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ECSIT_RAT
ID   ECSIT_RAT               Reviewed;         434 AA.
AC   Q5XIC2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Ecsit {ECO:0000312|RGD:1359488};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION IN THE MCIA COMPLEX, AND FUNCTION.
RX   PubMed=22982022; DOI=10.1016/j.cmet.2012.08.009;
RA   Heide H., Bleier L., Steger M., Ackermann J., Drose S., Schwamb B.,
RA   Zornig M., Reichert A.S., Koch I., Wittig I., Brandt U.;
RT   "Complexome profiling identifies TMEM126B as a component of the
RT   mitochondrial complex I assembly complex.";
RL   Cell Metab. 16:538-549(2012).
CC   -!- FUNCTION: Adapter protein of the Toll-like and IL-1 receptor signaling
CC       pathway that is involved in the activation of NF-kappa-B via MAP3K1.
CC       Promotes proteolytic activation of MAP3K1. Involved in the BMP
CC       signaling pathway. Required for normal embryonic development.
CC       {ECO:0000269|PubMed:22982022}.
CC   -!- FUNCTION: As part of the MCIA complex, involved in the assembly of the
CC       mitochondrial complex I. {ECO:0000269|PubMed:22982022}.
CC   -!- SUBUNIT: Interacts with MAP3K1, SMAD4 and TRAF6. Interacts with SMAD1
CC       only after BMP4-treatment (By similarity). Part of the mitochondrial
CC       complex I assembly/MCIA complex that comprises at least the core
CC       subunits TMEM126B, NDUFAF1, ECSIT and ACAD9 and complement subunits
CC       such as COA1 and TMEM186 (By similarity) (PubMed:22982022). Interacts
CC       with NDUFAF1. Interacts with ACAD9 (By similarity). Interacts with
CC       TRIM59 (By similarity). Interacts with TMEM70 and TMEM242 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BQ95,
CC       ECO:0000250|UniProtKB:Q9QZH6, ECO:0000269|PubMed:22982022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ECSIT family. {ECO:0000305}.
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DR   EMBL; BC083762; AAH83762.1; -; mRNA.
DR   RefSeq; NP_001006987.1; NM_001006986.1.
DR   RefSeq; XP_006242700.1; XM_006242638.3.
DR   AlphaFoldDB; Q5XIC2; -.
DR   STRING; 10116.ENSRNOP00000019115; -.
DR   iPTMnet; Q5XIC2; -.
DR   PhosphoSitePlus; Q5XIC2; -.
DR   jPOST; Q5XIC2; -.
DR   PaxDb; Q5XIC2; -.
DR   PRIDE; Q5XIC2; -.
DR   Ensembl; ENSRNOT00000019115; ENSRNOP00000019115; ENSRNOG00000014128.
DR   GeneID; 300447; -.
DR   KEGG; rno:300447; -.
DR   UCSC; RGD:1359488; rat.
DR   CTD; 51295; -.
DR   RGD; 1359488; Ecsit.
DR   eggNOG; KOG3941; Eukaryota.
DR   GeneTree; ENSGT00390000005147; -.
DR   HOGENOM; CLU_046917_0_0_1; -.
DR   InParanoid; Q5XIC2; -.
DR   OMA; FGQHNVH; -.
DR   OrthoDB; 995360at2759; -.
DR   PhylomeDB; Q5XIC2; -.
DR   TreeFam; TF314943; -.
DR   Reactome; R-RNO-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR   Reactome; R-RNO-6799198; Complex I biogenesis.
DR   Reactome; R-RNO-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR   Reactome; R-RNO-975871; MyD88 cascade initiated on plasma membrane.
DR   PRO; PR:Q5XIC2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000014128; Expressed in heart and 20 other tissues.
DR   Genevisible; Q5XIC2; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR   GO; GO:0051341; P:regulation of oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0061635; P:regulation of protein complex stability; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:RGD.
DR   InterPro; IPR029342; ECIST_C.
DR   InterPro; IPR010418; ECSIT.
DR   PANTHER; PTHR13113; PTHR13113; 1.
DR   Pfam; PF06239; ECSIT; 1.
DR   Pfam; PF14784; ECSIT_C; 1.
DR   SMART; SM01284; ECSIT_Cterm; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Immunity; Innate immunity; Mitochondrion; Nucleus;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..434
FT                   /note="Evolutionarily conserved signaling intermediate in
FT                   Toll pathway, mitochondrial"
FT                   /id="PRO_0000291988"
FT   REGION          403..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  49620 MW;  04B3DEEEE8072319 CRC64;
     MSWVQVNLLA RGLSRGWGSI CRTVLSGTPF AQPSLQARGL HCSAVTHKDD VWLVPRPSEP
     QKKPIKVPAM HEDLFRPSGN GEQDKASFLN AVRSFGEHNV RKRGHVDFIY LALRKMPEFG
     VERDLSVYNL LLDVFPKEVF RPRNAIQRIF VHYPRQQECG VAVLEQMERH GVMPNTETEF
     LLIQVFGHKS YPMLKFLRMK LWFTRFKNIN PYPVPRDLPQ DPLDLAKLGL RHMEPDLSAK
     VTVYQMSLPS ESTGIEDPTQ PHIVGIQSPD QQAALARHNP SRPVFVEGPF PLWLRNKCVY
     YHILRADLPP PEEETVEEIP EEWNLYYPMQ LDLEYSRSAW DNYEFDMDEV TEGPVFAMCM
     TGAHDQATLV KWIQGLQETN PTLAQIPVVF RLARSTGELL ATTRLEGQSP PHSPPKGPEE
     DDEAIQAQQR QGQS
 
 
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