TRIM2_BOVIN
ID TRIM2_BOVIN Reviewed; 744 AA.
AC A4IF63;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tripartite motif-containing protein 2;
DE EC=2.3.2.27;
DE AltName: Full=E3 ubiquitin-protein ligase TRIM2;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM2 {ECO:0000305};
GN Name=TRIM2;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination
CC of phosphorylated BCL2L11. Also mediates the UBE2D1-dependent
CC ubiquitination of NEFL. Plays a neuroprotective function. May play a
CC role in neuronal rapid ischemic tolerance.
CC {ECO:0000250|UniProtKB:Q9ESN6}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with myosin V; myosin V may not be a substrate for
CC ubiquitination. Interacts with NEFL. Interacts with phosphorylated
CC BCL2L11. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- DOMAIN: The interaction with myosin V is dependent upon its NHL
CC repeats, which form a beta-propeller (NHL) domain containing six
CC blades. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- PTM: RING-type zinc finger-dependent and UBE2D1-dependent
CC autoubiquitination. {ECO:0000250|UniProtKB:Q9ESN6}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC134423; AAI34424.1; -; mRNA.
DR EMBL; AAFC03054408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001077204.1; NM_001083735.2.
DR AlphaFoldDB; A4IF63; -.
DR SMR; A4IF63; -.
DR STRING; 9913.ENSBTAP00000011609; -.
DR PaxDb; A4IF63; -.
DR PRIDE; A4IF63; -.
DR Ensembl; ENSBTAT00000011609; ENSBTAP00000011609; ENSBTAG00000008816.
DR GeneID; 538617; -.
DR KEGG; bta:538617; -.
DR CTD; 23321; -.
DR VEuPathDB; HostDB:ENSBTAG00000008816; -.
DR VGNC; VGNC:36318; TRIM2.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155905; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR InParanoid; A4IF63; -.
DR OMA; CTSGEHR; -.
DR OrthoDB; 489543at2759; -.
DR TreeFam; TF331018; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000008816; Expressed in occipital lobe and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase 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; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR001258; NHL_repeat.
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; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
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 Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..744
FT /note="Tripartite motif-containing protein 2"
FT /id="PRO_0000413606"
FT REPEAT 320..421
FT /note="Filamin"
FT REPEAT 473..516
FT /note="NHL 1"
FT REPEAT 520..563
FT /note="NHL 2"
FT REPEAT 564..605
FT /note="NHL 3"
FT REPEAT 609..652
FT /note="NHL 4"
FT REPEAT 656..699
FT /note="NHL 5"
FT REPEAT 700..743
FT /note="NHL 6"
FT ZN_FING 23..64
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 113..154
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 432..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZQG6"
FT MOD_RES 371
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESN6"
SQ SEQUENCE 744 AA; 81476 MW; 6E826474FC83A622 CRC64;
MASEATNIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVAALQNN FFITNLMDVL QRSPGSSAEE SSILETVTAV AAGKPLSCPN
HDGNVMDFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AANRRLPEID
SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQSQ
LDTLLEGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
VIRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
RNKGEFTNLQ GVAASTNGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
VHPSGDIIIA DYDNKWVSIF SSDGKFKTKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
IFQPNGKIVT RFGSRGNGDR QFAGPHFAAV NSNNEIIVTD FHNHSVKVFN QEGEFMLKFG
SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
LTSDGHVVVA DSGNHCFKVY RYLQ
