ID   TRI10_BOVIN             Reviewed;         489 AA.
AC   Q5E9G4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Tripartite motif-containing protein 10;
GN   Name=TRIM10;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 between 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; BT020956; AAX08973.1; -; mRNA.
DR   EMBL; BC114866; AAI14867.1; -; mRNA.
DR   RefSeq; NP_001015607.1; NM_001015607.1.
DR   AlphaFoldDB; Q5E9G4; -.
DR   SMR; Q5E9G4; -.
DR   STRING; 9913.ENSBTAP00000009909; -.
DR   PaxDb; Q5E9G4; -.
DR   GeneID; 515628; -.
DR   KEGG; bta:515628; -.
DR   CTD; 10107; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; Q5E9G4; -.
DR   OrthoDB; 423686at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..489
FT                   /note="Tripartite motif-containing protein 10"
FT                   /id="PRO_0000244603"
FT   DOMAIN          292..486
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         94..135
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          142..245
FT                   /evidence="ECO:0000255"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   489 AA;  56377 MW;  FA4AA34F980090C0 CRC64;
     MASAASVTSL ADEVNCPVCQ GTLREPVTID CGHNFCRVCL TRYLEITSPD PEEPPTCPLC
     KEPFRPGNFR PNWQLANVVE NIERLKLVSQ MDLDEEDVCP EHGEKVYFFC EDDEMQLCVV
     CREAWEHRAH TVRFLEDAAG PYREQIQKCL ECLRKEREEI QEIQSRENRR IQVLLTQVAT
     KKQKVISEFA HLSQFLEEQQ NILLDQLEKL DEDILKHRDE FDVLVTGEIG RFNTLIEELE
     EKKERPAREL LTDIRSTLIR CETRRCRKPV AISPELGQRI RDFPQQAFPL QREMKMFLEK
     LSFELDYEPA HISLDPRTSH PKLLLSEDYQ QARFSYKWQK SPDNPQRFDR ATCVLAHGGF
     TGGRHTWVVS VDLAHGGSCT LGVVSKDIRR KGELRMRPEE GVWAVRLAWG FVSALSSFPT
     RLTLEEQPQQ VRVSIDYEVG WVTFANAVTQ EPIYTFTASF TQKVFPFFGL WGRGSKFSLS
     SQEGAATLS