TRIM3_RAT
ID TRIM3_RAT Reviewed; 744 AA.
AC O70277;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tripartite motif-containing protein 3;
DE AltName: Full=Brain-expressed RING finger protein;
DE AltName: Full=RING finger protein 22;
GN Name=Trim3; Synonyms=Berp, Rnf22;
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], AND INTERACTION WITH MYO5B.
RC TISSUE=Brain;
RX PubMed=10391919; DOI=10.1074/jbc.274.28.19771;
RA El-Husseini A.E.-D., Vincent S.R.;
RT "Cloning and characterization of a novel RING finger protein that interacts
RT with class V myosins.";
RL J. Biol. Chem. 274:19771-19777(1999).
RN [2]
RP INTERACTION WITH ACTN4.
RX PubMed=10673389; DOI=10.1006/bbrc.1999.2045;
RA El-Husseini A.E.-D., Kwasnicka D., Yamada T., Hirohashi S., Vincent S.R.;
RT "BERP, a novel ring finger protein, binds to alpha-actinin-4.";
RL Biochem. Biophys. Res. Commun. 267:906-911(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-427, AND
RP IDENTIFICATION BY 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: Probably involved in vesicular trafficking via its
CC association with the CART complex. The CART complex is necessary for
CC efficient transferrin receptor recycling but not for EGFR degradation.
CC Positively regulates motility of microtubule-dependent motor protein
CC KIF21B. {ECO:0000250|UniProtKB:O75382, ECO:0000250|UniProtKB:Q9R1R2}.
CC -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4 (ACTN4)
CC (PubMed:10391919, PubMed:10673389). Component of the CART complex, at
CC least composed of ACTN4, HGS/HRS, MYO5B and TRIM3 (By similarity).
CC Interacts with ZFYVE28/LST2 (By similarity). Interacts with KIF21B (By
CC similarity). {ECO:0000250|UniProtKB:O75382,
CC ECO:0000250|UniProtKB:Q9R1R2, ECO:0000269|PubMed:10391919,
CC ECO:0000269|PubMed:10673389}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q9R1R2}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9R1R2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain, moderate levels in
CC the lung, very low levels in the liver, kidney and heart. In the brain,
CC expression was highest in the cerebellum.
CC -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL repeats,
CC which form a beta-propeller (NHL) domain containing six blades.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF036255; AAC17997.1; -; mRNA.
DR RefSeq; NP_113974.1; NM_031786.1.
DR AlphaFoldDB; O70277; -.
DR SMR; O70277; -.
DR BioGRID; 249781; 4.
DR IntAct; O70277; 2.
DR MINT; O70277; -.
DR STRING; 10116.ENSRNOP00000024850; -.
DR iPTMnet; O70277; -.
DR PhosphoSitePlus; O70277; -.
DR SwissPalm; O70277; -.
DR jPOST; O70277; -.
DR PaxDb; O70277; -.
DR PRIDE; O70277; -.
DR GeneID; 83616; -.
DR KEGG; rno:83616; -.
DR UCSC; RGD:70074; rat.
DR CTD; 10612; -.
DR RGD; 70074; Trim3.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; O70277; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; O70277; -.
DR PRO; PR:O70277; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cell projection; Coiled coil; Cytoplasm; Endosome;
KW Golgi apparatus; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75382"
FT CHAIN 2..744
FT /note="Tripartite motif-containing protein 3"
FT /id="PRO_0000056199"
FT REPEAT 317..418
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 22..63
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 110..151
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 2..290
FT /note="Interaction with KIF21B"
FT /evidence="ECO:0000250|UniProtKB:Q9R1R2"
FT REGION 420..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..224
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75382"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 744 AA; 80796 MW; 4BFF839B7A4809EB CRC64;
MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI PPQSLTLSCP
VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPDGAHDPE DPHPLSAVAG RPLSCPNHEG
KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT
LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
EVDGLRRSVL NLGALLTTSA AAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
ELCAEITGPD GMRLAVPVVD HKNGTYELVY TARTEGDLLL SVLLYGQPVR GSPFRVRALR
PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIVD ELVFRVGSRG
REKGEFTNLH PLSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
LTSDGHVVVA DAGNHCFKAY RYLQ
