TRI13_XENTR
ID TRI13_XENTR Reviewed; 408 AA.
AC F6ZQ54;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Tripartite motif containing 13;
GN Name=trim13;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
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; AAMC01049541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6ZQ54; -.
DR SMR; F6ZQ54; -.
DR STRING; 8364.ENSXETP00000034221; -.
DR PaxDb; F6ZQ54; -.
DR PRIDE; F6ZQ54; -.
DR Ensembl; ENSXETT00000034221; ENSXETP00000034221; ENSXETG00000015691.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_053708_0_0_1; -.
DR InParanoid; F6ZQ54; -.
DR OMA; NLQVNYS; -.
DR TreeFam; TF331669; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000015691; Expressed in heart and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..408
FT /note="Tripartite motif containing 13"
FT /id="PRO_0000416766"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 89..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 408 AA; 46602 MW; 39F9AD3E9A3F6DB1 CRC64;
MEVLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLDGVLEE NSRTMQWRPS SFKCPTCRKE
TPTMGVNGLQ VNYLLKGIVE KYNKIKVSPK MPVCKEHSDQ PLNIFCSTDL KLICGSCATT
GEHKKHVFSS IGDAYIQEKS SLETLFQGVE EWNSKEVHSH LDTLESNKRK ALHSLAKESD
KVKAYFEKLQ YLLEQKKNEI LSDFETLKLA VMQAYDTEIN KLHTVLSEQR KACNIVEDLK
NISDPFMFLQ QMQEFRDKMT FIKEAPLTTG QDVNVNPAMK EFDTSMWDSI KLGEVDKLSL
PQDTTSKKEP GDAKTLHSLK PILVVACLIL LLVTFLCAYP FIDSLPTFTI DLQVISSYFF
TTTAKAANLT ILFWEQLSEE LLILKQRCQT YVSVFLENVA EFVCKYKL
