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Database: UniProt
Entry: A0A0D9QZW0_CHLSB
LinkDB: A0A0D9QZW0_CHLSB
Original site: A0A0D9QZW0_CHLSB 
ID   A0A0D9QZW0_CHLSB        Unreviewed;       630 AA.
AC   A0A0D9QZW0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Tripartite motif containing 25 {ECO:0000313|Ensembl:ENSCSAP00000001899.1};
GN   Name=TRIM25 {ECO:0000313|Ensembl:ENSCSAP00000001899.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000001899.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000001899.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000001899.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; AQIB01117344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01117345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01117346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008009564.1; XM_008011373.1.
DR   AlphaFoldDB; A0A0D9QZW0; -.
DR   STRING; 60711.ENSCSAP00000001899; -.
DR   Ensembl; ENSCSAT00000003623.1; ENSCSAP00000001899.1; ENSCSAG00000005591.1.
DR   GeneID; 103242879; -.
DR   KEGG; csab:103242879; -.
DR   CTD; 7706; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000160741; -.
DR   OMA; KRGVHYW; -.
DR   OrthoDB; 5359093at2759; -.
DR   BioGRID-ORCS; 103242879; 6 hits in 16 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 16.
DR   Bgee; ENSCSAG00000005591; Expressed in adrenal cortex and 6 other cell types or tissues.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039552; F:RIG-I binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0036503; P:ERAD pathway; IEA:Ensembl.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR   GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
DR   CDD; cd19842; Bbox1_TRIM25-like_C-IV; 1.
DR   CDD; cd19776; Bbox2_TRIM25_C-IV; 1.
DR   CDD; cd16597; RING-HC_TRIM25_C-IV; 1.
DR   CDD; cd13736; SPRY_PRY_TRIM25; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR042753; TRIM25_SPRY_PRY.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR25465:SF40; E3 UBIQUITIN_ISG15 LIGASE TRIM25; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          13..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          439..630
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          356..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..301
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        356..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  70668 MW;  19DDEEBA2B35CB75 CRC64;
     MAQLCPLAEE LSCSICLEPF KEPVTTPCGH NFCGSCLNET WAVQGAPYLC PQCRAVYQAR
     PQLHKNTVLC NVVEQFLQAE LAREPPADGW TPPARASAPS PGAQVACDHC LKEAAVKTCL
     VCMASFCQEH LQPHFDSPAF QDHPLQSPVR DLLRRKCSQH NRLREFFCPE HGECICHICL
     VEHKACSPAS LSQASANVEA PLRHKLTVMY SQINGASRAL DDVRNRQQDV RMTANRKVEQ
     LRQEYTEMKA LLEASETTST RKIKEEEKRV NTKFDTIYQI LLKKKSEIQT LKEEIEQGLT
     EGDEFEFLEK ASKLRGISTK PVYIPEVELN RKLIKGIYHS TLDLKNELKQ CIRQLQEPSP
     SSGDPGEHDP ASTQKSTRPA KKVSKEEKKS KKPPSVPASS SKLPTFGAPE QLVDLKQSGS
     EAAAKATSSH PNSASLKAKV LETFLAKSRP ELLEYYVKVI LDYNTAHNKV ALSESYTVAS
     VAEMPQNYRP HPQRFTYCSQ VLGLHCYKKG IHYWEVELQK NNFCGVGICY GSMNRQGPES
     RLGRNSASWC VEWFNTKISA WHNNVEKTLP STKATRVGVL LNCDHGFVIF FAVADRVHLM
     YKFKVDFTEA LYPAFWVFSA GATLSICSPK
//
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