TRIM9_RAT
ID TRIM9_RAT Reviewed; 710 AA.
AC Q91ZY8;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
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=SNAP-25-interacting RING finger protein;
DE AltName: Full=Tripartite motif-containing protein 9;
GN Name=Trim9; Synonyms=Spring;
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], INTERACTION WITH SNAP25, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=11524423; DOI=10.1074/jbc.m106141200;
RA Li Y., Chin L.-S., Weigel C., Li L.;
RT "Spring, a novel RING finger protein that regulates synaptic vesicle
RT exocytosis.";
RL J. Biol. Chem. 276:40824-40833(2001).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=20085810; DOI=10.1016/j.nbd.2010.01.007;
RA Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H., Wakabayashi K.;
RT "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in the
RT brain of Parkinson's disease and dementia with Lewy bodies.";
RL Neurobiol. Dis. 38:210-218(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). May act as a regulator of synaptic
CC vesicle exocytosis by controlling the availability of SNAP25 for the
CC SNARE 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:0000269|PubMed:11524423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle {ECO:0000269|PubMed:11524423}. Synapse
CC {ECO:0000269|PubMed:11524423}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11524423}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9C026}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9C026}. Note=Found in proximal dendrites of
CC pyramidal neurons in the cerebral cortex and hippocampus, and Purkinje
CC cells in the cerebellum (By similarity). Enriched at synaptic terminals
CC where it exists in a soluble form and a synaptic vesicle-associated
CC form. Associated with the cytoskeleton (PubMed:11524423).
CC {ECO:0000250|UniProtKB:Q9C026, ECO:0000269|PubMed:11524423}.
CC -!- TISSUE SPECIFICITY: Brain (at protein level). Expressed in fetal and
CC adult brain. {ECO:0000269|PubMed:20085810}.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with the N-
CC terminal t-SNARE domain of SNAP25.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9C026}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF350422; AAL27988.1; -; mRNA.
DR RefSeq; NP_569104.1; NM_130420.1.
DR AlphaFoldDB; Q91ZY8; -.
DR BioGRID; 250896; 1.
DR IntAct; Q91ZY8; 1.
DR MINT; Q91ZY8; -.
DR STRING; 10116.ENSRNOP00000009559; -.
DR iPTMnet; Q91ZY8; -.
DR PhosphoSitePlus; Q91ZY8; -.
DR PaxDb; Q91ZY8; -.
DR PRIDE; Q91ZY8; -.
DR Ensembl; ENSRNOT00000009560; ENSRNOP00000009559; ENSRNOG00000007031.
DR GeneID; 155812; -.
DR KEGG; rno:155812; -.
DR UCSC; RGD:621540; rat.
DR CTD; 114088; -.
DR RGD; 621540; Trim9.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00940000154071; -.
DR HOGENOM; CLU_013137_19_2_1; -.
DR InParanoid; Q91ZY8; -.
DR OMA; PDTICTI; -.
DR OrthoDB; 516512at2759; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q91ZY8; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007031; Expressed in frontal cortex and 6 other tissues.
DR Genevisible; Q91ZY8; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:RGD.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; IDA:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEP:RGD.
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 1: Evidence at protein 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_0000056210"
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:0007744|PubMed:22673903"
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; 79206 MW; 84A85EA27152CD51 CRC64;
MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSR RASGSGVSDY
DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPP THLSPALAPV
PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRT
MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV AADGYILELD
DGSGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEVAWFAF
DPGSAHSDII FSNDNLTVTC SSYDDRVVLG KTGFSKGVHY WELTIDRYDN HPDPAFGVAR
IDVMKDMMLG KDDKAWAMYV DNNRSWFMHN NSHTNRTEGG ITKGATIGVL LDLNRKTLTF
FVNNEQQGPI AFENVEGLFF PAVSLNRNVQ VTLHTGLPVP DFYSSRASIA
