TRI45_BOVIN
ID TRI45_BOVIN Reviewed; 580 AA.
AC Q5BIM1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Tripartite motif-containing protein 45;
GN Name=TRIM45;
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).
CC -!- FUNCTION: May act as a transcriptional repressor in mitogen-activated
CC protein kinase signaling pathway. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BT021203; AAX31385.1; -; mRNA.
DR RefSeq; NP_001014952.1; NM_001014952.1.
DR RefSeq; XP_010801425.1; XM_010803123.2.
DR AlphaFoldDB; Q5BIM1; -.
DR SMR; Q5BIM1; -.
DR STRING; 9913.ENSBTAP00000002293; -.
DR PaxDb; Q5BIM1; -.
DR PRIDE; Q5BIM1; -.
DR Ensembl; ENSBTAT00000002293; ENSBTAP00000002293; ENSBTAG00000001748.
DR GeneID; 539091; -.
DR KEGG; bta:539091; -.
DR CTD; 80263; -.
DR VEuPathDB; HostDB:ENSBTAG00000001748; -.
DR VGNC; VGNC:36337; TRIM45.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154334; -.
DR HOGENOM; CLU_013137_14_8_1; -.
DR InParanoid; Q5BIM1; -.
DR OMA; TRCPLCM; -.
DR OrthoDB; 489543at2759; -.
DR TreeFam; TF324196; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000001748; Expressed in corpus luteum and 107 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
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; PF00630; Filamin; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
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; Nucleus; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..580
FT /note="Tripartite motif-containing protein 45"
FT /id="PRO_0000245027"
FT REPEAT 394..497
FT /note="Filamin"
FT ZN_FING 29..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 130..176
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 186..227
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 281..335
FT /evidence="ECO:0000255"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 580 AA; 63754 MW; 40D775EE512057CA CRC64;
MAEKRRPLLG FVGKLPSGTT AGNSGKTHCP LCMGLFKAPR LLPCLHTVCT TCLEQLEPFS
VVDIRGGESD TSSEGSVFQE LKPRALQPQI GILCPVCDAQ VDLPMGGVKA LTIDHLAMND
VMLESLRGEG QGLVCDLCSD REVEKRCQTC KANLCRFCCQ AHRRQKKTTY HTMVDLKDLK
GYSQIGKPIL CPAHPAEELR LFCELCDRPV CRDCVVGEHR EHPCDFTSNV IHKHGDSVRE
LLRGTQPHVE ALEEALAQIK GTNSAVQERV KAVAADIRTF SEGYIKAIEE HRDKLLKQLE
DIRVQKENSL QLQKAQLEQL LADMRTGVEF TEHLLTSGSD LEILITKGVV VERLTKLNKV
EYSAHPGVNE KISFSPKQKA GLCRGYEVYG AINTKEVDPA KCVLQGEDLH RAREKQPASF
IVLCKDATGE SMGRGGDNVQ VTVIPNDKKD SPVKTMVHDN KDGTYYVSYT PKEPGTYTVL
VCVKEQHVQG SPFTVTVRKR HRSHPGVFHC CTFCSSGGQK TARCACGGTM PGGYLGCGHG
HKGHPGRPHW SCCGKFAEKS ECTWAGGQSA PRSLLRTVAL
