TRIM9_DROME
ID TRIM9_DROME Reviewed; 740 AA.
AC M9MRI4; Q86P21; Q9VKT3;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM9 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9C026};
DE AltName: Full=Anomalies in sensory axon patterning protein {ECO:0000303|PubMed:22084112};
DE Short=asap {ECO:0000303|PubMed:22084112};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM9 {ECO:0000305};
DE AltName: Full=Tripartite motif containing protein 9 {ECO:0000312|FlyBase:FBgn0051721};
GN Name=Trim9 {ECO:0000312|FlyBase:FBgn0051721};
GN ORFNames=CG31721 {ECO:0000312|FlyBase:FBgn0051721};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAP51207.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
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] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAO39531.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39531.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAO39531.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21338947; DOI=10.1016/j.jcg.2010.12.004;
RA Song S., Ge Q., Wang J., Chen H., Tang S., Bi J., Li X., Xie Q., Huang X.;
RT "TRIM-9 functions in the UNC-6/UNC-40 pathway to regulate ventral
RT guidance.";
RL J. Genet. Genomics 38:1-11(2011).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PICO AND FRA, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=22084112; DOI=10.1073/pnas.1109843108;
RA Morikawa R.K., Kanamori T., Yasunaga K., Emoto K.;
RT "Different levels of the Tripartite motif protein, Anomalies in sensory
RT axon patterning (Asap), regulate distinct axonal projections of Drosophila
RT sensory neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19389-19394(2011).
RN [7] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24746793; DOI=10.1016/j.cub.2014.03.041;
RA Yang L., Li R., Kaneko T., Takle K., Morikawa R.K., Essex L., Wang X.,
RA Zhou J., Emoto K., Xiang Y., Ye B.;
RT "Trim9 regulates activity-dependent fine-scale topography in Drosophila.";
RL Curr. Biol. 24:1024-1030(2014).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27743477; DOI=10.7554/elife.20762;
RA Akin O., Zipursky S.L.;
RT "Frazzled promotes growth cone attachment at the source of a Netrin
RT gradient in the Drosophila visual system.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase activity (By similarity). During
CC embryonic and larval development, regulates the pattern of axonal
CC projections of class IV nociceptive sensory neurons (C4da) downstream
CC of netrin receptor fra (PubMed:22084112, PubMed:21338947). Regulates
CC fine-scale topography of C4da axon terminals upon neuronal activity
CC (PubMed:24746793). During eye development, consolidates the attachment
CC of R8 photoreceptor growth cones to the target medulla layer, probably
CC downstream of fra (PubMed:27743477). {ECO:0000250|UniProtKB:Q9C026,
CC ECO:0000269|PubMed:21338947, ECO:0000269|PubMed:22084112,
CC ECO:0000269|PubMed:24746793, ECO:0000269|PubMed:27743477}.
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; Evidence={ECO:0000250|UniProtKB:Q9C026};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9C026}.
CC -!- SUBUNIT: Interacts (via fibronectin type-III domain) with pico.
CC Interacts (via SPRY domain) with netrin receptor fra.
CC {ECO:0000269|PubMed:22084112}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:22084112}. Perikaryon
CC {ECO:0000269|PubMed:22084112}. Note=Colocalizes with fra and pico.
CC {ECO:0000269|PubMed:22084112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0051721};
CC IsoId=M9MRI4-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0051721};
CC IsoId=M9MRI4-2; Sequence=VSP_058962;
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic stages 13-14
CC (PubMed:22084112). During embryonic and larval development, expressed
CC in the ventral nerve cord (VNC) in a subset of peripheral nervous
CC system neurons including C4da (at protein level) (PubMed:22084112,
CC PubMed:21338947, PubMed:24746793). {ECO:0000269|PubMed:21338947,
CC ECO:0000269|PubMed:22084112, ECO:0000269|PubMed:24746793}.
CC -!- INDUCTION: Induced by neuronal activity in C4da neurons.
CC {ECO:0000269|PubMed:24746793}.
CC -!- DOMAIN: The fibronectin type-III, SPRY and coil-coil domains are
CC necessary for C4da axon patterning. {ECO:0000269|PubMed:22084112}.
CC -!- DISRUPTION PHENOTYPE: Defective axonal patterning of terminal processes
CC in class IV nociceptive sensory neurons (C4da), including defective
CC contralateral projections in ddaC and vdaB neurons, during larval
CC development (PubMed:22084112, PubMed:21338947, PubMed:24746793).
CC Defective larval locomotion behavior (PubMed:22084112). Defective
CC targeting of R8 photoreceptor growth cones to the medulla layer during
CC eye development (PubMed:27743477). {ECO:0000269|PubMed:21338947,
CC ECO:0000269|PubMed:22084112, ECO:0000269|PubMed:24746793,
CC ECO:0000269|PubMed:27743477}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY251387; AAP51207.1; -; mRNA.
DR EMBL; AE014134; AAF52977.3; -; Genomic_DNA.
DR EMBL; AE014134; ADV37036.1; -; Genomic_DNA.
DR EMBL; BT003527; AAO39531.1; -; mRNA.
DR RefSeq; NP_001188786.1; NM_001201857.2. [M9MRI4-1]
DR RefSeq; NP_723600.2; NM_164935.3. [M9MRI4-2]
DR AlphaFoldDB; M9MRI4; -.
DR IntAct; M9MRI4; 3.
DR STRING; 7227.FBpp0293057; -.
DR PaxDb; M9MRI4; -.
DR DNASU; 34453; -.
DR EnsemblMetazoa; FBtr0080096; FBpp0079685; FBgn0051721. [M9MRI4-2]
DR EnsemblMetazoa; FBtr0304114; FBpp0293057; FBgn0051721. [M9MRI4-1]
DR GeneID; 34453; -.
DR KEGG; dme:Dmel_CG31721; -.
DR UCSC; CG31721-RA; d. melanogaster.
DR CTD; 114088; -.
DR FlyBase; FBgn0051721; Trim9.
DR VEuPathDB; VectorBase:FBgn0051721; -.
DR eggNOG; KOG4367; Eukaryota.
DR GeneTree; ENSGT00940000170097; -.
DR OMA; PDTICTI; -.
DR PhylomeDB; M9MRI4; -.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; M9MRI4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 34453; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Trim9; fly.
DR GenomeRNAi; 34453; -.
DR PRO; PR:M9MRI4; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051721; Expressed in lateral cord neuron (Drosophila) and 49 other tissues.
DR ExpressionAtlas; M9MRI4; baseline and differential.
DR GO; GO:0044295; C:axonal growth cone; IMP:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:UniProtKB.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0048936; P:peripheral nervous system neuron axonogenesis; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:UniProtKB.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR CDD; cd00063; FN3; 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; IPR003649; Bbox_C.
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; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 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; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Metal-binding;
KW Neurogenesis; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..740
FT /note="E3 ubiquitin-protein ligase TRIM9"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440178"
FT DOMAIN 399..459
FT /note="COS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00586"
FT DOMAIN 474..567
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 549..736
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 7..30
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 195..244
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 250..291
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 64..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..324
FT /evidence="ECO:0000255"
FT COMPBIAS 81..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 464..474
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_058962"
SQ SEQUENCE 740 AA; 80192 MW; FE72064EFDF581B3 CRC64;
MEDELRCPTC KQLYANPVLL PCFHALCLGC ALDIQTPYSP GSALPGAVNG AGAASAAGHN
GLHGNGGGAG GGAAAPVTNP NGPGTRHSSH SSAASTASSN TGSESVTSDQ DQSDKVSIFS
EADSGVVCCS NTSRPVSYAG TGLLPGVGNV VAPPGAAYCL TCPLCRKLVF FDDGGVRNLP
TYRAMEAIVD RFCAREALRC QMCETDPKVA SLICEQCEIR YCDACRELTH PARGPLAKHT
LVKPRGAAQQ RESVCGEHEE TLSQYCLSCK APACGLCIGE LRHQAHDVQS INVTCKAQKT
ELSHNLQQLS EKARSTTEFI QRLKGMSDKV TESCMEFERL VHAQCEALIQ AIHDRREYLL
EAIRMDKDTK IRILKDQQSN CTGKLQQTTG LIQFCIEALK ETDSAAFLQV GSMLINRVTN
TDMTWHQEVT NAAPRVSPIV DLTLDDAALA RAIDNLNFIQ MRAVKDGDER CPAAPMTPTI
LPSDCSAENN SVTVAWQPPN HSFVEGYVLE LDDGSGGEFR EVYCGKETIC TVDGLHFNSM
YNARVKAFNS AGEGEYSELI GLQTAEVAWF TFDPVLSGGA GSGLIFSKNN ATVSVEGWEH
RVALGSVGFS RGVHYWEFTI DNYTADTDPA FGVARIDVAR NKMLGKDEKS FAMYIDRQRS
WFQHNSIHER RVEGGITTGS TIGVLLDLER HTLSFLVNEM PQGSVAFRDL YGVFYPAVSI
NRGVTLTMHT AMDAPKMDYF
