TRIM3_MOUSE
ID TRIM3_MOUSE Reviewed; 744 AA.
AC Q9R1R2; Q3UMU5;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Tripartite motif-containing protein 3;
DE AltName: Full=RING finger protein 22;
DE AltName: Full=RING finger protein HAC1;
GN Name=Trim3; Synonyms=Hac1, Rnf22;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Yanai K., Shimamoto Y., Hirota K., Fukamizu A.;
RT "Cloning of a new co-activator with ring finger motif.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH KIF21B, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24086586; DOI=10.1371/journal.pone.0075603;
RA Labonte D., Thies E., Pechmann Y., Groffen A.J., Verhage M., Smit A.B.,
RA van Kesteren R.E., Kneussel M.;
RT "TRIM3 regulates the motility of the kinesin motor protein KIF21B.";
RL PLoS ONE 8:E75603-E75603(2013).
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 (By similarity). Positively regulates motility of microtubule-dependent
CC motor protein KIF21B (PubMed:24086586). {ECO:0000250|UniProtKB:O75382,
CC ECO:0000269|PubMed:24086586}.
CC -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4 (ACTN4)
CC (By similarity). Component of the CART complex, at least composed of
CC ACTN4, HGS/HRS, MYO5B and TRIM3 (By similarity). Interacts with
CC ZFYVE28/LST2 (By similarity). Interacts with KIF21B (PubMed:24086586).
CC {ECO:0000250|UniProtKB:O70277, ECO:0000250|UniProtKB:O75382,
CC ECO:0000269|PubMed:24086586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:24086586}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24086586}.
CC -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL repeats,
CC which form a beta-propeller (NHL) domain containing six blades.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:24086586}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AB030912; BAA83343.1; -; mRNA.
DR EMBL; AF220019; AAG53473.1; -; mRNA.
DR EMBL; AK019165; BAB31580.1; -; mRNA.
DR EMBL; AK144674; BAE26003.1; -; mRNA.
DR EMBL; BC034263; AAH34263.1; -; mRNA.
DR CCDS; CCDS21655.1; -.
DR RefSeq; NP_001272799.1; NM_001285870.1.
DR RefSeq; NP_001272800.1; NM_001285871.1.
DR RefSeq; NP_001272802.1; NM_001285873.1.
DR RefSeq; NP_061368.1; NM_018880.3.
DR AlphaFoldDB; Q9R1R2; -.
DR SMR; Q9R1R2; -.
DR BioGRID; 207763; 17.
DR IntAct; Q9R1R2; 9.
DR STRING; 10090.ENSMUSP00000053384; -.
DR iPTMnet; Q9R1R2; -.
DR PhosphoSitePlus; Q9R1R2; -.
DR jPOST; Q9R1R2; -.
DR MaxQB; Q9R1R2; -.
DR PaxDb; Q9R1R2; -.
DR PRIDE; Q9R1R2; -.
DR ProteomicsDB; 258980; -.
DR Antibodypedia; 11249; 268 antibodies from 33 providers.
DR DNASU; 55992; -.
DR Ensembl; ENSMUST00000057525; ENSMUSP00000053384; ENSMUSG00000036989.
DR Ensembl; ENSMUST00000106789; ENSMUSP00000102401; ENSMUSG00000036989.
DR Ensembl; ENSMUST00000147044; ENSMUSP00000114822; ENSMUSG00000036989.
DR GeneID; 55992; -.
DR KEGG; mmu:55992; -.
DR UCSC; uc009iym.2; mouse.
DR CTD; 10612; -.
DR MGI; MGI:1860040; Trim3.
DR VEuPathDB; HostDB:ENSMUSG00000036989; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158173; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR InParanoid; Q9R1R2; -.
DR OMA; EPCETAM; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q9R1R2; -.
DR TreeFam; TF331018; -.
DR BioGRID-ORCS; 55992; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trim3; mouse.
DR PRO; PR:Q9R1R2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R1R2; protein.
DR Bgee; ENSMUSG00000036989; Expressed in cerebellar cortex and 242 other tissues.
DR ExpressionAtlas; Q9R1R2; baseline and differential.
DR Genevisible; Q9R1R2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:FlyBase.
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; IDA:FlyBase.
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_0000056198"
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:0000269|PubMed:24086586"
FT REGION 419..464
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:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 744 AA; 80774 MW; D9AEF4FA264BA168 CRC64;
MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI PPQSLTLSCP
VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE DPHPLSAVAG RPLSCPNHEG
KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT
LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
ELCAEITGPD GVRLAVPVVD HKNGTYELVY TARTEGDLLL SVLLYGQPVR GSPFRVRALR
PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
REKGEFTNLQ GVSAASSGRI 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
