ID A0A5N5N416_PANHP Unreviewed; 1740 AA.
AC A0A5N5N416;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=PHYPO_G00015990 {ECO:0000313|EMBL:KAB5562270.1};
OS Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Pangasiidae; Pangasianodon.
OX NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5562270.1, ECO:0000313|Proteomes:UP000327468};
RN [1] {ECO:0000313|EMBL:KAB5562270.1, ECO:0000313|Proteomes:UP000327468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indonesia {ECO:0000313|EMBL:KAB5562270.1,
RC ECO:0000313|Proteomes:UP000327468};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB5562270.1};
RA Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA Schartl M., Guiguen Y.;
RT "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT hypophthalmus.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Interacts with RECQL4. {ECO:0000256|ARBA:ARBA00062088}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the E3 ubiquitin-protein ligase UBR1-like
CC family. {ECO:0000256|ARBA:ARBA00046341, ECO:0000256|RuleBase:RU366018}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB5562270.1}.
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DR EMBL; VFJC01000011; KAB5562270.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000327468; Chromosome 10.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:TreeGrafter.
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 FunFam; 3.30.1390.10:FF:000005; E3 ubiquitin-protein ligase UBR1 isoform X2; 1.
DR FunFam; 2.10.110.30:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform 1; 1.
DR FunFam; 1.10.10.2670:FF:000001; E3 ubiquitin-protein ligase UBR2 isoform X1; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR003769; ClpS_core.
DR InterPro; IPR042065; E3_ELL-like.
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; IPR055194; UBR1-like_WH.
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; PF22960; WHD_UBR1; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000327468};
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|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU366018}.
FT DOMAIN 88..159
FT /note="UBR-type"
FT /evidence="ECO:0000259|PROSITE:PS51157"
FT ZN_FING 88..159
FT /note="UBR-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00508"
FT REGION 835..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1740 AA; 197166 MW; B935EAF9463002E9 CRC64;
MAEGEGPVNA LQLCTRWWEA SDQRSAILQY LAEKVPQIYC LQAEPQLVKE EERVQECILQ
PLEYFLFGED PSVGLEKLQQ RNGSSSSQLC GRVFKEGETV YSCRDCAIDP TCVLCMDCFQ
NSVHKSHRYK MHASSGGGFC DCGDLEAWKT GPCCSQHDSG TTIAMETDEC VLEAALQERA
QVLFQVLLQY ITDLMVWEEG DELPEEMEPR SKENTYYCVL YNDEHHSYDH VIYTLQRAIN
CNSTEAQAHT VLIDKEGRRA VRRGSLRSCQ QAKELIRTSS EHITQQPLRV ELLHSVVMAH
QTFALRLGTW FQQITGYSVG FRQVFCQVAL EPSADSSKPC LISRLMLHDA RLYKGARKVI
HELIFCSLLM ETEYKRQFAM KFTELYKQLQ EDFIRDDHER NISITALSVQ IFTVPTLARQ
LIEEGNVIKV IIETVMEMLR EHLDSNQRFH FQGYNSDKFL RVQVIFHDLK YILISKPTVW
TDQLRGKFLE GFTVFLGFLN CMQGMEEVKR QVGQHIEVEP EWEAGFTIQI QLRHILSMFQ
DWCSSDERVL LLAFQECHRA LQRCTNQPFH SEPTDRYMCK HILHTRSYKV SQEPVSIHLP
ITRLLAGLYV LLCRTGAVKY LPDFVDPEQM DLPFFAEFPL RCVVLAAQVS AEMWRRNGLS
LVSQVYYYQD VKCRDEMFDK DIIMLQIAAS KMDPNHFVML ILLRFELFEV FNGNCSSKDQ
DLQKQWNRLT EEMLYLLIII TGERYVPGVS NVTKEEVTMR EVIHLLCIEP MAHSSMVKAL
PENENQETGL ETVISKVATF KKPGVSGHGL YELKKECLKE FNPFFYHYTK SQHSKAEDAQ
KKRRAQEGSD KALRPPVPPP FTQAFSSIVR LLCCDVFVHV LRRVLQRAVE ERSALWTEAM
IQRALHLVGQ ALLEEKNQLE ACSVEEVTFD FSLKARKVGS DHGKSLFHFL SKMKSHPSLE
AHNDMINWTL QMFEIVKCLR EKSIPSASCA ADQTKAEESI HDKEKAERKR KAEAAKLHRQ
KIMAQMSAMQ KNFIETHKML YDNVPESGSQ GEPVVSTESS VMELESRVAV GPKQGVCPAD
WETLTCILCQ EEQEVQAQAP AMVLTACVQR STVLTQCRGK TLTPKESSYP LFVPPDLAVG
THTGSCGHVM HATCWQKYFE AVQNTTRNRL HAELIIDLEN GEYMCPLCKS LCNTVVPLVP
MEPSKLNYES AEMIGQFLTL PRWIQIVLAR IKGLRVLQGA ENTTETGKEE TGLLLEDTQT
DFRSILSFGV QPPPKYSSSI MEMLVVCATT VHRVGLQTAP NELCPYVPVM TWNTCAYTIQ
ATENMLQEEG KALFGSLQNR QLAGLKALVQ FSAIQRMKSS HSVIQKHFTE MLAVLLPVSN
AEGTPTILEV DFFNLLVGLV LSIPVLYQEE NVDLQPSAIS TAYNQQHLVH LVTMAHIVQV
LLSSQDLNAG AVGGGDAEEV RAAAALYSTV SQHTEGLKSG VSASMTVDTV KRGVLPFLRC
AALFFHCLTG VPAPEELSNA AVSSESQLSL LCSYLALPCN LFQLFQDHQD TATSLIQRWC
GNKAISDTLK GEMHIIRYPR TRNRLIDLPE DYSVLLNQAS HFKCPNSSDD ERKHPTLCLF
CGVMLCSQNP CCQVPLNGEG VGACTAHAAT CGAGVGMFLR VRECEIVLMA SRTRGSTYPA
PYLDEYGETD PQLNRGNPLH LCPERYRKLN QLWQQHCILE EIARSLEVLN VMFAFEWQML
//
