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CATIN_MOUSE
ID   CATIN_MOUSE             Reviewed;         772 AA.
AC   Q9CS00;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Cactin;
GN   Name=Cactin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-772.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H., Arakawa T.,
RA   Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M., Hanagaki T.,
RA   Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H., Kawai J., Kojima Y.,
RA   Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., Miyazaki A.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Okazaki Y., Okido T., Owa C.,
RA   Saito H., Saito R., Sakai C., Sakai K., Sano H., Sasaki D., Shibata K.,
RA   Shibata Y., Shinagawa A., Shiraki T., Sogabe Y., Suzuki H., Tagami M.,
RA   Tagawa A., Takahashi F., Tanaka T., Tejima Y., Toya T., Yamamura T.,
RA   Yasunishi A., Yoshida K., Yoshino M., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=20829348; DOI=10.1074/jbc.m110.139113;
RA   Atzei P., Gargan S., Curran N., Moynagh P.N.;
RT   "Cactin targets the MHC class III protein IkappaB-like (IkappaBL) and
RT   inhibits NF-kappaB and interferon-regulatory factor signaling pathways.";
RL   J. Biol. Chem. 285:36804-36817(2010).
CC   -!- FUNCTION: Involved in the regulation of innate immune response (By
CC       similarity). Acts as negative regulator of Toll-like receptor,
CC       interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling
CC       pathways (By similarity). Contributes to the regulation of
CC       transcriptional activation of NF-kappa-B target genes in response to
CC       endogenous pro-inflammatory stimuli (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WUQ7}.
CC   -!- SUBUNIT: Interacts (via N-terminal domain) with NFKBIL1; the
CC       interaction occurs in a pro-inflammatory-independent manner (By
CC       similarity). Does not interact with RELA NF-kappa-B subunit (By
CC       similarity). Identified in the spliceosome C complex (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WUQ7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WUQ7}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WUQ7}. Note=Nuclear
CC       localization with a speckled expression pattern in some cells.
CC       Colocalizes with NFKBIL1 in the nucleus (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WUQ7}.
CC   -!- TISSUE SPECIFICITY: Expressed in cortex, hippocampus, cerebellum,
CC       heart, lung, kidney, liver, spleen and thymus.
CC       {ECO:0000269|PubMed:20829348}.
CC   -!- SIMILARITY: Belongs to the CACTIN family. {ECO:0000305}.
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DR   EMBL; AC155937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK010963; BAB27295.1; -; mRNA.
DR   CCDS; CCDS35995.1; -.
DR   RefSeq; NP_081657.1; NM_027381.2.
DR   AlphaFoldDB; Q9CS00; -.
DR   SMR; Q9CS00; -.
DR   BioGRID; 213980; 28.
DR   STRING; 10090.ENSMUSP00000059533; -.
DR   iPTMnet; Q9CS00; -.
DR   PhosphoSitePlus; Q9CS00; -.
DR   EPD; Q9CS00; -.
DR   jPOST; Q9CS00; -.
DR   MaxQB; Q9CS00; -.
DR   PaxDb; Q9CS00; -.
DR   PRIDE; Q9CS00; -.
DR   ProteomicsDB; 265542; -.
DR   Antibodypedia; 52584; 89 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000050867; ENSMUSP00000059533; ENSMUSG00000034889.
DR   GeneID; 70312; -.
DR   KEGG; mmu:70312; -.
DR   UCSC; uc007ghf.2; mouse.
DR   CTD; 58509; -.
DR   MGI; MGI:1917562; Cactin.
DR   VEuPathDB; HostDB:ENSMUSG00000034889; -.
DR   eggNOG; KOG2370; Eukaryota.
DR   GeneTree; ENSGT00950000183102; -.
DR   HOGENOM; CLU_011759_0_0_1; -.
DR   InParanoid; Q9CS00; -.
DR   OMA; HEPYMLL; -.
DR   OrthoDB; 1252926at2759; -.
DR   PhylomeDB; Q9CS00; -.
DR   TreeFam; TF300906; -.
DR   BioGRID-ORCS; 70312; 19 hits in 75 CRISPR screens.
DR   ChiTaRS; Cactin; mouse.
DR   PRO; PR:Q9CS00; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9CS00; protein.
DR   Bgee; ENSMUSG00000034889; Expressed in dorsal pancreas and 222 other tissues.
DR   ExpressionAtlas; Q9CS00; baseline and differential.
DR   Genevisible; Q9CS00; MM.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IBA:GO_Central.
DR   GO; GO:0032688; P:negative regulation of interferon-beta production; ISS:UniProtKB.
DR   GO; GO:0032717; P:negative regulation of interleukin-8 production; ISS:UniProtKB.
DR   GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR   GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR019134; Cactin_C.
DR   InterPro; IPR018816; Cactin_central.
DR   Pfam; PF10312; Cactin_mid; 1.
DR   Pfam; PF09732; CactinC_cactus; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Developmental protein; Immunity; Innate immunity;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome; Ubl conjugation.
FT   CHAIN           1..772
FT                   /note="Cactin"
FT                   /id="PRO_0000231618"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          157..207
FT                   /evidence="ECO:0000255"
FT   COILED          247..299
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..75
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUQ7"
FT   MOD_RES         573
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUQ7"
FT   CROSSLNK        491
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUQ7"
FT   CROSSLNK        506
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WUQ7"
SQ   SEQUENCE   772 AA;  90661 MW;  4A4C6DF15D077D8B CRC64;
     MRGAGRQMGR DSRSRSRSVG RRGRKQRSRS RGRSRSRSRS RSRSRSRSRS RSRSHGRSSR
     RRREHERRRE RKRRSRGRRS DSEGEQRQKS RRRSQSLRPP RWHSQNQSSC SDSGEERAQG
     SWARKGHRRS WSPGSSASSL DSPRRSRSPG TATLALSQQQ SLQERLRLRE ERKQQEELLK
     AFETPEEKRA RRLAKKEAKE RKKREKMGWG EEYMGYTNTD NPFGDNNLLG TFIWNKALEK
     KGISHLEEKE LKERNKRIQE DNRLELQKVK QLRLEREREK AMREQELELL QREKEAEHFK
     TWEEQEDSFH LRQAKLRSKI RIRDGRAKPI DLLAKYISAE DDDLAVEMHE PYTFLNGLTV
     ADMEDLLEDI QVYMELEQGK NVDFWRDMTT ITEDEIAKLR KLEASGKGPG ERREGVNASV
     SSDVQSVFKG KTYNQLQVIF QGIEGKIRAG GPNLDMGYWE SLLQQLRAHM ARARLRERHQ
     DVLRQKLFKL KQEQGVESEP LFPILKSEPS AAHSPEPEER PPSPGTSVDP VEPVEPEEAT
     APGEAEGEAE GEAVLMEEDL IQQSLADYDA GRYSPRLLTA HELPLDAHVL EPHEDLQRLQ
     LSRQQLQATG DASESAEDIF FRRAREGMGQ DEAQFSVEMP LGGRAYLWAD KYRPRKPRFF
     NRVHTGFEWN KYNQTHYDFD NPPPKIVQGY KFNIFYPDLI RKRATPEYFL EACADNRDFA
     ILRFHAGPPY EDIAFKIVSR EWEYSHRHGF RCQFANGIFQ LWFHFKRYRY RR
 
 
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