ID A0A2Y9PKC2_DELLE Unreviewed; 619 AA.
AC A0A2Y9PKC2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN Name=DTX2 {ECO:0000313|RefSeq:XP_022443726.1,
GN ECO:0000313|RefSeq:XP_022443727.1, ECO:0000313|RefSeq:XP_022443728.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022443727.1};
RN [1] {ECO:0000313|RefSeq:XP_022443726.1, ECO:0000313|RefSeq:XP_022443727.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022443726.1,
RC ECO:0000313|RefSeq:XP_022443727.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR RefSeq; XP_022443726.1; XM_022588018.2.
DR RefSeq; XP_022443727.1; XM_022588019.2.
DR RefSeq; XP_022443728.1; XM_022588020.1.
DR STRING; 9749.A0A2Y9PKC2; -.
DR Ensembl; ENSDLET00000011900; ENSDLEP00000010769; ENSDLEG00000007815.
DR KEGG; dle:111182014; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd09633; Deltex_C; 1.
DR CDD; cd16672; RING-H2_DTX2; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF21; E3 UBIQUITIN-PROTEIN LIGASE DTX2-RELATED; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 2.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 8..97
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 98..174
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 409..470
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 281..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 66573 MW; AB46D8AF8DA86C76 CRC64;
MAMAPSPSLA QVYTSPVAVA VWEWQDGLGT WHPYSATVCN YIEQQFVQQK GQRFGLGSLA
HSIPLGQADP SLAPYIIDLP SWTQFRQDTG TMRAVRRHLF PQHSAPGRGI VWEWLSDDGS
WTAYEASVCD YLEQQVARGA QLVDLAALGY NYTVNCATHT QTNKTSSFCR SVRRQAGPPY
PATTVIAPPG HTGVACSCHQ CLGGGAAGPV SGRYRHSMTN LPAYAVPQPP HRTAVVLGAH
QTFSPYNKPS LSGARSAPKL STANLWAGAL PSLGNQPLYR SSLSHLGPQH QPPGLSAAGA
ASASLPSGPV SSPRSVPATV PVQMSKPSRV QQALAGMTSI LMSAIGLPVC LSRAPQPASP
PASCLASKSH SSVKRLRKMS MKGGPPKPEP EQVIKNYTEE LKTALDEDCI ICMEKLSMAS
GYSDATDSKT FGPVAVGRLA KCSHAFHLLC LLAMYCNGNK DGSLQCPSCK TIYGEKTGTQ
PRGKMEVFTF QVSLPGHEDC GTILIVYNIP HGIQGPEHPN PGKPFTARGF PRQCYLPDNA
QGRKVLELLK VAWKRRLIFT VGTSSTTGET DTVVWNEIHH KTEMDRNVTG HGYPDPNYLQ
NVLAELAAQG VTEDCLQQQ
//
