CTIF_MOUSE
ID CTIF_MOUSE Reviewed; 600 AA.
AC Q6PEE2; Q6A069;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=CBP80/20-dependent translation initiation factor;
GN Name=Ctif; Synonyms=Gm672, Kiaa0427;
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 MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-600 (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP 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 TISSUE SPECIFICITY.
RX PubMed=19648179; DOI=10.1101/gad.1823409;
RA Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA Kim Y.K.;
RT "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding
RT protein CBP80/20-dependent translation.";
RL Genes Dev. 23:2033-2045(2009).
CC -!- FUNCTION: Specifically required for the pioneer round of mRNA
CC translation mediated by the cap-binding complex (CBC), that takes place
CC during or right after mRNA export via the nuclear pore complex (NPC).
CC Acts via its interaction with the NCBP1/CBP80 component of the CBC
CC complex and recruits the 40S small subunit of the ribosome via eIF3. In
CC contrast, it is not involved in steady state translation, that takes
CC place when the CBC complex is replaced by cytoplasmic cap-binding
CC protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD),
CC the pioneer round of mRNA translation mediated by the cap-binding
CC complex playing a central role in nonsense-mediated mRNA decay (NMD)
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NCBP1/CBP80; the interaction is direct.
CC Associates with the eukaryotic translation initiation factor 3 (eIF-3)
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PEE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PEE2-2; Sequence=VSP_038120;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19648179}.
CC -!- SIMILARITY: Belongs to the CTIF family. {ECO:0000305}.
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DR EMBL; BC058104; AAH58104.1; -; mRNA.
DR EMBL; AK172949; BAD32227.1; -; mRNA.
DR CCDS; CCDS37861.1; -. [Q6PEE2-2]
DR RefSeq; NP_958742.2; NM_201354.2.
DR AlphaFoldDB; Q6PEE2; -.
DR SMR; Q6PEE2; -.
DR BioGRID; 234598; 3.
DR STRING; 10090.ENSMUSP00000129974; -.
DR iPTMnet; Q6PEE2; -.
DR PhosphoSitePlus; Q6PEE2; -.
DR jPOST; Q6PEE2; -.
DR MaxQB; Q6PEE2; -.
DR PaxDb; Q6PEE2; -.
DR PeptideAtlas; Q6PEE2; -.
DR PRIDE; Q6PEE2; -.
DR ProteomicsDB; 285218; -. [Q6PEE2-1]
DR ProteomicsDB; 285219; -. [Q6PEE2-2]
DR DNASU; 269037; -.
DR GeneID; 269037; -.
DR KEGG; mmu:269037; -.
DR UCSC; uc008fqf.2; mouse. [Q6PEE2-1]
DR CTD; 9811; -.
DR MGI; MGI:2685518; Ctif.
DR eggNOG; KOG3942; Eukaryota.
DR InParanoid; Q6PEE2; -.
DR OrthoDB; 578545at2759; -.
DR PhylomeDB; Q6PEE2; -.
DR BioGRID-ORCS; 269037; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ctif; mouse.
DR PRO; PR:Q6PEE2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6PEE2; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008494; F:translation activator activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nonsense-mediated mRNA decay;
KW Phosphoprotein; Reference proteome; Translation regulation.
FT CHAIN 1..600
FT /note="CBP80/20-dependent translation initiation factor"
FT /id="PRO_0000050755"
FT DOMAIN 378..579
FT /note="MIF4G"
FT REGION 1..305
FT /note="Interaction with NCBP1/CBP80"
FT /evidence="ECO:0000250"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43310"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43310"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43310"
FT VAR_SEQ 359
FT /note="R -> RDIPNPTETSAPLRCVLCVPHVPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038120"
FT CONFLICT 383
FT /note="I -> S (in Ref. 2; BAD32227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 67831 MW; C648CFDEBC94D8AD CRC64;
MENSSAASAS SEAGSSRSQE IEELERFIDS YVLEYQVQGL LTDKTEGDGE SQRTQSHISQ
WTADCREQLD GSCSFSRGRA PPQQNGNKDN SLDMLGTDIW AANTFDSFSG ATWDLQPEKL
DFTQFHRKVR HTPKQPLPHI DREGCGKGKL EDGDGISLND IEKVLPTWQG YHPMPHEAEI
AHTKKLFRRR RNDRRRQQRP PGGNKPQQHG DHQPGSAKHN RDHQKSYQGG SGPHPSGRPT
HHGYSQNRRW HHGNMKHPPG DKGEAGSHRN AKETVTVENP KLEDGPGDTG HSGLEPPCSP
DTLTPAASER PTPQLPGGPE AEIKHKDTVL PERLRERPKI TLLQSSKDRL RRRLKEKDRD
EVAVETSSPQ PSKMDRLMEI LNIMRNNSSD VDAKLTSFME EAQNSTNSEE MLGEIVRTIY
QKAVSDRSFA FTAAKLCDKM ALFMVEGTKF RSLLLNMLQK DFTVREELQQ QDVERWLGFI
TFLCEVFGTM RSSTGEPFRV LVCPIYTCLR ELLQSQDVKE DAVLCCSMEL QSTGRLLEEQ
LPEMMTELLA SARDKMLCPS ESMLTRSLLL EVIELHANSW NPLTPPITQY YNRTIQKLTA
