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IFIT3_PANTR
ID   IFIT3_PANTR             Reviewed;         490 AA.
AC   A5A6J9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Interferon-induced protein with tetratricopeptide repeats 3;
DE            Short=IFIT-3;
GN   Name=IFIT3;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA   Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA   Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT   "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT   large potential divergence of the transcriptome.";
RL   Gene 399:1-10(2007).
CC   -!- FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of
CC       cellular as well as viral processes, cell migration, proliferation,
CC       signaling, and viral replication. Enhances MAVS-mediated host antiviral
CC       responses by serving as an adapter bridging TBK1 to MAVS which leads to
CC       the activation of TBK1 and phosphorylation of IRF3 and phosphorylated
CC       IRF3 translocates into nucleus to promote antiviral gene transcription.
CC       Exhibits an antiproliferative activity via the up-regulation of cell
CC       cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally,
CC       CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in
CC       the nucleus and exports it to the cytoplasm for ubiquitin-dependent
CC       degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby
CC       increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21
CC       by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively
CC       regulate the apoptotic effects of IFIT2 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of an interferon-dependent multiprotein complex, at
CC       least composed of IFIT1, IFIT2 and IFIT3 (By similarity). Interacts
CC       with IFIT1 and IFIT2 (By similarity). Interacts (via N-terminus) with
CC       MAVS, TBK1, TRAF6 and DDX58 (By similarity). Interacts with COPS5 (By
CC       similarity). {ECO:0000250|UniProtKB:O14879}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14879}.
CC       Mitochondrion {ECO:0000250|UniProtKB:O14879}.
CC   -!- SIMILARITY: Belongs to the IFIT family. {ECO:0000305}.
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DR   EMBL; AB222127; BAF62372.1; -; mRNA.
DR   RefSeq; NP_001182075.1; NM_001195146.1.
DR   AlphaFoldDB; A5A6J9; -.
DR   SMR; A5A6J9; -.
DR   GeneID; 738542; -.
DR   KEGG; ptr:738542; -.
DR   CTD; 3437; -.
DR   InParanoid; A5A6J9; -.
DR   OrthoDB; 460948at2759; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEA:InterPro.
DR   GO; GO:0051607; P:defense response to virus; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR024122; Interferon-induced_IFIT3.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR10271:SF3; PTHR10271:SF3; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   Pfam; PF13181; TPR_8; 3.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Antiviral defense; Cytoplasm; Immunity; Innate immunity; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..490
FT                   /note="Interferon-induced protein with tetratricopeptide
FT                   repeats 3"
FT                   /id="PRO_0000295305"
FT   REPEAT          51..84
FT                   /note="TPR 1"
FT   REPEAT          94..127
FT                   /note="TPR 2"
FT   REPEAT          136..169
FT                   /note="TPR 3"
FT   REPEAT          172..206
FT                   /note="TPR 4"
FT   REPEAT          207..240
FT                   /note="TPR 5"
FT   REPEAT          241..274
FT                   /note="TPR 6"
FT   REPEAT          415..448
FT                   /note="TPR 7"
FT   REPEAT          450..481
FT                   /note="TPR 8"
FT   REGION          386..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14879"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14879"
SQ   SEQUENCE   490 AA;  55978 MW;  96D0B4FCBD7F7CFC CRC64;
     MSEVTKNSLE KILPQLKCHF TWNLFKEESV SRDLEDRVCN QIEFLNTEFK ATMYNLLAYI
     KHLDGNNEAA LECLRQAEEL IQQEHADQAE IRSLVTWGNY VWVYYHLGRL SDAQIYVDKV
     KQTCKKFSNP YSIEYSELDC EEGWTQLKCG RNERAKVCFE KALEEKPNNP EFSSGLAIAM
     YHLDNNPEKQ FSTDVLKQAI ELSPDNQYVK VLLGLKLQKM NKEAEGEQFV EEALEKAPCQ
     TDVLRSAAKF YRRKGDLDKA IELFQRVLES TPNNGYLYHQ IGCCYKAKVR QMQNTGESEA
     SGNKEMIEAL KQYAMDYSNK ALEKGLNPLN AYSDCAEFLE TECYQTPFNK EVPDAEKQQS
     HQRYCNLQKY NGKSEDTAVQ HGLEGLSISK KSTDKEEIKD QPQNVSENLL PQNAPNYWYL
     QGLIHKQNGD LLQAAKCYEK ELGRLLRDAP SGIGSIFLSA SELEDGSEEM GQGAVSSSPR
     ELLSNSEQLN
 
 
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