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PSBS_ARATH
ID   PSBS_ARATH              Reviewed;         265 AA.
AC   Q9XF91; Q56XH2; Q94EI1; Q9ST34;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Photosystem II 22 kDa protein, chloroplastic {ECO:0000305};
DE   AltName: Full=CP22 {ECO:0000303|PubMed:10366881};
DE   AltName: Full=Protein NONPHOTOCHEMICAL QUENCHING 4 {ECO:0000303|PubMed:10667783};
DE   AltName: Full=Protein PHOTOSYSTEM II SUBUNIT S {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PSBS {ECO:0000303|PubMed:10366881};
GN   Synonyms=NPQ4 {ECO:0000303|PubMed:10667783}; OrderedLocusNames=At1g44575;
GN   ORFNames=T18F15.3;
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].
RX   PubMed=10366881; DOI=10.1016/s1360-1385(99)01419-3;
RA   Jansson S.;
RT   "A guide to the Lhc genes and their relatives in Arabidopsis.";
RL   Trends Plant Sci. 4:236-240(1999).
RN   [2]
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   [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].
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 111-265.
RC   STRAIN=cv. Landsberg erecta;
RA   Kuno N., Muramatsu T., Hamazato F., Furuya M.;
RT   "Large-scale screening of phytochrome-regulated genes in etiolated
RT   seedlings of Arabidopsis thaliana using fluorescent differential display.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10667783; DOI=10.1038/35000131;
RA   Li X.P., Bjorkman O., Shih C., Grossman A.R., Rosenquist M., Jansson S.,
RA   Niyogi K.K.;
RT   "A pigment-binding protein essential for regulation of photosynthetic light
RT   harvesting.";
RL   Nature 403:391-395(2000).
CC   -!- FUNCTION: Plays an important role in non-photochemical quenching, a
CC       process maintains the balance between dissipation and utilization of
CC       light energy to minimize generation of oxidizing molecules, thereby
CC       protecting the plant against photo-oxidative damage. Is not necessary
CC       for efficient light harvesting and photosynthesis.
CC       {ECO:0000269|PubMed:10667783}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:10667783}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9XF91-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: Non-photochemical quenching phenotype.
CC       {ECO:0000269|PubMed:10667783}.
CC   -!- SIMILARITY: Belongs to the ELIP/psbS family. {ECO:0000305}.
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DR   EMBL; AF134131; AAD28778.1; -; mRNA.
DR   EMBL; AC084807; AAK43481.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32039.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60500.1; -; Genomic_DNA.
DR   EMBL; AF410304; AAK95290.1; -; mRNA.
DR   EMBL; BT002251; AAN72262.1; -; mRNA.
DR   EMBL; AK221702; BAD95419.1; -; mRNA.
DR   EMBL; AB015859; BAA84769.1; -; mRNA.
DR   PIR; T52313; T52313.
DR   RefSeq; NP_001319163.1; NM_001333231.1. [Q9XF91-1]
DR   RefSeq; NP_175092.1; NM_103552.4. [Q9XF91-1]
DR   AlphaFoldDB; Q9XF91; -.
DR   SMR; Q9XF91; -.
DR   BioGRID; 26258; 8.
DR   STRING; 3702.AT1G44575.1; -.
DR   iPTMnet; Q9XF91; -.
DR   PaxDb; Q9XF91; -.
DR   PRIDE; Q9XF91; -.
DR   ProteomicsDB; 226005; -. [Q9XF91-1]
DR   EnsemblPlants; AT1G44575.1; AT1G44575.1; AT1G44575. [Q9XF91-1]
DR   EnsemblPlants; AT1G44575.3; AT1G44575.3; AT1G44575. [Q9XF91-1]
DR   GeneID; 841033; -.
DR   Gramene; AT1G44575.1; AT1G44575.1; AT1G44575. [Q9XF91-1]
DR   Gramene; AT1G44575.3; AT1G44575.3; AT1G44575. [Q9XF91-1]
DR   KEGG; ath:AT1G44575; -.
DR   Araport; AT1G44575; -.
DR   TAIR; locus:2823639; AT1G44575.
DR   eggNOG; ENOG502SI3U; Eukaryota.
DR   HOGENOM; CLU_090803_0_0_1; -.
DR   InParanoid; Q9XF91; -.
DR   OMA; NAAQISW; -.
DR   PhylomeDB; Q9XF91; -.
DR   BioCyc; MetaCyc:AT1G44575-MON; -.
DR   PRO; PR:Q9XF91; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XF91; baseline and differential.
DR   Genevisible; Q9XF91; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0009517; C:PSII associated light-harvesting complex II; TAS:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0016168; F:chlorophyll binding; TAS:TAIR.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0051738; F:xanthophyll binding; TAS:TAIR.
DR   GO; GO:0010196; P:nonphotochemical quenching; IMP:TAIR.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Membrane; Photosynthesis;
KW   Photosystem II; Plastid; Reference proteome; Repeat; Thylakoid;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..265
FT                   /note="Photosystem II 22 kDa protein, chloroplastic"
FT                   /id="PRO_0000007805"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          54..158
FT                   /note="1"
FT   REPEAT          159..264
FT                   /note="2"
FT   CONFLICT        5
FT                   /note="M -> F (in Ref. 4; AAK95290/AAN72262)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  28008 MW;  0D585321DE6675D6 CRC64;
     MAQTMLLTSG VTAGHFLRNK SPLAQPKVHH LFLSGNSPVA LPSRRQSFVP LALFKPKTKA
     APKKVEKPKS KVEDGIFGTS GGIGFTKANE LFVGRVAMIG FAASLLGEAL TGKGILAQLN
     LETGIPIYEA EPLLLFFILF TLLGAIGALG DRGKFVDDPP TGLEKAVIPP GKNVRSALGL
     KEQGPLFGFT KANELFVGRL AQLGIAFSLI GEIITGKGAL AQLNIETGIP IQDIEPLVLL
     NVAFFFFAAI NPGNGKFITD DGEES
 
 
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