons throughout postembryonic development
CC (PubMed:29649217). Prominently expressed in premotor interneurons, but
CC not expressed in ventral cord motor neurons (PubMed:29649217). Weakly
CC expressed in hypodermal seam cells (PubMed:29649217).
CC {ECO:0000269|PubMed:29649217}.
CC -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a His
CC ligand in place of the fourth Cys of the classical motif.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown enhances the excessive
CC seam cell proliferation phenotype of the ain-1 ku322 mutant.
CC {ECO:0000269|PubMed:28602583}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000305}.
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DR EMBL; BX284601; CCD66417.1; -; Genomic_DNA.
DR PIR; T25604; T25604.
DR RefSeq; NP_491231.2; NM_058830.4.
DR AlphaFoldDB; P91133; -.
DR SMR; P91133; -.
DR BioGRID; 37427; 8.
DR IntAct; P91133; 1.
DR STRING; 6239.C32E8.11; -.
DR EPD; P91133; -.
DR PaxDb; P91133; -.
DR PeptideAtlas; P91133; -.
DR PRIDE; P91133; -.
DR EnsemblMetazoa; C32E8.11.1; C32E8.11.1; WBGene00016326.
DR GeneID; 171953; -.
DR KEGG; cel:CELE_C32E8.11; -.
DR UCSC; C32E8.11; c. elegans.
DR CTD; 171953; -.
DR WormBase; C32E8.11; CE40441; WBGene00016326; ubr-1.
DR eggNOG; KOG1140; Eukaryota.
DR GeneTree; ENSGT00950000183075; -.
DR HOGENOM; CLU_001801_2_0_1; -.
DR InParanoid; P91133; -.
DR OMA; ILCQEDQ; -.
DR OrthoDB; 81415at2759; -.
DR PhylomeDB; P91133; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P91133; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00016326; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:WormBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:2000212; P:negative regulation of glutamate metabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0043058; P:regulation of backward locomotion; IMP:UniProtKB.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IBA:GO_Central.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497; PTHR21497; 1.
DR Pfam; PF02617; ClpS; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..2058
FT /note="E3 ubiquitin-protein ligase ubr-1"
FT /id="PRO_0000056138"
FT TRANSMEM 1695..1715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 93..164
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT ZN_FING 1217..1335
FT /note="RING-type; atypical"
FT REGION 1107..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 18..25
FT /note="Missing: In hp820; animals are viable, but display
FT defective locomotion that progressively develops from the
FT late larval stage into adulthood. Animals are capable of
FT backwards locomotion or 'reversals' movements, but exhibit
FT limited body flexing, with decreased body curvature during
FT reversals, increased duration of reversals and a reduced
FT frequency of reversal initiation compared to wild-type.
FT Reduced bending is due to a defective activation pattern of
FT A class motor neurons, whereby the posterior clusters of A
FT class motor neurons DA7, VA10 and VA11, that innervate body
FT wall muscles to execute reversals, are activated at the
FT same time, which is in contrast to wild-type. Animals also
FT display morphological and synaptic activity defects in AVA
FT and AVE interneurons. Increases glutamate levels which is
FT likely through increased got-1.2 activity. Defective
FT reversals movement phenotype and increased glutamate levels
FT are rescued in the got-1.2 hp731 mutant."
FT /evidence="ECO:0000269|PubMed:29649217"
FT MUTAGEN 34..2058
FT /note="Missing: In hp821; animals are viable, but display
FT defective locomotion that progressively develops from the
FT late larval stage into adulthood. Animals are capable of
FT backwards locomotion or 'reversals' movements, but exhibit
FT limited body flexing, with decreased body curvature during
FT reversals, increased duration of reversals and a reduced
FT frequency of reversal initiation compared to wild-type.
FT Reduced bending is due to a defective activation pattern of
FT A class motor neurons, whereby the posterior clusters of A
FT class motor neurons DA7, VA10 and VA11, that innervate body
FT wall muscles to execute reversals, are activated at the
FT same time, which is in contrast to wild-type. Animals also
FT display morphological and synaptic activity defects in AVA
FT and AVE interneurons. Increases glutamate levels which is
FT likely through increased got-1.2 activity. Defective
FT reversals movement phenotype and increased glutamate levels
FT are rescued in the got-1.2 hp731 mutant."
FT /evidence="ECO:0000269|PubMed:29649217"
FT MUTAGEN 136..163
FT /note="Missing: In tm5996; increases lin-28 protein levels
FT 30 hours post feeding. Enhances the excessive seam cell
FT proliferation phenotype and enhances the delay in temporal
FT cell fate patterning of seam cells during the progression
FT of larval development of the ain-1 ku322 mutant."
FT /evidence="ECO:0000269|PubMed:28602583"
FT MUTAGEN 1864..2058
FT /note="Missing: In hp684; animals are viable, but display
FT defective locomotion that progressively develops from the
FT late larval stage into adulthood. Animals are capable of
FT backwards locomotion or 'reversals' movements, but exhibit
FT limited body flexing, with decreased body curvature during
FT reversals, increased duration of reversals and a reduced
FT frequency of reversal initiation compared to wild-type.
FT Reduced bending is due to a defective activation pattern of
FT A class motor neurons, whereby the posterior clusters of A
FT class motor neurons DA7, VA10 and VA11, that innervate body
FT wall muscles to execute reversals, are activated at the
FT same time, which is in contrast to wild-type. Animals also
FT display morphological and synaptic activity defects in AVA
FT and AVE interneurons. Increases glutamate levels which is
FT likely through increased got-1.2 activity. Defective
FT reversals movement phenotype and increased glutamate levels
FT are rescued in the got-1.2 hp731 mutant."
FT /evidence="ECO:0000269|PubMed:29649217"
SQ SEQUENCE 2058 AA; 232816 MW; DBAE0014CE89F7AC CRC64;
MIVDLIQSAR QGEWAQVRQL LLKHWLVQVP EVFEVNSDLP WDNTAANERI LGSQGEILLA
PLVSAFVLDV RNTKSTLEAM NGIAGVDPAR RGQICGHVFK NGELTYTCLD CATDGTCVMC
LQCFEVSIHK SHKYKMHSSS GSGYCDCGDA DAWTEGYACA NHEKKDDEEA AVLAPELKKR
CEQLVEIILQ FSLSMITHKD DLKLPEIFEK MKPEVTNEAQ QYLTVLYNDE THTYESVIKV
LELYIHCTKD QAMLVATIVD REGRSAVKLG SKADCTKAKD DVQRKTARDP TSIRRSSNHN
LPLSVKVMDT TLFALQNFSI SLLTWLNTQM DVFPPLREIV GEILLSSKFA LKKNYTRKMK
SEDQRLVAGI IRNVMVLPDD EEEELFALDG RMDVDEMDDD DIGGEALQME IDADDEEEIT
AALAGVSEHQ ESPGPSRDSS TFTMLENILL QDTQMWKAGR SILHQMLMRT VFMIYDQKVR
FAKAFMLHYN EIYEDFIKDD HEMDVSVVGL SVQFMTVPSL ARKLVAEDQA FSVISKAIRD
QTDKFVKYYN DGKIARFDFT SRSFPPELRR SLHITRDMAY ILNAVPSESD WNRELIDGFV
QGFADFLLFL QHLQGMDEVK RQAVEHQVWE SEWETAFNIL LRLKDAISMI IGWAETNEEV
HNRLMIMCLE LMNRMPPVYT KSEEDTYELT VTINGESCRI SHFDVLKSST SVHQPVVRII
AGLFSASNYT GFLLNRSNNS HTSLNQERIK ELINCKDETN LYELSLRVLV LCAQSNATLW
RRNGFSLINQ IHNYFSPLCR NEMFDRDVLM MQVGAALTPS TKFIFHLLHR FRLFKWATSE
FEQDKANEKP AKPESEDLSK TLVMIAEEFI QCLILILCER YTYGVGKTRP MDQMKREVIH
ILCTGSHTFS HIQQKMSHDI NSKRLSLHEA VNLVADFRKP LATTAGQFHC KESSLPTYSP
FFMHYSKSDQ SAAEQSQARV RAKMEKSVRA CAPPILPDFQ TFFERIPEIL TTNVLIHVVR
LIIDRTARRS RFSSDRLFHK TLYLIGIALN EEEKNPSFGF TQRAEESIGL LSLLEGLVGK
PESSICPILL EVTVEKYRKL IKARAGVPEA APAPENKPAQ SEEEIKAKRA ARAAEMRQKA
MAKMSNMQSK FMKKIEDEEK KDESQTPSEK SETVVKKDDY DNKHFFDEDV VKQVGHDFPV
CIGANKWHAE LVKPRTLTCI LCQEDEIIAP QQGKPMVCAA FIQQSQLFTH KNKNGELMTA
SSGTISTRDL LTAPATLQYG VDVSTCSHSM HYECYRSLAE ANRSRESLRA RQVGQHSHKM
VDTENGEYQC PLCKRLSNAA IPVLPAYQLT NQNGFSTVSG AGKENFDTWV ARVKRNLEMP
LSSESVSKKG HSRKRSHSER SLLDLEKLSK DPDTANTSAG VLQFGAMEMS SATHMPASAE
SQMLMTTSPS QDDVEFYNEL AAMFVDQDVN NTTSPAATPE TIPAIGSSSR IPESQESGKK
PLSSQIQHVL YSLIRPFPAL INSNRICSSS FEGFEEPIKD LGKNMMKFRK RGNELKTNFI
EKHLKGYVIS TVTWQSTAHV ARAISSYLHY DKKPLFGALN TRQRDCLSAM ARLCASLSHN
MQFLLHAVSD MLRVFLCEPP RPKLAQTPGS PLLSAPSTSS FTPAPAQIPH SGTNFAFLVQ
LFNPAGPRKN VNLNILQIDI LSLAISLMMT IGWTWNNGTQ SMNSSSTHQK ARLLTPDGSV
DEAYVLRLSL LAHYFQIIAT HSEADGNDVN MEEEQESQME VDPVAAQTIR KLYALCHPFD
GPLRRVDILW RKMEEGAQSL LRPIALLYHF ITLVDPPEAL KDPSINSSEP LFRYLGLPHK
IEEQISGSML EKLFTMWSSS IPSDQALRQD LVVQPVRPNL LVELPEKYSQ LINQVATFKC
PTIPIEESTS NVPTLCLVCG TILCSQAYCC QKIINKQSYG ACRYHMSQCS GSVGMFLRVR
DCSLVLMTTR KRGCFRPAPY VDEFGEVDQG FRRGNPLHLN PELYQKLKSL WLQQGITEEV
VNYNEIDFRN VQYDWGHF
