TRI10_PIG
ID TRI10_PIG Reviewed; 482 AA.
AC O19085;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tripartite motif-containing protein 10;
DE AltName: Full=B30-RING finger protein;
DE AltName: Full=RING finger protein 9;
GN Name=TRIM10; Synonyms=RFB30, RNF9;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white;
RX PubMed=11685460; DOI=10.1007/s002510100348;
RA Renard C., Vaiman M., Chiannilkulchai N., Cattolico L., Robert C.,
RA Chardon P.;
RT "Sequence of the pig major histocompatibility region containing the
RT classical class I genes.";
RL Immunogenetics 53:490-500(2001).
CC -!- FUNCTION: E3 ligase that plays an essential role in the differentiation
CC and survival of terminal erythroid cells. May directly bind to PTEN and
CC promote its ubiquitination, resulting in its proteasomal degradation
CC and activation of hypertrophic signaling (By similarity). In addition,
CC plays a role in immune response regulation by repressing the
CC phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling
CC pathway independent of its E3 ligase activity. Mechanistically,
CC interacts with the intracellular domain of IFNAR1 and thereby inhibits
CC the association of TYK2 and IFNAR1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UDY6, ECO:0000250|UniProtKB:Q9WUH5}.
CC -!- SUBUNIT: Interacts with IFNAR1; this interaction prevents association
CC of IFNAR1 with TYK2. {ECO:0000250|UniProtKB:Q9UDY6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UDY6}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AJ251829; CAB63932.1; -; Genomic_DNA.
DR RefSeq; NP_001116679.1; NM_001123207.1.
DR AlphaFoldDB; O19085; -.
DR SMR; O19085; -.
DR STRING; 9823.ENSSSCP00000001312; -.
DR PaxDb; O19085; -.
DR Ensembl; ENSSSCT00005032235; ENSSSCP00005019642; ENSSSCG00005020408.
DR Ensembl; ENSSSCT00025038056; ENSSSCP00025016029; ENSSSCG00025028050.
DR Ensembl; ENSSSCT00035080976; ENSSSCP00035033435; ENSSSCG00035060362.
DR Ensembl; ENSSSCT00045038194; ENSSSCP00045026531; ENSSSCG00045022313.
DR Ensembl; ENSSSCT00050106083; ENSSSCP00050046805; ENSSSCG00050077097.
DR Ensembl; ENSSSCT00060108926; ENSSSCP00060048665; ENSSSCG00060078750.
DR Ensembl; ENSSSCT00065110146; ENSSSCP00065049596; ENSSSCG00065079230.
DR Ensembl; ENSSSCT00070049482; ENSSSCP00070041790; ENSSSCG00070024775.
DR GeneID; 100144459; -.
DR KEGG; ssc:100144459; -.
DR CTD; 10107; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; O19085; -.
DR OrthoDB; 423686at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd16593; RING-HC_TRIM10_C-IV; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042784; TRIM10_RING-HC.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
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 Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..482
FT /note="Tripartite motif-containing protein 10"
FT /id="PRO_0000056214"
FT DOMAIN 293..482
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 95..136
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 482 AA; 55462 MW; 309A2EC6960CBE14 CRC64;
MASAASVSSL ADEVNCPICQ GTLREPVTID CGHNFCCVCL TRYLEIPCLD PGELPTCPLC
KEPFRPGSFR PNWQLASVVE NIERLKLGSQ LGSEEEEDVC LEHREKVYYF CEDDEMQLCV
VCREAWEHRH HTVRFLEDAA GPYREQIQKC LECLRKEGEE IQRIQLRENQ RIQVLLTQVA
TKKQKVISEF AHLSQFLEEQ QSVLLAQLER LDGDILKHRD EFDVLVAGEI CRFNTLIEEL
EEKNQRPARD LLTDIRSTLI RCETRRCRKP EAVSPELGQR IRDFPQQALP LRREMKTFLE
KLCFELDYEP AHISLDPQTS HPKLLLSEDN QQARFSYKWQ NSPDNPQRFD RATCVLAHSG
FTEGRHTWVV SVDLAHGGSC TVGVVSQDIR RKGELRMRPE EGVWAVRLAW GFVSALGSFP
TRLALEEHPR QVRVSIDYEV GWVTFVNAVT QEPIYTFTAS FTQKVFPFFG LWGRGSKFSL
SS
