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STR12_ARATH
ID   STR12_ARATH             Reviewed;         299 AA.
AC   Q93WI0; O23727; Q8LCM5;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Rhodanese-like/PpiC domain-containing protein 12, chloroplastic;
DE   AltName: Full=Sulfurtransferase 12;
DE            Short=AtStr12;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g19370; ORFNames=F7K24.120;
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 [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=9356517; DOI=10.1073/pnas.94.23.12722;
RA   Babiychuk E., Fuangthong M., Van Montagu M., Inze D., Kushnir S.;
RT   "Efficient gene tagging in Arabidopsis thaliana using a gene trap
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12722-12727(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
RA   Bartels A., Mock H.P., Papenbrock J.;
RT   "Differential expression of Arabidopsis sulfurtransferases under various
RT   growth conditions.";
RL   Plant Physiol. Biochem. 45:178-187(2007).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-82, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER ALA-81, 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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB06699.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; Z86095; CAB06699.1; ALT_SEQ; mRNA.
DR   EMBL; AF296837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92692.1; -; Genomic_DNA.
DR   EMBL; AF370165; AAK43980.1; -; mRNA.
DR   EMBL; AY059127; AAL15233.1; -; mRNA.
DR   EMBL; AY086512; AAM63512.1; -; mRNA.
DR   PIR; T52622; T52622.
DR   RefSeq; NP_568372.1; NM_121942.5.
DR   AlphaFoldDB; Q93WI0; -.
DR   SMR; Q93WI0; -.
DR   STRING; 3702.AT5G19370.1; -.
DR   iPTMnet; Q93WI0; -.
DR   PaxDb; Q93WI0; -.
DR   PRIDE; Q93WI0; -.
DR   ProteomicsDB; 245223; -.
DR   EnsemblPlants; AT5G19370.1; AT5G19370.1; AT5G19370.
DR   GeneID; 832057; -.
DR   Gramene; AT5G19370.1; AT5G19370.1; AT5G19370.
DR   KEGG; ath:AT5G19370; -.
DR   Araport; AT5G19370; -.
DR   TAIR; locus:2150235; AT5G19370.
DR   eggNOG; KOG2017; Eukaryota.
DR   HOGENOM; CLU_056271_0_0_1; -.
DR   InParanoid; Q93WI0; -.
DR   OMA; AVEYSMC; -.
DR   OrthoDB; 1397633at2759; -.
DR   PhylomeDB; Q93WI0; -.
DR   PRO; PR:Q93WI0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q93WI0; baseline and differential.
DR   Genevisible; Q93WI0; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chloroplast; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..81
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           82..299
FT                   /note="Rhodanese-like/PpiC domain-containing protein 12,
FT                   chloroplastic"
FT                   /id="PRO_0000416534"
FT   DOMAIN          93..183
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   DOMAIN          205..297
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   ACT_SITE        257
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   MOD_RES         82
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        5
FT                   /note="T -> A (in Ref. 5; AAM63512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="N -> D (in Ref. 5; AAM63512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="N -> D (in Ref. 5; AAM63512)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="T -> S (in Ref. 5; AAM63512)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  32980 MW;  1EFF898DDCFD1D5B CRC64;
     MFRVTGTLSA ASSPAVAAAS FSAALRLSIT PTLAIASPPH LRWFSKFSRQ FLGGRISSLR
     PRIPSPCPIR LSGFPALKMR ASFSSGSSGS SASREILVQH LLVKNNDVEL FAELQKKFLD
     GEEMSDLAAE YSICPSKKDG GILGWVKLGQ MVPEFEEAAF KAELNQVVRC RTQFGLHLLQ
     VLSEREPVKD IQVEELHSKM QDPVFMDEAQ LIDVREPNEI EIASLPGFKV FPLRQFGTWA
     PDITSKLNPE KDTFVLCKVG GRSMQVANWL QSQGFKSVYN ITGGIQAYSL KVDPSIPTY
 
 
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