ID A0A341CGX6_NEOAA Unreviewed; 2000 AA.
AC A0A341CGX6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 10-JUN-2026, entry version 34.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TTC3 {ECO:0000313|RefSeq:XP_024614031.1};
OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS (Neophocaena phocaenoides subsp. asiaeorientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Neophocaena.
OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024614031.1};
RN [1] {ECO:0000313|RefSeq:XP_024614031.1}
RP IDENTIFICATION.
RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024614031.1};
RG RefSeq;
RL Submitted (JAN-2026) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_024614031.1; XM_024758263.1.
DR FunCoup; A0A341CGX6; 1652.
DR STRING; 1706337.A0A341CGX6; -.
DR GeneID; 112408586; -.
DR KEGG; nasi:112408586; -.
DR CTD; 7267; -.
DR InParanoid; A0A341CGX6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000252040; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR CDD; cd16481; RING-H2_TTC3; 1.
DR FunFam; 1.25.40.10:FF:000370; E3 ubiquitin-protein ligase TTC3; 1.
DR FunFam; 1.25.40.10:FF:000143; E3 ubiquitin-protein ligase TTC3 isoform X2; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_rpt.
DR InterPro; IPR056872; TTC3/DZIP3-like_helical.
DR InterPro; IPR056870; TTC3/DZIP3/RBM44-like_helical.
DR InterPro; IPR043866; TTC3/DZIP3_dom.
DR InterPro; IPR056871; WH_TTC3.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR17550; E3 UBIQUITIN-PROTEIN LIGASE TTC3; 1.
DR PANTHER; PTHR17550:SF4; E3 UBIQUITIN-PROTEIN LIGASE TTC3; 1.
DR Pfam; PF24525; TTC3; 1.
DR Pfam; PF24905; TTC3_9th; 1.
DR Pfam; PF19179; TTC3_DZIP3_dom; 1.
DR Pfam; PF24812; WHD_TTC3; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000252040};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1952..1991
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 436..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1491..1596
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1662..1724
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1031..1041
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1911..1925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2000 AA; 227035 MW; F3487A479375CB9A CRC64;
MDLGFVVSLG GCTMDDFALG NFTVADYALL EECPYVDDCV FASEFMSNDY VRVTQLYCDG
VGRQYKDYTQ SEGNLEFDIC TMWCSKPISI LQDYCDAIKI HVFWPLLFQR QHSSVISRLH
PCVEANSSHA SEISLKKLQH LELMEDIVDL AKKAANDSFF IGGLLRIGYK IENKILAMEE
ALNWVKYTGD VTILPRLGAV DNCWPMLSIF FTEYKYHITK VVTENCNLLE EFKTQSCAEC
LEQGELMKMK GNEEFSKERF DIAIIYYTRA IECRPENHLL YGNRALCFLR TGQFRNALGD
GKRAIILKNN WTKGHYRYCA ALSMLGEYDW ALQANIKAQK LCKNDPEGIK DLIQQHVKLQ
KQIEDLQGRT PTRNPIKAFY ESRAYIPSLS APAFSTSLNF VETEKNSRKP NHEMANGGNQ
NPKVADEALK VDDCDCHPEF LPPSSQPPKY KGKQKSRNNE LEKFSSGSQG SLPVDLKNIL
EKQFSKSSRA AHQDFANIMK MLRSLIQDGY TALLEQRCRS AAQAFTELLN GLDPQKIKQL
NLAMINYVLV VYGLAISLLG IGQPEELSEA ENQFKRMIEH YPNEGLDCLA YCGIGKVYLK
KNRFLEALNH FEKARTLICR LPGVLTWPTS NVVIEETQPG KIKMLLEKFI EECRFPPVPD
AICCYQKCRG YSKIQIYITD PDFKGFIRIS CCQYCKIEFH MNCWKKLKTT TFNDKIDKDF
LQGICLTPDC EGIISKIIIF SSGGQVKCEF EHKVIKEKVP PRPILKQKCS SLEKLRLKED
KKLKRKIQKK EAKKLAQERL EEDLRESNPP KIEEQKETVD SVQSCQFLDD RILQCIKQYA
DKIKSGILNT SKLLKELLSW KVLTTEDYTT CFSSRNFLNE AVDYVICHLV QEKNRVKTRV
FLHVLSELKE VEPKLATWIQ KLNSFGLDAT GPFFSRYGAA LKELDFSIMT FLWNEKYGHK
LGSIEGKQLD YFCEPASLKE ARCLIWLLEE HRDKFPALQN ALDEFFDIMD SRCIVLRRQD
SGDVPFNSTK IKNKGKKKKP KDSKPMLVGS GTTSVAPNNE TVTSGEDHNK RNSNSAGPFV
VPDHLRHDVE EFEALYEQHS NEYVVRNKKL WDINPKQKCS TLYDYFSQLL EEHGPLDMSN
KMFSEEYEFF PEETRQILEK AGGLKSFLLG CPRFVVIDNC IALKKVALRL KKKRKKKNIK
TKVEEISKTG EYLRVKLPLN PTAREFKPDV KSKPVSDLSS APASEDVKPH LTSANSPQSP
CEAVKPKLIS DNSSKSVSED EKPKGVSSDS PKPVSEETSH KHVTSNSPKP VTEDVKPTYW
TQPQLVTGYC TYLPFRGFDI TQTPPAFINV LPTLPQYSIY APLARVSSEY QLQRSIPVVP
SFVASDITEV RFEGHHFSAE NAPGNQIASE TQILQESLEI SVKSQCITDG ADTAQSESNR
NDDHCGNSAK QEVNPESTDE VTEIPHTQMV AVQVSRNVMH QEVNTEPYDP FEAQQGSISQ
IEKEYQVLQE QLKEACENYE QRNIKGSEET KDLEEKLKRH LEENKISKTE LDWFLEDLEK
EIKKWEQEKK EIQERLKALK KKMKKVLNAS EMYTQENAGK EKERELLLDQ SFEISNTFMN
EKMKIEECIK KEKEHYEESL QRAVDAEVSV LENWKETEVY KLQNMESQAE GFLKNLKLMS
SESAAYPVME SDIHSWESFL SNVREEIEKA KSQFEEQIEA IKNGSRLSEL SKVQISELSF
PACNTVHPKL LPESSDHDDQ GPSTSTSHRT GDRTAVPEES SLVSATGGPV ESPSCEPEAG
RLPECESAGQ AAQSEPSPVA DQKLPGAPGR ATRSSQSPKK PFNSIIEHLS VVFPCYSSTE
LAGFIKKVRN KNKNSLSGLS IDEIVQRVTE HILDEEKKKK PNPGKDRRPS EPSSAASVTR
ATQGPPSVLV GSSPESQGQK TDNVPVSGAN SCEICLEVFK SKNVRVLKCG HKFHKGCFKQ
WLKEQSTCPA CLARDLLSEE
//
