ID A0A2I0MBL7_COLLI Unreviewed; 2050 AA.
AC A0A2I0MBL7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=TRIP12 {ECO:0000313|EMBL:PKK27071.1};
GN ORFNames=A306_00007671 {ECO:0000313|EMBL:PKK27071.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK27071.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK27071.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK27071.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins.
CC {ECO:0000256|RuleBase:RU369009}.
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; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
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:PKK27071.1}.
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DR EMBL; AKCR02000022; PKK27071.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:PKK27071.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 786..862
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1653..2050
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1090
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2017
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2050 AA; 227211 MW; FA4439204C438845 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDAV GGRSHLGQAK HKAHSPPESR KSISKTPKVQ
SNTTSEQSKG HFSKRGCSSS ALLIPQEDPE RVNTSDKQKT GQVLKKDNSR GVKRSASPDY
RRTNSPSSAK KPKALQNTEP SLESNKPHTK SKRRHLDQEQ PKSTQLPSTS KAHTRKGGAV
GSSRSQKRKR TENLSCXGAE EKSAKLSKLA SKSVTSAKAG CSTITDSSSS ASTSSSSSAV
ASASSTVPQG ARVKQGKDQN KARRSRSASS PSPRRSSRDK EPSKTSGSSK FDWAARFSPK
VSLPKTKLSL PGSSKSETSK PGPSGLQAKL ASLRKSTKKR SESPPAELPS LRRSTRQKTT
GSCASTSRRG SGLGKRGAAE ARRQEKMADP DNNQDGVNSS AARTDEAPQG AAASSSVAGA
VGMTTSGESE SDDSEMGRLQ ALLEARGLPP HLFGPLGPRM SQLFHRTIGS GASSKAQQLL
QGLQATDESQ QLQAVIEMCQ LLVMGNEETL GGFPVKSVVP ALITLLQMEH NFDIMNHACR
ALTYMMEALP RSSAVVVDAI PVFLEKLQVI QCIDVAEQAL TALEMLSRRH SKAILQAGGL
ADCLLYLEFF SINAQRNALA IAANCCQSIT PDEFHFVADS LPLLTQRLTH QDKKSVESTC
LCFARLVDNF QHEENLLQQV ASKDLLTNIQ QLLVVTPPIL SSGMFIMVVR MFSLMCSNCP
TLAVQLMKQN IAETLHFLLC GASNGSCQEQ IDLVPRSPQE LYELTSLICE LMPCLPKEGI
FAVDTMLKKG NAQNTDGAIW QWRDDRGLWH PYNRIDSRII EAAHQVGEDE ISLSTLGRVY
TIDFNSMQQI NEDTGTARAI QRKPNPLANT NTSGHSELKK DDARAQLMKE DPELAKSFIK
TLFGVLYEVY SSSAGPAVRH KCLRAILRII YFADAELLKD VLKNHAVSSH IASMLSSQDL
KIVVGALQMA EILMQKLPDI FSVYFRREGV MHQVKNLAES EALLTSPPKV CTNGSGTLGT
TTISTGTATA ASNAAADLGS PSLQHSREDS LDLSPQGRLS DVLKRKRLPK RGPRRPKYSP
PRDDDKVDNQ AKSPTTTQSP KSSFLASLNP KTWGRLSTQS NSNNIEPART AGVSGLARAA
SKDTISNNRE KIKGWIKEQA HKFVERYFSS ENMDGSNPAL NVLQRLCTAT EQLNLQVDGG
TECLVEIRSI VSESDVSSFE IQHSGFVKQL LLYLTSKSEK DAVSRDIRLK RFLHVFFSSP
LPGEEPLGRL EPLENAPLLA LVHKMNNCLS QMEQFPVKVH DFPSGNGTGS RGSQALKFFN
THQLKCQLQR HPDCANVKQW KGGPVKIDPL ALVQAIERYL VVRGYGRVRE DDEDSDDDGS
DEEIDESLAA QFLNSGNVRH RLQFYIGDHL LPYNMTVYQA VRQYSLQAEE ERESTDDESN
PLGRAGIWTK THTIWYKPVR EDEDGSKDCV GGKRGRAQTA PTKTSPRNSK KHDELWHDGV
CPSVLNPLEV YLISTPPENI TFEDPSLDVI LLLRVLHAIS RYWYYLYDNA ICKEIIPTSE
FINSKLTAKA NRQLQDPLVI MTGNIPTWLT ELGKTCPFFF PFDTRQMLFY VTAFDRDRAM
QRLLDTNPEI NQSDSQDSRV APRLDRKKRT VNRDELLKQA ESVMQDLGSS RAMLEIQYEN
EVGTGLGPTL EFYALVSQEL QRADLGLWRG EEVTLANPKG NQEGTKYIHN LQGLFALPFG
RTAKPAHIAK VKMKFRFLGK LMAKAIMDFR LVDLPLGLPF YKWMLRQETS LTSHDLFSID
PVVAKSIYHL EDIVRQKKRL EQDKTQTKES LQYALEALTM NGCSVEDLGL DFTLPGFPNI
ELKKGGKDTP VTIHNLEEYL RLVIFWALNE GVARQFDSFR DGFESVFPLS HLQYFYPEEL
EQLLCGSKTD TWDAKTLMEC CRPDHGYTHD SRAVKYLFEI LSSFDSEQQR LFLQFVTGSP
RLPVGGFRSL NPPLTIVRKT FESTENPDDF LPSVMTCVNY LKLPDYSTIE IMREKLLIAA
REGQQSFHLS
//
