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TRI17_RAT
ID   TRI17_RAT               Reviewed;         477 AA.
AC   Q9WV59;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM17;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM17 {ECO:0000305};
DE   AltName: Full=Testis RING finger protein;
DE   AltName: Full=Tripartite motif-containing protein 17;
GN   Name=Trim17; Synonyms=Terf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9792805; DOI=10.1006/bbrc.1998.9502;
RA   Ogawa S., Goto W., Orimo A., Hosoi T., Ouchi Y., Muramatsu M., Inoue S.;
RT   "Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein,
RT   terf, expressed in the testis.";
RL   Biochem. Biophys. Res. Commun. 251:515-519(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin ligase that plays important roles in the
CC       regulation of neuronal apoptosis, selective autophagy or cell
CC       proliferation. Stimulates the degradation of kinetochore ZW10
CC       interacting protein ZWINT in a proteasome-dependent manner, leading to
CC       negative regulation of cell proliferation. Inhibits autophagic
CC       degradation of diverse known targets while contributing to autophagy of
CC       midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17
CC       assembles into complexes with the key autophagy regulator BECN1 (By
CC       similarity). Controls neuronal apoptosis by mediating ubiquitination
CC       and degradation of MCL1 to initiate neuronal death. In addition,
CC       regulates NFAT transcription factors NFATC3 and NFATC4 activities by
CC       preventing their nuclear localization, thus inhibiting their
CC       transcriptional activities. Decreases TRIM41-mediated degradation of
CC       ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in
CC       neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase
CC       activity of TRIM28 and its interaction with anti-apoptotic BCL2A1,
CC       blocking TRIM28 from ubiquitinating BCL2A1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q7TPM3, ECO:0000250|UniProtKB:Q9Y577}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (via coiled coil) with TRIM44 (via coiled coil).
CC       Interacts with TRIM28; this interaction prevents TRIM28 activity on
CC       BCL2A1 (By similarity). Interacts with TRIM41; this interaction
CC       prevents TRIM41 activity on ZSCAN2 (By similarity). Interacts with
CC       BECN1 (By similarity). Interacts with NFATC3 and NFATC4; these
CC       interactions prevent NFATC3 and NFATC4 nuclear localization (By
CC       similarity). {ECO:0000250|UniProtKB:Q7TPM3,
CC       ECO:0000250|UniProtKB:Q9Y577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y577}.
CC       Lysosome {ECO:0000250|UniProtKB:Q9Y577}.
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in the testis.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9Y577}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AF156272; AAD40287.1; -; mRNA.
DR   EMBL; BC078819; AAH78819.1; -; mRNA.
DR   PIR; JE0343; JE0343.
DR   RefSeq; NP_073635.1; NM_022798.2.
DR   AlphaFoldDB; Q9WV59; -.
DR   SMR; Q9WV59; -.
DR   STRING; 10116.ENSRNOP00000060549; -.
DR   PhosphoSitePlus; Q9WV59; -.
DR   PaxDb; Q9WV59; -.
DR   Ensembl; ENSRNOT00000003885; ENSRNOP00000003885; ENSRNOG00000022983.
DR   GeneID; 64702; -.
DR   KEGG; rno:64702; -.
DR   UCSC; RGD:69290; rat.
DR   CTD; 51127; -.
DR   RGD; 69290; Trim17.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162155; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q9WV59; -.
DR   OrthoDB; 423686at2759; -.
DR   PhylomeDB; Q9WV59; -.
DR   TreeFam; TF338674; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9WV59; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000022983; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q9WV59; baseline and differential.
DR   Genevisible; Q9WV59; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR   CDD; cd15812; SPRY_PRY_TRIM17; 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; IPR032918; TRIM17.
DR   InterPro; IPR035687; TRIM17_PRY/SPRY.
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   PANTHER; PTHR24103:SF397; PTHR24103:SF397; 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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Lysosome; Metal-binding; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..477
FT                   /note="E3 ubiquitin-protein ligase TRIM17"
FT                   /id="PRO_0000056226"
FT   DOMAIN          276..475
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..66
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          135..225
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   477 AA;  54954 MW;  1AAB42BB02615ADF CRC64;
     MDAVELARRL QEEATCSICL DYFTDPVMTA CGHNFCRECI QMSWEKGKGK KGKKKQKGSF
     PCPECREMSP QRNLRPNRLL TKVAEMARQH PGLHKRDLCQ IHQEPLKLFC QDDQTPICVV
     CREAQEHRMH RVLPLDEAAR EYKLRLEEDI KYLREEMMKT ETLQAKEEQT LTEWQERVKE
     RRERILEEFQ KVVLFLVEEE RRLLQILKKE EDDTLGKLQD SKASLDHQSR SLDLILLQLE
     EQTQQEPLQM LQDVKDTLTR KESLSMQYPE VVLPVAIKTV CRVPGQIEVL KSFQEDVVPD
     PSTAYPYLLL YESRQRRYLS PPPEGSAPYS KDRFLAYPCA VGQKSFSSGR HYWEVGMNLT
     GDALWALGVC RDNVSRKDRV LKSPENGFWV VQLSKGKKHL PLLPNSIPVT LTEPPSHMGI
     FLDFQAGEVS FYSVNDGSHL HSFSQVAFPG PLLPFFCLGS PKSGQMVIST VTMWVKG
 
 
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