TIG_ARATH
ID TIG_ARATH Reviewed; 547 AA.
AC Q8S9L5; Q56WB5; Q9FLP1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Trigger factor-like protein TIG, Chloroplastic;
DE EC=5.2.1.8;
DE AltName: Full=Immunophilin TIG;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase TIG;
DE Short=PPIase TIG;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=TIG; OrderedLocusNames=At5g55220; ORFNames=MCO15_17;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-547.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-78, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER ALA-77, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by
CC maintaining the newly synthesized protein in an open conformation.
CC Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, the
CC middle domain has PPIase activity, while the C-terminus has intrinsic
CC chaperone activity on its own. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD95133.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010071; BAB08591.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96601.1; -; Genomic_DNA.
DR EMBL; AY074845; AAL75898.1; -; mRNA.
DR EMBL; BT002296; AAN73293.1; -; mRNA.
DR EMBL; AK222129; BAD95133.1; ALT_INIT; mRNA.
DR RefSeq; NP_200333.2; NM_124904.5.
DR AlphaFoldDB; Q8S9L5; -.
DR SMR; Q8S9L5; -.
DR BioGRID; 20859; 4.
DR IntAct; Q8S9L5; 5.
DR STRING; 3702.AT5G55220.1; -.
DR iPTMnet; Q8S9L5; -.
DR PaxDb; Q8S9L5; -.
DR PRIDE; Q8S9L5; -.
DR ProteomicsDB; 246425; -.
DR EnsemblPlants; AT5G55220.1; AT5G55220.1; AT5G55220.
DR GeneID; 835615; -.
DR Gramene; AT5G55220.1; AT5G55220.1; AT5G55220.
DR KEGG; ath:AT5G55220; -.
DR Araport; AT5G55220; -.
DR TAIR; locus:2161640; AT5G55220.
DR eggNOG; ENOG502QUET; Eukaryota.
DR HOGENOM; CLU_033058_0_0_1; -.
DR InParanoid; Q8S9L5; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 1291443at2759; -.
DR PhylomeDB; Q8S9L5; -.
DR PRO; PR:Q8S9L5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S9L5; baseline and differential.
DR Genevisible; Q8S9L5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR Gene3D; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.70.1050; -; 1.
DR HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR005215; Trig_fac.
DR InterPro; IPR008880; Trigger_fac_C.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac.
DR InterPro; IPR036611; Trigger_fac_ribosome-bd_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR30560; PTHR30560; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR Pfam; PF05697; Trigger_N; 1.
DR SUPFAM; SSF102735; SSF102735; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Chloroplast; Isomerase; Plastid;
KW Reference proteome; Rotamase; Transit peptide.
FT TRANSIT 1..77
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 78..547
FT /note="Trigger factor-like protein TIG, Chloroplastic"
FT /id="PRO_0000416139"
FT DOMAIN 271..366
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT MOD_RES 78
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 410
FT /note="Q -> K (in Ref. 4; BAD95133)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="N -> K (in Ref. 4; BAD95133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 547 AA; 61734 MW; 7494BA17F822B06E CRC64;
MELCVISTTT TVKAINPFLP SITRRVSSRL FQSDSVLQFG GRLKKPISRP LDMSCVSRKI
GFFGDFMSHG GNFRLFAAAS PAVETSVKED KLPADLKVTE TVQANSSVKL SVEVPEIVCE
DCYQRVLTEF MKLSKVPGFR PKTRVPENII VGFVGRQYVL RATVESILKR TLPHAMESVT
GRALKDSIQI VSSFPDMEKA YSKLKTLSYE VVVDVVPELK WNPEDGYKNM KVVVELGDEI
DAKKACERQL RQKYKSLGAL KIVTERGLQV GDLAVVDISA TTIDEDGSTG QAIPDAESKG
FHFDTEEGNR LLPGFLDAII GIRAGESKSF TLVFPESWKQ ESLRGQRAQF TVDCKELFYR
DLPTLDDSLA DKLLPGCTTL KEVEETLAKR CQEMEQEAKE QATDNAILEQ IRKMVEVEIP
QSLFEEQGRQ FYGARLLEIQ GNMKLNEDQL ASLSSQKAVN EFLETQRESI TNIIKQNIAV
GDIFKRENLE FSTDELVKEV ENSISEFKKH KQEFDEERVK DQVQEILEGA KVLEWLKDRA
EIQYITR
