TRI46_RAT
ID TRI46_RAT Reviewed; 759 AA.
AC A0A0G2JXN2; A0A096MKD9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Tripartite motif-containing protein 46 {ECO:0000305};
GN Name=Trim46 {ECO:0000312|RGD:1305993};
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 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM00656.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION BY
RP 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).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TUBB3 AND TUBA4A, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 specification, 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 -!- TISSUE SPECIFICITY: Expressed in primary hippocampal and cortical
CC neurons. {ECO:0000269|PubMed:26671463}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDM00656.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC098750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473976; EDM00656.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001101161.1; NM_001107691.1.
DR RefSeq; XP_008759392.1; XM_008761170.2.
DR AlphaFoldDB; A0A0G2JXN2; -.
DR iPTMnet; A0A0G2JXN2; -.
DR Ensembl; ENSRNOT00000077074; ENSRNOP00000075661; ENSRNOG00000055433.
DR GeneID; 310641; -.
DR KEGG; rno:310641; -.
DR CTD; 80128; -.
DR RGD; 1305993; Trim46.
DR GeneTree; ENSGT00940000158021; -.
DR OrthoDB; 180330at2759; -.
DR PRO; PR:A0A0G2JXN2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0044304; C:main axon; IDA:ARUK-UCL.
DR GO; GO:1990769; C:proximal neuron projection; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:ARUK-UCL.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; IMP:ARUK-UCL.
DR GO; GO:0099612; P:protein localization to axon; ISO:RGD.
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 Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..759
FT /note="Tripartite motif-containing protein 46"
FT /id="PRO_0000441888"
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 513..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:0000250|UniProtKB:Q7TNM2"
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:0000250|UniProtKB:Q7TNM2"
FT COILED 294..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:0000250|UniProtKB:Q7TNM2"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 759 AA; 83431 MW; DA3FC4EA88F91C5E CRC64;
MAEGEDMQTF TSIMDALVRI STSMKNMEKE LLCPVCQEMY KQPLVLPCTH NVCQACAREV
LGQQGYIGHG GDPSSEPTSP ASTPSTRSPR LSRRTLPKPD RLDRLLKSGF GTYPGRKRGA
LHPQTILFPC PACQGDVELG ERGLSGLFRN LTLERVVERY RQSVSVGGAI LCQLCKPPPL
EATKGCSECR ATFCNECFKL FHPWGTQKAQ HEPTLPTLSF RPKGLMCPDH KEEVTHYCKT
CQRLVCQLCR VRRTHSGHKI TPVLSAYQAL KDKLTKSLAY ILGNQDTVQT QICELEETIR
HTEVSGQQAK EEVSQLVRGL GAVLEEKRSS LLQAIEECQQ ERLSRLSAQI HEHQSLLDGS
GLVGYAQEVL KETDQPCFVQ AAKQLHNRIA RATEALQTFR PAASSSFRHC QLDVGREMKL
LTELNFLRVP EAPVIDTQRT FAYDQIFLCW RLPPHSPPAW HYTVEFRRTD VPAQPGPTRW
QRREEVRGTS ALLENPDTGS VYVLRVRGCN KAGYGEYSED VHLHTPPAPV LHFFLDGRWG
ASRERLAISK DQRAVRSIPG LPLLLAAERL LTGCHLSVDV VLGDVAVTQG RSYWACAVDP
ASYLVKVGVG LESKLQESFQ GAPDVISPRY DPDSGHDSGA EDAAVEALPP FAFLTIGMGK
ILLGSGASSN AGLTGRDGPA ASCTVPLPPR LGICLDYERG RVSFLDAVSF RGLLECPLDC
SGPVCPAFCF IGGGAVQLQE PVGTKPERKV TIGGFAKLD
