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IF34_ARATH
ID   IF34_ARATH              Reviewed;         281 AA.
AC   Q94B52; Q9SUH7;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Translation initiation factor IF3-4, chloroplastic {ECO:0000305};
DE            Short=AtIF3-4 {ECO:0000303|PubMed:25630975};
DE   AltName: Full=AtINFC-4 {ECO:0000303|PubMed:25630975};
DE   AltName: Full=Protein SVR9-LIKE 1 {ECO:0000303|PubMed:27535792};
DE   Flags: Precursor;
GN   Name=IF3-4 {ECO:0000303|PubMed:25630975};
GN   Synonyms=SVR9L1 {ECO:0000303|PubMed:27535792};
GN   OrderedLocusNames=At4g30690 {ECO:0000312|Araport:AT4G30690};
GN   ORFNames=T10C21.40 {ECO:0000312|EMBL:CAB52442.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27535792; DOI=10.1104/pp.15.02040;
RA   Zheng M., Liu X., Liang S., Fu S., Qi Y., Zhao J., Shao J., An L., Yu F.;
RT   "Chloroplast translation initiation factors regulate leaf variegation and
RT   development.";
RL   Plant Physiol. 172:1117-1130(2016).
CC   -!- FUNCTION: Chloroplast translation initiation factor that is essential
CC       for the coordination of leaf and chloroplast development
CC       (PubMed:27535792). IF-3 binds to the 30S ribosomal subunit and shifts
CC       the 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 (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_00080, ECO:0000269|PubMed:27535792}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00080}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:25630975, ECO:0000269|PubMed:27535792}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:27535792}.
CC   -!- SIMILARITY: Belongs to the IF-3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00080}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB52442.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL109787; CAB52442.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161577; CAB79787.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85796.1; -; Genomic_DNA.
DR   EMBL; AY042848; AAK68788.1; -; mRNA.
DR   EMBL; AY072500; AAL66915.1; -; mRNA.
DR   PIR; B85359; B85359.
DR   RefSeq; NP_567851.1; NM_119215.4.
DR   AlphaFoldDB; Q94B52; -.
DR   SMR; Q94B52; -.
DR   STRING; 3702.AT4G30690.1; -.
DR   iPTMnet; Q94B52; -.
DR   PaxDb; Q94B52; -.
DR   PRIDE; Q94B52; -.
DR   ProteomicsDB; 228881; -.
DR   EnsemblPlants; AT4G30690.1; AT4G30690.1; AT4G30690.
DR   GeneID; 829192; -.
DR   Gramene; AT4G30690.1; AT4G30690.1; AT4G30690.
DR   KEGG; ath:AT4G30690; -.
DR   Araport; AT4G30690; -.
DR   TAIR; locus:2131929; AT4G30690.
DR   eggNOG; ENOG502QUHV; Eukaryota.
DR   HOGENOM; CLU_054919_3_1_1; -.
DR   InParanoid; Q94B52; -.
DR   OMA; FRDRNMT; -.
DR   OrthoDB; 1344007at2759; -.
DR   PhylomeDB; Q94B52; -.
DR   PRO; PR:Q94B52; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94B52; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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   HAMAP; MF_00080; IF_3; 1.
DR   InterPro; IPR036788; T_IF-3_C_sf.
DR   InterPro; IPR036787; T_IF-3_N_sf.
DR   InterPro; IPR019813; Translation_initiation_fac3_CS.
DR   InterPro; IPR001288; Translation_initiation_fac_3.
DR   InterPro; IPR019815; Translation_initiation_fac_3_C.
DR   InterPro; IPR019814; Translation_initiation_fac_3_N.
DR   PANTHER; PTHR10938; PTHR10938; 1.
DR   Pfam; PF00707; IF3_C; 1.
DR   Pfam; PF05198; IF3_N; 1.
DR   SUPFAM; SSF54364; SSF54364; 1.
DR   SUPFAM; SSF55200; SSF55200; 1.
DR   TIGRFAMs; TIGR00168; infC; 1.
DR   PROSITE; PS00938; IF3; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Initiation factor; Plastid; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..281
FT                   /note="Translation initiation factor IF3-4, chloroplastic"
FT                   /id="PRO_0000439377"
FT   REGION          63..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31823 MW;  A93BBA6678F38FE2 CRC64;
     MAGITSTVGF NAILAGATKT VSHPVKSKLF GLRLCVPEFS IVSLSPYHHR RCPAITCRYG
     GGGGGGSRFP GDRRGRQKES EDDDSLDISA IRSATVRLID DQQNMIGLVS KEEAVRRAED
     AELDLVILSP DADPPVVRMM DYSKYRYEQQ KRKKEQQKKT TRMDLKELKM GYNIDQHDYS
     VRMRAARKFL QDGDKVKVIV NMKGRENEFR NIAIELLRRF QTEIGELGTE ESKNFRDRNL
     FIVLVPNKEV IRKVQEPPPK KKKKPADDKV SAANITATQD I
 
 
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