ID TRI13_DANRE Reviewed; 404 AA.
AC Q503I2; F1R8C7;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Tripartite motif-containing 13;
GN Name=trim13; ORFNames=zgc:110578;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin ligase involved in the retrotranslocation and
CC turnover of membrane and secretory proteins from the ER through a set
CC of processes named ER-associated degradation (ERAD). This process acts
CC on misfolded proteins as well as in the regulated degradation of
CC correctly folded proteins (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Note=Also concentrates at
CC the perinuclear endoplasmic reticulum. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal transmembrane domain is indispensable for the
CC localization to the ER. {ECO:0000250}.
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DR EMBL; CU855930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC095319; AAH95319.1; -; mRNA.
DR RefSeq; NP_001018439.1; NM_001020603.1.
DR RefSeq; XP_009303017.1; XM_009304742.2.
DR AlphaFoldDB; Q503I2; -.
DR SMR; Q503I2; -.
DR STRING; 7955.ENSDARP00000013495; -.
DR PaxDb; 7955-ENSDARP00000013495; -.
DR GeneID; 553630; -.
DR KEGG; dre:553630; -.
DR AGR; ZFIN:ZDB-GENE-050522-516; -.
DR CTD; 10206; -.
DR ZFIN; ZDB-GENE-050522-516; trim13.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q503I2; -.
DR OrthoDB; 5383069at2759; -.
DR PhylomeDB; Q503I2; -.
DR Reactome; R-DRE-3134975; Regulation of innate immune responses to cytosolic DNA.
DR UniPathway; UPA00143; -.
DR ChiTaRS; trim13; zebrafish.
DR PRO; PR:Q503I2; -.
DR Proteomes; UP000000437; Alternate scaffold 9.
DR Proteomes; UP000000437; Chromosome 9.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR CDD; cd19767; Bbox2_TRIM13_C-XI; 1.
DR CDD; cd16762; RING-HC_TRIM13_C-V; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR027370; Znf-RING_euk.
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 PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF609; E3 UBIQUITIN-PROTEIN LIGASE TRIM13; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Ligase; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..404
FT /note="Tripartite motif-containing 13"
FT /id="PRO_0000416765"
FT TRANSMEM 102..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 87..129
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 186..236
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 404 AA; 45867 MW; C43EB2671E027FAD CRC64;
MELLEEDLTC PICCCLFEDP RVLPCSHSFC KKCLEGILDG NRSPTWRPPF KCPTCRKETV
HNGIASLQVN YSLRGIVEKY NRIRVMPRMS QCRVHSGQPL NIFCATDLKL ICGFCATTGD
HKGHKFCALE EAYEREKLAF EELFRVVEGW KGAEVHSCLE SLESAKKKAL ERVSRDADRV
SEYFDKLLRT LEHKRSEILS DLETLKLAVM QTFDPEINRL RSALEEQRRA LNIAESFRSL
SDPLTFLQQM QDFREKLRVI QGTPLPSRTD MDVSLSALQS FDVKEWDRVR LGQVDKLCAP
YESSAYLSSL PPAAAPRFTR VMWRVVLVVC ACLPALNFLP SDCLALSFQD KVVALGGFSL
PSPGEIVRWL GFCWKEAASI CTLLTELCRN CMLDLINTTS DFIS
//
