位置:首页 > 蛋白库 > LI181_CHLMO
LI181_CHLMO
ID   LI181_CHLMO             Reviewed;         270 AA.
AC   Q03965;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chlorophyll a-b binding protein LI818, chloroplastic;
DE   Flags: Precursor;
GN   Name=LI818;
OS   Chlamydomonas moewusii (Chlamydomonas eugametos).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=UTEX 9;
RX   PubMed=1371402; DOI=10.1007/bf00040659;
RA   Gagne G., Guertin M.;
RT   "The early genetic response to light in the green unicellular alga
RT   Chlamydomonas eugametos grown under light/dark cycles involves genes that
RT   represent direct responses to light and photosynthesis.";
RL   Plant Mol. Biol. 18:429-445(1992).
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; Single-
CC       pass membrane protein.
CC   -!- INDUCTION: By light.
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; X60721; CAA43128.1; -; mRNA.
DR   PIR; S20520; S20520.
DR   AlphaFoldDB; Q03965; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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:0009765; P:photosynthesis, light harvesting; IEA:InterPro.
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; Thylakoid; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           48..270
FT                   /note="Chlorophyll a-b binding protein LI818,
FT                   chloroplastic"
FT                   /id="PRO_0000003714"
FT   TRANSMEM        96..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         56
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"
FT   BINDING         74
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
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"
FT   BINDING         98
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"
FT   BINDING         138
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
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"
FT   BINDING         158
FT                   /ligand="chlorophyll b"
FT                   /ligand_id="ChEBI:CHEBI:61721"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
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"
FT   BINDING         208
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"
FT   BINDING         210
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
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"
FT   MOD_RES         48
FT                   /note="N2-acetylarginine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29249 MW;  5367B6691E4BFE1A CRC64;
     MAFTTKMQRS AVASRSSTVR VQAAGKTVSG SKTVSGGKTV GSASAESRRV AEVQAYLATL
     PGCGVESGPF KGVWDPLSLA ATATVGDVRR WRESEITHGR VAMLAALGFV VGEQLEDFPA
     FFNFDGHITG QAIKQFDQVQ QGFWEPLLIA IGLAESYRVS LGWATPTGTG FNNLKDEYDL
     GNLYFDPLGL KPEDPEELRE LQTKELNNGR LAMIAIAGFV LQEVAEPGVE IFQHLFFTIE
     KDIVEEIDII EKDLGLPPSF PVPTLPNLSS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024