TRI10_PANTR
ID TRI10_PANTR Reviewed; 481 AA.
AC Q7YR32; Q1XHU7; Q1XHU9;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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; BA000041; BAC78185.1; -; Genomic_DNA.
DR EMBL; AB210201; BAE92821.1; -; Genomic_DNA.
DR EMBL; AB210202; BAE92823.1; -; Genomic_DNA.
DR RefSeq; NP_001065287.1; NM_001071819.1.
DR AlphaFoldDB; Q7YR32; -.
DR SMR; Q7YR32; -.
DR STRING; 9598.ENSPTRP00000030567; -.
DR PaxDb; Q7YR32; -.
DR GeneID; 742346; -.
DR KEGG; ptr:742346; -.
DR CTD; 10107; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q7YR32; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF342569; -.
DR Proteomes; UP000002277; Unplaced.
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; IPR027370; Znf-RING_LisH.
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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..481
FT /note="Tripartite motif-containing protein 10"
FT /id="PRO_0000056213"
FT DOMAIN 292..481
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..177
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 481 AA; 55113 MW; 67FACDDD78DEDE52 CRC64;
MASAASVTSL ADEVNCPICQ GTLREPVTID CGHNFCRACL TRYCEIPGPD LEESPTCPLC
KEPFRPGSFR PNWQLANVVE NIERLQLVST LGLGEEDVCQ EHGEKIYFFC EDDEMQLCVV
CREAGEHATH TMRFLEDAAA PYREQIHKCL KRLRKEREET QEIQSRENKR MQVLLTQVST
KRQQVISEFA HLRKFLEEQQ SILLAQLESL DGDILKQRDE FDLLIAGESC RFSALIEELE
EKNERPAREL LTDIRSTLIR CETRKCRKPV AVSPELGQRI RDFPQQALPL QREMKMFLEK
LCFELDYEPA HISLDPQTSH PKLLLSEDHQ RAQFSYKWQN SPDNPQRFDR ATCVLAHTGI
TGGRHTWVVS IDLAHGGSCT VGVVSEDVQR KGELRLRPEE GVWAVRLAWG FVSALGSFPT
RLTLKEQPWQ VRVSLDYEVG WVTFTNAVTR EPIYTFTASF TRKVIPFFGL WGRGSSFFLS
S
