TRIM9_BOVIN
ID TRIM9_BOVIN Reviewed; 710 AA.
AC Q29RQ5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM9;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9C026};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM9 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 9;
GN Name=TRIM9;
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].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself in
CC cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting
CC signal for proteasomal degradation. May play a role in regulation of
CC neuronal functions. May act as a regulator of synaptic vesicle
CC exocytosis by controlling the availability of SNAP25 for the SNARE
CC complex formation. {ECO:0000250|UniProtKB:Q9C026}.
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; Evidence={ECO:0000250|UniProtKB:Q9C026};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9C026}.
CC -!- SUBUNIT: Interacts with SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C026}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q9C026}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000250|UniProtKB:Q91ZY8}. Synapse {ECO:0000250|UniProtKB:Q91ZY8}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZY8}. Note=Enriched
CC at synaptic terminals where it exists in a soluble form and a synaptic
CC vesicle-associated form. Associated with the cytoskeleton (By
CC similarity). Found in proximal dendrites of pyramidal neurons in the
CC cerebral cortex and hippocampus, and Purkinje cells in the cerebellum
CC (By similarity). {ECO:0000250|UniProtKB:Q91ZY8,
CC ECO:0000250|UniProtKB:Q9C026}.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with the N-
CC terminal t-SNARE domain of SNAP25. {ECO:0000250|UniProtKB:Q91ZY8}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9C026}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC114071; AAI14072.1; -; mRNA.
DR RefSeq; NP_001070005.1; NM_001076537.2.
DR AlphaFoldDB; Q29RQ5; -.
DR PaxDb; Q29RQ5; -.
DR Ensembl; ENSBTAT00000013346; ENSBTAP00000013346; ENSBTAG00000010103.
DR GeneID; 767615; -.
DR KEGG; bta:767615; -.
DR CTD; 114088; -.
DR VEuPathDB; HostDB:ENSBTAG00000010103; -.
DR VGNC; VGNC:36353; TRIM9.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00940000154071; -.
DR HOGENOM; CLU_013137_19_2_1; -.
DR InParanoid; Q29RQ5; -.
DR OrthoDB; 516512at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000010103; Expressed in occipital lobe and 47 other tissues.
DR ExpressionAtlas; Q29RQ5; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003877; SPRY_dom.
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; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 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; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 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 Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..710
FT /note="E3 ubiquitin-protein ligase TRIM9"
FT /id="PRO_0000240608"
FT DOMAIN 374..432
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 440..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 533..702
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 10..50
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 163..212
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 224..266
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 273..340
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7M3"
SQ SEQUENCE 710 AA; 79347 MW; E919DCE99DC25F30 CRC64;
MEEMEEELKC PVCGSFYREP IILPCSHNIC QACARNILVQ TPESESPQSR RASGSGVSDY
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPA THLSPALASV
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRN
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
PLLQSIHQLD FVQMKASSPV PATPILQLED CCTHNNSATL SWKQPPLSTV PAEGYILELD
DGNGGQFREV YVGKETMCTV DGLHFNSTYN ARIKAFNKTG VSQYSKTLVL QTSEVAWFAF
DPGSAHSDII FSNDNLTVTC SSYDDRVVLG KTGFSKGVHY WELTVDRYDN HPDPAFGVAR
IDVMKDVMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDFNRKTLTF
FINDEQQGPI AFENVEGLFF PAVSLNRNVQ VTLHTGLQVP DFYSSRASIA
