IF31_ARATH
ID IF31_ARATH Reviewed; 520 AA.
AC Q6NLP2; Q9C8N4;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Translation initiation factor IF3-1, mitochondrial {ECO:0000305};
DE Short=AtIF3-1 {ECO:0000303|PubMed:25630975};
DE AltName: Full=AtINFC-1 {ECO:0000303|PubMed:25630975};
DE Flags: Precursor;
GN Name=IF3-1 {ECO:0000303|PubMed:25630975};
GN OrderedLocusNames=At1g34360 {ECO:0000312|Araport:AT1G34360};
GN ORFNames=F7P12.8 {ECO:0000312|EMBL:AAG51900.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=25630975; DOI=10.1007/s11120-015-0074-4;
RA Nesbit A.D., Whippo C., Hangarter R.P., Kehoe D.M.;
RT "Translation initiation factor 3 families: what are their roles in
RT regulating cyanobacterial and chloroplast gene expression?";
RL Photosyn. Res. 126:147-159(2015).
CC -!- FUNCTION: IF-3 binds to the 30S ribosomal subunit and shifts the
CC equilibrum between 70S ribosomes and their 50S and 30S subunits in
CC favor of the free subunits, thus enhancing the availability of 30S
CC subunits on which protein synthesis initiation begins.
CC {ECO:0000250|UniProtKB:P0A707}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0A707}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25630975}.
CC -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023913; AAG51900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31702.1; -; Genomic_DNA.
DR EMBL; BT012288; AAS76775.1; -; mRNA.
DR PIR; H86467; H86467.
DR RefSeq; NP_174696.2; NM_103159.4.
DR AlphaFoldDB; Q6NLP2; -.
DR SMR; Q6NLP2; -.
DR STRING; 3702.AT1G34360.1; -.
DR PaxDb; Q6NLP2; -.
DR PRIDE; Q6NLP2; -.
DR EnsemblPlants; AT1G34360.1; AT1G34360.1; AT1G34360.
DR GeneID; 840338; -.
DR Gramene; AT1G34360.1; AT1G34360.1; AT1G34360.
DR KEGG; ath:AT1G34360; -.
DR Araport; AT1G34360; -.
DR TAIR; locus:2036309; AT1G34360.
DR eggNOG; ENOG502QWD8; Eukaryota.
DR HOGENOM; CLU_524159_0_0_1; -.
DR InParanoid; Q6NLP2; -.
DR OrthoDB; 1139287at2759; -.
DR PhylomeDB; Q6NLP2; -.
DR PRO; PR:Q6NLP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NLP2; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR Gene3D; 3.10.20.80; -; 1.
DR Gene3D; 3.30.110.10; -; 1.
DR InterPro; IPR036788; T_IF-3_C_sf.
DR InterPro; IPR036787; T_IF-3_N_sf.
DR InterPro; IPR001288; Translation_initiation_fac_3.
DR InterPro; IPR019814; Translation_initiation_fac_3_N.
DR PANTHER; PTHR10938; PTHR10938; 1.
DR Pfam; PF05198; IF3_N; 1.
DR SUPFAM; SSF54364; SSF54364; 1.
DR SUPFAM; SSF55200; SSF55200; 1.
DR TIGRFAMs; TIGR00168; infC; 1.
PE 2: Evidence at transcript level;
KW Initiation factor; Mitochondrion; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 67..520
FT /note="Translation initiation factor IF3-1, mitochondrial"
FT /id="PRO_0000439375"
FT REGION 271..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 520 AA; 58582 MW; 5A117CB259394B4A CRC64;
MAIWRIINRS YLKYASNQLT RNYYTQVCLA SSTHVVKQTT KLSSFDIPNS DICTRPSNIF
QNLRFLATSA QTRKKEAEVD SDGPRLNEKI TGDYVRLVSE EGHCVVSLRE ALRRAKELQC
DLVEVQRDAK PPVCKIVKYS LELYKKAKVG KERAKAKRAE AIRPDIKEIR FTPKIEAKDL
KFKSDQALKL MESGYRVKCL AVPDKDKHKE LEPEKLLELL FRFTCFIGDA LVESWPEADR
KGAVVIVRHA KFGPPKKGGV KLMKDIDIKS ARVKEESPKP DSSKAGVATV DDQEDIEKSE
PRFSVEQAQP VKFQNAYAKR EPSSEFSGGR DASRFEPQSP NQHVNPQRPR FSNQAPNQQP
TGRFDPQSPN QPPSAPRPQF PNQQPTGRFD PQFPSQPPRP QFPNQAPNQQ STGRFNPQFP
NQRPSPPQSR FPDQAPNQQP SGPSPNRHPD RQGPPPRFQN QAPNQQPTGR FEPQPPNPPR
APPRPQTRLP NETSNEQPTA PGRSSGPASG YGIFSTPKTK
