位置:首页 > 蛋白库 > CB22_ORYSJ
CB22_ORYSJ
ID   CB22_ORYSJ              Reviewed;         261 AA.
AC   P12331; Q0JLH1; Q5ZBV8;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Chlorophyll a-b binding protein 2, chloroplastic;
DE   AltName: Full=LHCII type I CAB-2;
DE            Short=LHCP;
DE   Flags: Precursor;
GN   Name=CAB2R; OrderedLocusNames=Os01g0600900, LOC_Os01g41710;
GN   ORFNames=OsJ_28992 {ECO:0000312|EMBL:EAZ44370.1}, P0518F01.17-1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2649869; DOI=10.1093/nar/17.6.2357;
RA   Luan S., Bogorad L.;
RT   "Nucleotide sequences of two genes encoding the light harvesting
RT   chlorophyll a/b binding protein of rice.";
RL   Nucleic Acids Res. 17:2357-2358(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: The light-harvesting complex (LHC) functions as a light
CC       receptor, it captures and delivers excitation energy to photosystems
CC       with which it is closely associated.
CC   -!- COFACTOR:
CC       Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and
CC       carotenoids such as lutein and neoxanthin. {ECO:0000250};
CC   -!- SUBUNIT: The LHC complex consists of chlorophyll a-b binding proteins.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC       pass membrane protein.
CC   -!- DOMAIN: The N-terminus of the protein extends into the stroma where it
CC       is involved with adhesion of granal membranes and post-translational
CC       modifications; both are believed to mediate the distribution of
CC       excitation energy between photosystems I and II.
CC   -!- PTM: Photoregulated by reversible phosphorylation of its threonine
CC       residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding
CC       (LHC) protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X13909; CAA32109.1; -; Genomic_DNA.
DR   EMBL; AP003278; BAD52990.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05407.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS73022.1; -; Genomic_DNA.
DR   EMBL; CM000146; EAZ44370.1; -; Genomic_DNA.
DR   EMBL; AK119173; BAG99560.1; -; mRNA.
DR   EMBL; AK121563; BAH00551.1; -; mRNA.
DR   PIR; S03706; S03706.
DR   RefSeq; XP_015621226.1; XM_015765740.1.
DR   AlphaFoldDB; P12331; -.
DR   SMR; P12331; -.
DR   BioGRID; 793636; 1.
DR   STRING; 4530.OS01T0600900-02; -.
DR   PaxDb; P12331; -.
DR   PRIDE; P12331; -.
DR   EnsemblPlants; Os01t0600900-02; Os01t0600900-02; Os01g0600900.
DR   GeneID; 4324599; -.
DR   Gramene; Os01t0600900-02; Os01t0600900-02; Os01g0600900.
DR   KEGG; osa:4324599; -.
DR   eggNOG; ENOG502QPU1; Eukaryota.
DR   HOGENOM; CLU_057943_2_0_1; -.
DR   InParanoid; P12331; -.
DR   OMA; INNAWAY; -.
DR   OrthoDB; 961261at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; P12331; baseline and differential.
DR   Genevisible; P12331; OS.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; ISS:Gramene.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; ISS:Gramene.
DR   GO; GO:0009768; P:photosynthesis, light harvesting in photosystem I; IBA:GO_Central.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR   InterPro; IPR001344; Chloro_AB-bd_pln.
DR   InterPro; IPR022796; Chloroa_b-bind.
DR   PANTHER; PTHR21649; PTHR21649; 1.
DR   Pfam; PF00504; Chloroa_b-bind; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chlorophyll; Chloroplast; Chromophore; Magnesium; Membrane;
KW   Metal-binding; Phosphoprotein; Photosynthesis; Photosystem I;
KW   Photosystem II; Plastid; Reference proteome; Thylakoid; Transit peptide;
KW   Transmembrane; Transmembrane helix.
FT   TRANSIT         1..29
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           30..261
FT                   /note="Chlorophyll a-b binding protein 2, chloroplastic"
FT                   /id="PRO_0000003678"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         53
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="1"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         75
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         97
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="2"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         99
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P07371"
FT   BINDING         168
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="3"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         171
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         212
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="4"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         214
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="5"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         241
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="6"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P12333"
FT   BINDING         250
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         30
FT                   /note="N2-acetylarginine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        40
FT                   /note="A -> AS (in Ref. 1; CAA32109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="G -> GR (in Ref. 1; CAA32109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        105
FT                   /note="A -> G (in Ref. 1; CAA32109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="S -> A (in Ref. 1; CAA32109)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  27553 MW;  446CDB08FB766297 CRC64;
     MAAATMALSS PALAGKAAAK VFGEGRITMR KSAAKPKPAA SGSPWYGADR VLYLGPLSGE
     PPSYLTGEFP GDYGWDTAGL SADPETFAKN RELEVIHSRW AMLGALGCVF PELLARNGVK
     FGEAVWFKAG SQIFSEGGLD YLGNPSLIHA QSILAIWAVQ VVLMGAVEGY RIAGGPLGEV
     VDPLYPGGSF DPLGLADDPE AFAELKVKEI KNGRLAMFSM FGFFVQAIVT GKGPLENLAD
     HLADPVNNNA WAYATNFVPG K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024