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Q80XI3 (IF4G3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 4 gamma 3

Short name=eIF-4-gamma 3
Short name=eIF-4G 3
Short name=eIF4G 3
Alternative name(s):
eIF-4-gamma II
Short name=eIF4GII
Gene names
Name:Eif4g3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1 By similarity.

Subunit structure

Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA By similarity.

Sequence similarities

Belongs to the eukaryotic initiation factor 4G family.

Contains 5 HEAT repeats.

Contains 1 MI domain.

Contains 1 MIF4G domain.

Contains 1 W2 domain.

Sequence caution

The sequence AAH23898.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH23898.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80XI3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q80XI3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1084-1102: Missing.
Isoform 3 (identifier: Q80XI3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     11-11: F → FAAGPRPAHHQF
Note: No experimental confirmation available.
Isoform 4 (identifier: Q80XI3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: P → PFAAGPRPAHHQGGFRPIQ
     1084-1102: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15791579Eukaryotic translation initiation factor 4 gamma 3
PRO_0000213330

Regions

Repeat740 – 77839HEAT 1
Domain750 – 978229MIF4G
Repeat779 – 82648HEAT 2
Repeat827 – 90074HEAT 3
Repeat901 – 93939HEAT 4
Repeat940 – 97940HEAT 5
Domain1215 – 1337123MI
Domain1410 – 1579170W2
Region134 – 16229PABPC1-binding By similarity
Region614 – 62512EIF4E-binding By similarity
Region694 – 1014321eIF3/EIF4A-binding By similarity
Region1427 – 1579153EIF4A-binding By similarity
Region1565 – 157915Necessary but not sufficient for MKNK1-binding By similarity
Coiled coil989 – 101830 Potential
Coiled coil1154 – 117623 Potential
Coiled coil1406 – 143833 Potential

Amino acid modifications

Modified residue1681Phosphothreonine Ref.5
Modified residue2301Phosphoserine By similarity
Modified residue2321Phosphoserine By similarity
Modified residue2671Phosphoserine Ref.5
Modified residue4701Phosphoserine Ref.5
Modified residue4721Phosphoserine Ref.5 Ref.6
Modified residue4901Phosphoserine By similarity
Modified residue11501Phosphoserine; by CaMK1 By similarity

Natural variations

Alternative sequence101P → PFAAGPRPAHHQGGFRPIQ in isoform 4.
VSP_026029
Alternative sequence111F → FAAGPRPAHHQF in isoform 3.
VSP_010490
Alternative sequence1084 – 110219Missing in isoform 2 and isoform 4.
VSP_010491

Experimental info

Sequence conflict1831Missing in CF743072. Ref.2
Sequence conflict4101A → G in CF743072. Ref.2
Sequence conflict4921A → P in CB522417. Ref.2
Sequence conflict13241E → G in BAC26452. Ref.1
Sequence conflict13241E → G in AAH72600. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: EB4854590D250450

FASTA1,579174,890
        10         20         30         40         50         60 
MNSQPQARSP FFQRPQIQPP RAAIPNSSPS IRPGVQTPTA VYQANQHIMM VNHLPMPYPV 

        70         80         90        100        110        120 
TQGHQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFANAYGT PFYPSQPVYQ 

       130        140        150        160        170        180 
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPASTPTP 

       190        200        210        220        230        240 
PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVFQS PSTVLRLVLS 

       250        260        270        280        290        300 
GEKKEQAGQM PETAAGEPTP EPPRTSSPTS LPPLARSSLP SPMSAALSSQ PLFTAEDKCE 

       310        320        330        340        350        360 
LPSSKEEDAP PVPSPTSCTA ASGPSLTDNS DICKKPCSVA PHDSQLISST ILINEMNGVG 

       370        380        390        400        410        420 
EKLSAKENTV GMLRQEVLPL TLELEILEHP QEELKVECTP TPIAPSMLPA FSPAPPTPPT 

       430        440        450        460        470        480 
SPPCPPVVLS AAIARSPAVA TEVQRVADEG ESLRTCLSKD AKEMQDKAES ESDGQAEETA 

       490        500        510        520        530        540 
DPQSLHSGRS PAPVQTATTA PKSWKKTKEQ TRTPDEVLEA EAEPKAEEEL AVDSVLEPEQ 

       550        560        570        580        590        600 
EKMSQGFPSE RDPSALKRGK AEEGNGEEAE PVRNGAESAS EGEGGDGNSG SADSSADGLT 

       610        620        630        640        650        660 
FPFKAESWKP ADTEGKKQYD REFLLDIQFM PACIQKPEGL PPISDVVLDK INQPRLSMRT 

       670        680        690        700        710        720 
LDPRILPRGP DFTPAFADFP RQTPGGRGVP LLNVGPRRSQ PGQRREPRKI ITVSVKEDVH 

       730        740        750        760        770        780 
LRKAENAWKP SQKRDSHADD PESIKTQELF RKVRSILNKL TPQMFNQLMK QVSALTVDTE 

       790        800        810        820        830        840 
ERLKGVIDLV FEKAIDEPSF SVAYANMCRC LVTLKVPMAD KPGNTVNFRK LLLNRCQKEF 

       850        860        870        880        890        900 
EKDKADDDVF EKKQKELEAA SAPEERTRLH DELEEAKDKA RRRSIGNIKF IGELFKLKML 

       910        920        930        940        950        960 
TEAIMHDCVV KLLKNHDEES LECLCRLLTT IGKDLDFEKA KPRMDQYFNQ MEKIVKERKT 

       970        980        990       1000       1010       1020 
SSRIRFMLQD VIDLRLCNWV SRRADQGPKT IEQIHKEAKI EEQEEQRKVQ QLMTKEKRRP 

      1030       1040       1050       1060       1070       1080 
GVQRVDEGGW NTVQGAKNSR VLDPSKFLKI TKPTIDEKIQ LVPKAQLGSW GKGSSGGAKA 

      1090       1100       1110       1120       1130       1140 
SESDALRSSA SSLNRFSPLQ PPAPSGSPSA TPLEFDSRRA LTSRGSMGRE KSDKPIPAGT 

      1150       1160       1170       1180       1190       1200 
ARPNTFLRGS SKDLLDNQSQ EEQRREMLET VKQLTGGLDA ERASTEADRS KTRELAKSEM 

      1210       1220       1230       1240       1250       1260 
CAVPAPDKPA LSEEEVERKS KSIIDEFLHI NDFKEATQCI EELSAQGPLH VFVKVGVEFT 

      1270       1280       1290       1300       1310       1320 
LERSQITRDH MGHLLYQLVQ SEKLSKQDFF KGFSETLELA DDMAIDIPHI WLYLAELVTP 

      1330       1340       1350       1360       1370       1380 
MLKEGGISMR ELIVEFSKPL LPVGRAGVLL SEILHLLCRQ MSHKKVGALW READLSWKDF 

      1390       1400       1410       1420       1430       1440 
LPEGEDVHHF LLEQKLDFTE SEGPCSSEAL SKKELSAEEL SQRLEKLIME EKADDERIFD 

      1450       1460       1470       1480       1490       1500 
WVEANLDESQ MSSPTFLRAL MTAVCKAAII ADCSTFRVDT AVIKQRVPIL LKYLDSDTEK 

      1510       1520       1530       1540       1550       1560 
ELQALYALQA SIVKLDQPAN LLRMFFDCLY DEEVISEDAF YKWESSKDPA EQAGKGVALK 

      1570 
SVTAFFTWLR EAEEESEDN 

« Hide

Isoform 2 [UniParc].

Checksum: EBE892F0BBC70182
Show »

FASTA1,560172,865
Isoform 3 [UniParc].

Checksum: 384A47C5E2EE294C
Show »

FASTA1,590176,060
Isoform 4 [UniParc].

Checksum: 05FEAAD3A5AB616D
Show »

FASTA1,578174,791

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 AND 807-1579 (ISOFORM 2), NUCLEOTIDE SEQUENCE OF 1-135 (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Adipose tissue, Head and Oviduct.
[2]The MGC Project Team
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-492.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Colon, Kidney, Liver and Mammary tumor.
[4]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168; SER-267; SER-470 AND SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK029440 mRNA. Translation: BAC26452.1.
AK050887 mRNA. Translation: BAC34445.1.
AK054068 mRNA. Translation: BAC35644.1.
CB522417 mRNA. No translation available.
CF743072 mRNA. No translation available.
BC023898 mRNA. Translation: AAH23898.1. Different initiation.
BC047531 mRNA. Translation: AAH47531.1.
BC048848 mRNA. Translation: AAH48848.1.
BC057913 mRNA. Translation: AAH57913.1.
BC072600 mRNA. Translation: AAH72600.1.
RefSeqNP_766291.2. NM_172703.3.
UniGeneMm.268903.
Mm.407375.

3D structure databases

ProteinModelPortalQ80XI3.
SMRQ80XI3. Positions 136-161, 740-981, 1208-1572.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231042. 2 interactions.
MINTMINT-1864762.

PTM databases

PhosphoSiteQ80XI3.

Proteomic databases

PaxDbQ80XI3.
PRIDEQ80XI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084214; ENSMUSP00000081232; ENSMUSG00000028760.
GeneID230861.
KEGGmmu:230861.
UCSCuc008vka.2. mouse. [Q80XI3-4]
uc008vkb.2. mouse. [Q80XI3-2]

Organism-specific databases

CTD8672.
MGIMGI:1923935. Eif4g3.

Phylogenomic databases

eggNOGNOG301289.
GeneTreeENSGT00530000063038.
HOVERGENHBG052083.
KOK03260.
PhylomeDBQ80XI3.

Gene expression databases

ArrayExpressQ80XI3.
BgeeQ80XI3.
GenevestigatorQ80XI3.

Family and domain databases

Gene3D1.25.40.180. 3 hits.
InterProIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR003307. W2_domain.
[Graphical view]
PfamPF02847. MA3. 1 hit.
PF02854. MIF4G. 1 hit.
PF02020. W2. 1 hit.
[Graphical view]
SMARTSM00515. eIF5C. 1 hit.
SM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 3 hits.
PROSITEPS51366. MI. 1 hit.
PS51363. W2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF4G3. mouse.
NextBio380218.
PROQ80XI3.
SOURCESearch...

Entry information

Entry nameIF4G3_MOUSE
AccessionPrimary (citable) accession number: Q80XI3
Secondary accession number(s): Q6GQV5 expand/collapse secondary AC list , Q80Y69, Q8BJ68, Q8BQF3, Q8C6Q3, Q8CIH0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot