ID K7F055_PELSI Unreviewed; 647 AA.
AC K7F055;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM32 {ECO:0000313|Ensembl:ENSPSIP00000001415.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000001415.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000001415.1}
RP IDENTIFICATION.
RG Ensembl;
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; AGCU01071929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006121113.1; XM_006121051.2.
DR RefSeq; XP_006121114.1; XM_006121052.2.
DR RefSeq; XP_006121115.1; XM_006121053.2.
DR RefSeq; XP_006121116.1; XM_006121054.2.
DR RefSeq; XP_006121117.1; XM_006121055.2.
DR RefSeq; XP_006121118.1; XM_006121056.2.
DR RefSeq; XP_014428001.1; XM_014572515.1.
DR AlphaFoldDB; K7F055; -.
DR STRING; 13735.ENSPSIP00000001415; -.
DR Ensembl; ENSPSIT00000001419.1; ENSPSIP00000001415.1; ENSPSIG00000001419.1.
DR GeneID; 102447668; -.
DR KEGG; pss:102447668; -.
DR CTD; 22954; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160949; -.
DR HOGENOM; CLU_423860_0_0_1; -.
DR OMA; YTTDGHC; -.
DR OrthoDB; 5295945at2759; -.
DR TreeFam; TF331018; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005863; C:striated muscle myosin thick filament; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0017022; F:myosin binding; IEA:Ensembl.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007014; P:actin ubiquitination; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:1903886; P:positive regulation of chemokine (C-C motif) ligand 20 production; IEA:Ensembl.
DR GO; GO:1903883; P:positive regulation of interleukin-17-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR CDD; cd19806; Bbox1_TRIM32_C-VII; 1.
DR CDD; cd14961; NHL_TRIM32_like; 1.
DR CDD; cd16587; RING-HC_TRIM32_C-VII; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR047051; TRIM32_Bbox1_Znf.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25464:SF3; E3 UBIQUITIN-PROTEIN LIGASE TRIM32; 1.
DR PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR Pfam; PF01436; NHL; 3.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 18..63
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 93..136
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 352..395
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 409..452
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 458..493
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 556..599
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 610..640
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 647 AA; 71940 MW; FDB6C3B090E7CF88 CRC64;
MATASHLNSD ALREVLECPI CMESFTEDQL RPKLLHCGHT ICKQCLEKLL ANSINGIRCP
FCSKITRITN LAQLTDNLTV LKIIDTTGLC EAVGLFMCKV CGRRLPRHFC KSCNLVLCDP
CKETKHLQQG HGVVAIKEAA DERRKEFGAK LGRLRELMGD LQKRKTSLEG VSKDLQSRYK
AVLQDYSKEE RKIQEELARS RKFFTNSLSE VEKVNNQVME EQAYLLNIAE VQIVSRCDYF
LAKIKQGDIA LLEEAADEEE PEPTNSLPRE LTLQEVELLK VGHVGPLQIG QVVKKPRTVN
MEESLMETAA SSSFTFRETE VVQEETSLTP NSSPAKPRVP ETATSIQQCH FLKKMGSKGS
MPGMFNLPVS VHVTVQGEVL VADRGNFRIQ VFTRKGFLKE IRRSPSGIDS FVLSFLGADL
PNLTPLSVTM NCHGLIGVTD SYDNSVKVYT MDGHCVACHR SQLSKPWGIT ALPSGQFVVT
DVEGGKLWCF TVDRGVGVVK YSCLCSAVRP KFVTCDSEGT VYFTQGLGLN LENRQHEHHL
EGGFSIGSVG PDGQLGRQIS HFFSENEDFR CIAGMCVDAR GDLIVADSSR KEILHFPKGG
GYNILIREGL TCPVGIAITP KGQLLVLDCW DHCIKIYSYH LRRYSTP
//