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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
 
 
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