ID A0A2R8ZRV7_PANPA Unreviewed; 1705 AA.
AC A0A2R8ZRV7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN Name=UBR1 {ECO:0000313|Ensembl:ENSPPAP00000007263.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000007263.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000007263.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000007263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; AJFE02014773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02014782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000029457.1; ENSPPAP00000007263.1; ENSPPAG00000026281.1.
DR GeneTree; ENSGT00950000183075; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000240080; Chromosome 15.
DR Bgee; ENSPPAG00000026281; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd19678; UBR-box_UBR1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR047507; UBR-box_UBR1.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF27; E3 UBIQUITIN-PROTEIN LIGASE UBR1; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 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; ClpS-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 97..168
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 835..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1705 AA; 195400 MW; BED10613AF7E6FDA CRC64;
MADEEAGGTE RMEISAELPQ TPQRLASWWD QQVDFYTAFL HHLAQLVPEI YFAEMDPDLE
KQEESVQMSI FTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
CVLCMDCFQN SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVNHEPGR AGTIKENSRC
PLNEEVIVQA RKIFPSVIKY VVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH
VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGAYAACQ EAKEDIKSHS ENVSQHPLHV
EVLHSEIMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL REEPDSENPC LISRLMLWDA
KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ KEYISDDHDR SISITALSVQ
MFTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK
YILISKPTIW TERLRMQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
QLKNILLMFQ EWCACDEELL LVAYKECHKA VMRCSTSFIS SSKTVVQSCG HSLETKSYRV
SEDLVSIHLP LSRTLAGLHV RLSRLGAVSR LHEFVSFEDF QVEVLVEYPL RCLVLVAQVV
AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS LMDPNKFLLL VLQRYELAEA
FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTKEEVTMR EIIHLLCIEP
MPHSAIENNE TGLENVINKV ATFKKPGVSG HGVYELKDES LKDFNMYFYH YSKTQHSKAE
HMQKKRRKQE NKDEALPPPP PPEFCPAFSK VINLLNCDIM MYILRTVFER AIDTDSNLWT
EGMLQMAFHI LALGLLEEKQ QLQKAPEEEV TFDFYHKASR LGSSAMNIQM LLEKLKGIPQ
LEGQKDMITW ILQMFDTVKR LREKSCLIVA TTSGSESIKN DEITHDKEKA ERKRKAEAAR
LHRQKIMAQM SALQKNFIET HKLMYDNTSE MPGKEDSIME EESTPAVSDY SRIALGPKRG
PSVTEKEVLT CILCQEEQEV KIENNAMVLS ACVQKSTALT QHRGKPIELS GEALDPLFMD
PDLAYGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC PLCKSLCNTV
IPIIPLQPQK INSENADALA QLLTLARWIQ TVLARISGYN IRHAKGLIFI FKIIIVLKYG
LIKYSNSIKE MVILFATTIY RIGLKVPPDE TDPRVPMLTW STCAFTIQAI ENLLGDEGKP
LFGALQNRQH NGLKALMQFA VAQRITCPQV LIQKHLVLMT LSYVSLLSLV GAVLAFPSLY
WDDPVDLQPS SVSSSYNHLY LFHLITMAHM LQILLTVDTG LPLAQVQEDR EEAHSASSFF
AEISQYTSGS IGCDIPGWYL WVSLKNGITP YLRCAALFFH YLLGVTPPEE LHTNSAEGEY
SALCSYLSLP TNLFLLFQEY WDTVRPLLKR WCADPALINC LKYPRKRNSL IELPDDYSCL
LNQASHFRCP RSADDERKHP VLCLFCGAIL CSQNICCQEI VNGEEVGACI FHALHCGAGV
CIFLKIRECR VVLVEGKARG CAYPAPYLDE YGETDPGLKR GNPLHLSRER YRKLHLVWQQ
HCIIEEIARS QETNQMLFGF NWQLL
//
