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CB21_ORYSJ
ID   CB21_ORYSJ              Reviewed;         265 AA.
AC   P12330; Q0J2G2; Q6EQF5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Chlorophyll a-b binding protein 1, chloroplastic;
DE   AltName: Full=LHCII type I CAB-1;
DE            Short=LHCP;
DE   Flags: Precursor;
GN   Name=CAB1R; OrderedLocusNames=Os09g0346500, LOC_Os09g17740;
GN   ORFNames=OSJNBb0085I16.35, P0512H04.4;
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 [MRNA].
RC   STRAIN=cv. Nipponbare; TISSUE=Leaf;
RA   Matsuoka M.;
RT   "Classification and characterization of cDNA that encodes the light-
RT   harvesting chlorophyll a/b binding protein of photosystem II from rice.";
RL   Plant Cell Physiol. 31:519-526(1990).
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 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}.
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DR   EMBL; X13908; CAA32108.1; -; Genomic_DNA.
DR   EMBL; D00641; BAA00536.1; -; mRNA.
DR   EMBL; AP005313; BAD28469.1; -; Genomic_DNA.
DR   EMBL; AP005700; BAD29115.1; -; Genomic_DNA.
DR   EMBL; AP008215; BAF24853.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT07611.1; -; Genomic_DNA.
DR   EMBL; AK060851; BAG87574.1; -; mRNA.
DR   EMBL; AK104281; BAG96567.1; -; mRNA.
DR   EMBL; AK104288; BAG96573.1; -; mRNA.
DR   EMBL; AK104350; BAG96613.1; -; mRNA.
DR   PIR; A44956; A44956.
DR   PIR; S03705; S03705.
DR   RefSeq; XP_015611833.1; XM_015756347.1.
DR   AlphaFoldDB; P12330; -.
DR   SMR; P12330; -.
DR   BioGRID; 815840; 1.
DR   STRING; 4530.OS09T0346500-04; -.
DR   PaxDb; P12330; -.
DR   PRIDE; P12330; -.
DR   EnsemblPlants; Os09t0346500-04; Os09t0346500-04; Os09g0346500.
DR   GeneID; 4346803; -.
DR   Gramene; Os09t0346500-04; Os09t0346500-04; Os09g0346500.
DR   KEGG; osa:4346803; -.
DR   eggNOG; ENOG502QPU1; Eukaryota.
DR   HOGENOM; CLU_057943_2_0_1; -.
DR   InParanoid; P12330; -.
DR   OMA; MATTTMY; -.
DR   OrthoDB; 961261at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
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..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           33..265
FT                   /note="Chlorophyll a-b binding protein 1, chloroplastic"
FT                   /id="PRO_0000003677"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         57
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         79
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
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         101
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         103
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
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         156
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250|UniProtKB:P07371"
FT   BINDING         172
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         175
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
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         216
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         218
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         230
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         245
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         254
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="N2-acetylarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        63
FT                   /note="G -> GR (in Ref. 1; CAA32108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="V -> L (in Ref. 2; BAA00536)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="F -> C (in Ref. 1; CAA32108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="E -> K (in Ref. 1; CAA32108)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="N -> K (in Ref. 2; BAA00536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   265 AA;  28014 MW;  A585AAEAF64E76AB CRC64;
     MAAATMALSS PVMARAAPST SSALFGEARI TMRKTAAKPK PAASSGSPWY GADRVLYLGP
     LSGEPPSYLT GEFPGDYGWD TAGLSADPET FAKNRELEVI HSRWAMLGAL GCVFPELLAR
     NGVKFGEAVW FKAGSQIFSE GGLDYLGNPS LIHAQSILAI WAVQVVLMGA VEGYRIAGGP
     LGEVVDPLYP GGAFDPLGLA DDPEAFAELK VKEIKNGRLA MFSMFGFFVQ AIVTGKGPLE
     NLADHLADPV NNNAWAYATN FVPGK
 
 
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