TRI59_CHICK
ID TRI59_CHICK Reviewed; 408 AA.
AC Q5ZMD4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Tripartite motif-containing protein 59;
GN Name=TRIM59; ORFNames=RCJMB04_2h17;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: May serve as a multifunctional regulator for innate immune
CC signaling pathways. {ECO:0000250|UniProtKB:Q922Y2}.
CC -!- SUBUNIT: Interacts with ECSIT. {ECO:0000250|UniProtKB:Q922Y2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q922Y2}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AJ719450; CAG31109.1; -; mRNA.
DR RefSeq; NP_001026491.1; NM_001031320.1.
DR AlphaFoldDB; Q5ZMD4; -.
DR SMR; Q5ZMD4; -.
DR STRING; 9031.ENSGALP00000038403; -.
DR PaxDb; Q5ZMD4; -.
DR PRIDE; Q5ZMD4; -.
DR GeneID; 425013; -.
DR KEGG; gga:425013; -.
DR CTD; 286827; -.
DR VEuPathDB; HostDB:geneid_425013; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q5ZMD4; -.
DR OrthoDB; 635534at2759; -.
DR PhylomeDB; Q5ZMD4; -.
DR PRO; PR:Q5ZMD4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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: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:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; 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; SM00184; RING; 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; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..408
FT /note="Tripartite motif-containing protein 59"
FT /id="PRO_0000249681"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 163..247
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 408 AA; 46775 MW; AE86340E0601FC44 CRC64;
MHQFEEELTC SICYSLFEDP RVLPCSHTFC RSCLEGVIQL SSNFSIWRPL RVPLKCPNCR
SIVEIPASGT ESLPINFALK AIIEKYRQED HSDVATCSEH YRQPLNVYCL LDKKLVCGHC
LTIGKHNGHP IDDLHSAYLK EKESSGKILE QLTDKHWSDV CLLIEKLKEQ KAQCESIVQD
DKKVVVQYFK KLSETLEHKK QVLLAALDEI NRQILEEYEP HIEKLKKIRE EQLELMSLNT
SIQKEESPLV FLEKVDNVHQ RIKALKEKEL PDVKPVEVYP RVGHLLKDVW SKTEIGQINK
ILTPKIKLVP KRKLHSKNSE KERGKPEELL QAANPLSVTF IFTVIIAIAV LSFHKPISSV
VIESIPTHIS DFFGFLYQDF CTCMQNTVDV VCHKLNSLAE FLGGIVPF