ID G9KV39_MUSPF Unreviewed; 629 AA.
AC G9KV39;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM41 isoform X2 {ECO:0000313|RefSeq:XP_004780263.1};
DE SubName: Full=Tripartite motif-containing 41 {ECO:0000313|EMBL:AES08768.1, ECO:0000313|Ensembl:ENSMPUP00000001175.1};
DE Flags: Fragment;
GN Name=TRIM41 {ECO:0000313|Ensembl:ENSMPUP00000001175.1,
GN ECO:0000313|RefSeq:XP_004780263.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES08768.1};
RN [1] {ECO:0000313|EMBL:AES08768.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES08768.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
RN [2] {ECO:0000313|Ensembl:ENSMPUP00000001175.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_004780263.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004780263.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AEYP01099522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JP020170; AES08768.1; -; mRNA.
DR RefSeq; XP_004780263.1; XM_004780206.3.
DR STRING; 9669.ENSMPUP00000001175; -.
DR Ensembl; ENSMPUT00000001200.1; ENSMPUP00000001175.1; ENSMPUG00000001186.1.
DR GeneID; 101690656; -.
DR CTD; 90933; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154294; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR OMA; WDTPMRE; -.
DR OrthoDB; 3453019at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd13741; SPRY_PRY_TRIM41; 1.
DR Gene3D; 2.60.120.920; -; 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; IPR042828; TRIM41_SPRY_PRY.
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; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF659; E3 UBIQUITIN-PROTEIN LIGASE TRIM41; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 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; 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; 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 {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 20..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 221..262
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 412..629
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 51..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..311
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES08768.1"
FT NON_TER 629
FT /evidence="ECO:0000313|EMBL:AES08768.1"
SQ SEQUENCE 629 AA; 71377 MW; 6E144D968D298947 CRC64;
MAAVAMAPNP VQTLQEEAVC AICLDYFTDP VSIGCGHNFC RVCVTQLWGG EDEEDREELD
REEEEEDGEE EEVEAVGAGG GWDTPMRDED YEGDMEEEVE EEEEGVFWTS GMGGSNWDNM
DYVWEEEDEE EDLDYYLGDM EEDLRGEDEE DEEEVLEEDE EEELDPVTPL PPPPAPRRCF
TCPQCRKSFP RRSFRPNLQL ANMVQVIRQM HPTPGRGSRG SEQGICPKHQ EALKLFCEVD
EEAICVVCRE SRSHKQHSVV PLEEVVQEYK AKLQGHVEPL RKHLEAVQKM KAKEERRVTE
LKSQMKSELA AVASEFGRLT RFLAEEQAGL ERRLREMHEA QLGRAGAAAS RLAEQAAQLS
RLLAEAQERS QQGGLRLLQD IKETFNRCEE VQLQPPEVWS PDPCQPHSHD FLTDAIVRKM
SRMFCQAARV DLTLDPDTAH PALMLSPDRR GVRLAERRQE VADHSKRFSA DCCVLGAQGF
RSGRHYWEVE VGGRRGWAVG AARESTHHKE KVGSGGSSVG SGDASSSRHH HRRRRLHLPQ
QPLLQREVWC VGTNGKRYQA QSSTEQTLLS PSEKPRRFGV YLDYEAGRLG FYNAETLAHV
HTFSAAFLGE RVFPFFRVLS KGTRIKLCP
//
