TRI46_MOUSE
ID TRI46_MOUSE Reviewed; 759 AA.
AC Q7TNM2; Q60717; Q6P1I9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tripartite motif-containing protein 46;
DE AltName: Full=Gene Y protein;
DE Short=GeneY;
DE AltName: Full=Tripartite, fibronectin type-III and C-terminal SPRY motif protein;
GN Name=Trim46; Synonyms=Trific;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16434393; DOI=10.1074/jbc.m512755200;
RA Short K.M., Cox T.C.;
RT "Subclassification of the RBCC/TRIM superfamily reveals a novel motif
RT necessary for microtubule binding.";
RL J. Biol. Chem. 281:8970-8980(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-759 (ISOFORM 1).
RC STRAIN=BALB/cJ;
RX PubMed=8597643; DOI=10.1007/bf00539013;
RA Vos H.L., Mockensturm-Wilson M., Rood P.M.L., Maas A.M., Duhig T.,
RA Gendler S.J., Bornstein P.;
RT "A tightly organized, conserved gene cluster on mouse chromosome 3 (E3-
RT F1).";
RL Mamm. Genome 6:820-822(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-627, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5]
RP FUNCTION, INTERACTION WITH TUBB3 AND TUBA4A, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=26671463; DOI=10.1016/j.neuron.2015.11.012;
RA van Beuningen S.F., Will L., Harterink M., Chazeau A., van Battum E.Y.,
RA Frias C.P., Franker M.A., Katrukha E.A., Stucchi R., Vocking K.,
RA Antunes A.T., Slenders L., Doulkeridou S., Sillevis Smitt P.,
RA Altelaar A.F., Post J.A., Akhmanova A., Pasterkamp R.J., Kapitein L.C.,
RA de Graaff E., Hoogenraad C.C.;
RT "TRIM46 controls neuronal polarity and axon specification by driving the
RT formation of parallel microtubule arrays.";
RL Neuron 88:1208-1226(2015).
CC -!- FUNCTION: Microtubule-associated protein that is involved in the
CC formation of parallel microtubule bundles linked by cross-bridges in
CC the proximal axon. Required for the uniform orientation and maintenance
CC of the parallel microtubule fascicles, which are important for
CC efficient cargo delivery and trafficking in axons. Thereby also
CC required for proper axon formation, the establishment of neuronal
CC polarity and proper neuronal migration. {ECO:0000269|PubMed:26671463}.
CC -!- SUBUNIT: Interacts with TUBB3 and TUBA4A.
CC {ECO:0000269|PubMed:26671463}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:26671463}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26671463}. Note=Microtubule-associated. Localizes
CC to the proximal part of the axon. {ECO:0000269|PubMed:26671463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TNM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TNM2-2; Sequence=VSP_011985, VSP_011986, VSP_011987;
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, including
CC pyramidal neurons and interneurons in the cortex and hippocampus and
CC all neuronal cell types in the cerebral and cerebellar cortex, and in
CC the peripheral nervous system, including the dorsal root ganglion
CC neurons. {ECO:0000269|PubMed:26671463}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY251388; AAP51208.1; -; mRNA.
DR EMBL; BC065049; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U16175; AAA98539.1; -; Genomic_DNA.
DR CCDS; CCDS17497.1; -. [Q7TNM2-1]
DR RefSeq; NP_898858.1; NM_183037.2. [Q7TNM2-1]
DR AlphaFoldDB; Q7TNM2; -.
DR BioGRID; 237527; 3.
DR IntAct; Q7TNM2; 3.
DR MINT; Q7TNM2; -.
DR STRING; 10090.ENSMUSP00000036053; -.
DR iPTMnet; Q7TNM2; -.
DR PhosphoSitePlus; Q7TNM2; -.
DR MaxQB; Q7TNM2; -.
DR PaxDb; Q7TNM2; -.
DR PRIDE; Q7TNM2; -.
DR ProteomicsDB; 298301; -. [Q7TNM2-1]
DR ProteomicsDB; 298302; -. [Q7TNM2-2]
DR Antibodypedia; 34171; 103 antibodies from 20 providers.
DR Ensembl; ENSMUST00000041022; ENSMUSP00000036053; ENSMUSG00000042766. [Q7TNM2-1]
DR GeneID; 360213; -.
DR KEGG; mmu:360213; -.
DR UCSC; uc008pyk.1; mouse. [Q7TNM2-1]
DR CTD; 80128; -.
DR MGI; MGI:2673000; Trim46.
DR VEuPathDB; HostDB:ENSMUSG00000042766; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158021; -.
DR InParanoid; Q7TNM2; -.
DR OMA; AEMDFKT; -.
DR OrthoDB; 180330at2759; -.
DR PhylomeDB; Q7TNM2; -.
DR TreeFam; TF315216; -.
DR BioGRID-ORCS; 360213; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Trim46; mouse.
DR PRO; PR:Q7TNM2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TNM2; protein.
DR Bgee; ENSMUSG00000042766; Expressed in embryonic brain and 119 other tissues.
DR ExpressionAtlas; Q7TNM2; baseline and differential.
DR Genevisible; Q7TNM2; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR GO; GO:0044304; C:main axon; IDA:ARUK-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:1990769; C:proximal neuron projection; IMP:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISO:MGI.
DR GO; GO:0099612; P:protein localization to axon; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:ARUK-UCL.
DR CDD; cd00063; FN3; 1.
DR CDD; cd12895; SPRY_PRY_TRIM46; 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; 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; IPR040859; Midline-1_COS.
DR InterPro; IPR035731; SPRY/PRY_TRIM46.
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; PF18568; COS; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 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; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..759
FT /note="Tripartite motif-containing protein 46"
FT /id="PRO_0000056269"
FT DOMAIN 370..427
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 429..528
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 526..747
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 33..59
FT /note="RING-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 172..231
FT /note="RING-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 222..263
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..166
FT /note="Required for proximal axon localization, axon
FT formation and migration"
FT /evidence="ECO:0000269|PubMed:26671463"
FT REGION 67..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..429
FT /note="Required for microtubule association, proximal axon
FT localization and axon formation"
FT /evidence="ECO:0000269|PubMed:26671463"
FT COILED 322..400
FT /evidence="ECO:0000255"
FT COMPBIAS 75..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..23
FT /note="MAEGEDMQTFTSIMDALVRISTS -> MGGALEINAINPEMEGWRQTS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011985"
FT VAR_SEQ 429..447
FT /note="VPEAPVIDTQRTFAYDQIF -> GCGHRGLCSGAPQCPRRPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011986"
FT VAR_SEQ 448..759
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011987"
FT CONFLICT 743
FT /note="G -> A (in Ref. 3; AAA98539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 83432 MW; 8126C4C79841A536 CRC64;
MAEGEDMQTF TSIMDALVRI STSMKNMEKE LLCPVCQEMY KQPLVLPCTH NVCQACAREV
LGQQGYIGHG GDPSSEPTSP ASTPSTRSPR LSRRTLPKPD RLDRLLKSGF GTYPGRKRGA
LHPQTILFPC PACQGDVELG ERGLSGLFRN LTLERVVERY RQSVSVGGAI LCQLCKPPPL
EATKGCTECR ATFCNECFKL FHPWGTQKAQ HEPTLPTLSF RPKGLMCPDH KEEVTHYCKT
CQRLVCQLCR VRRTHSGHKI TPVLSAYQAL KDKLTKSLAY ILGNQDTVQT QICELEETIR
HTEVSGQQAK EEVSQLVRGL GAVLEEKRAS LLQAIEECQQ ERLSRLSAQI HEHQSLLDGS
GLVGYAQEVL KETDQPCFVQ AAKQLHNRIA RATEALQTFR PAASSSFRHC QLDVGREMKL
LTELSFLRVP EAPVIDTQRT FAYDQIFLCW RLPPHSPPAW HYTVEFRRTD VPAQPGPTRW
QRREEVRGTS ALLENPDTGS VYVLRVRGCN KAGYGEYSED VHLHTPPAPV LHFFLDGRWG
ASRERLAISK DQRAVRSIPG LPLLLAAERL LTGCHLSVDV VLGDVAVTQG RSYWACAVDP
ASYLVKVGVG LESKLQESFQ GAPDVISPRY DPDSGHDSGA EDAAVEALPP FAFLTIGMGK
ILLGSGASSN AGLTGRDGPT ASCTVPLPPR LGICLDYERG RVSFLDAVSF RGLLECPLDC
SGPVCPAFCF IGGGAVQLQE PVGTKPERKV TIGGFAKLD
