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FCPA_PHATR
ID   FCPA_PHATR              Reviewed;         196 AA.
AC   Q08584; Q01272;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Fucoxanthin-chlorophyll a-c binding protein A, chloroplastic;
DE   Flags: Precursor;
GN   Name=FCPA; Synonyms=FCP1;
OS   Phaeodactylum tricornutum (Diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=2850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UTEX 646 / Bohlin;
RX   PubMed=8233779; DOI=10.1093/nar/21.19.4458;
RA   Bhaya D., Grossman A.R.;
RT   "Characterization of gene clusters encoding the fucoxanthin chlorophyll
RT   proteins of the diatom Phaeodactylum tricornutum.";
RL   Nucleic Acids Res. 21:4458-4466(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=UTEX 646 / Bohlin;
RX   PubMed=2277634; DOI=10.1007/bf00259455;
RA   Grossman A., Manodori A., Snyder D.;
RT   "Light-harvesting proteins of diatoms: their relationship to the
RT   chlorophyll a/b binding proteins of higher plants and their mode of
RT   transport into plastids.";
RL   Mol. Gen. Genet. 224:91-100(1990).
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. Energy is transferred from the
CC       carotenoid and chlorophyll C (or B) to chlorophyll A and the
CC       photosynthetic reaction centers where it is used to synthesize ATP and
CC       reducing power.
CC   -!- SUBUNIT: The LHC complex of chromophytic algae is composed of
CC       fucoxanthin, chlorophyll A and C bound non-covalently by fucoxanthin
CC       chlorophyll proteins (FCPs). The ratio of the pigments in LHC;
CC       fucoxanthin: chlorophyll C: chlorophyll A; (0.6-1): (0.1-0.3): (1).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC       pass membrane protein. Note=FCPs are probably transported across the
CC       endoplasmic reticulum membranes that surround the plastid via a signal
CC       peptide, followed by translocation across the thylakoid membrane via a
CC       transit peptide.
CC   -!- SIMILARITY: Belongs to the fucoxanthin chlorophyll protein family.
CC       {ECO:0000305}.
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DR   EMBL; Z24768; CAA80894.1; -; Genomic_DNA.
DR   EMBL; X55250; CAA38990.1; -; mRNA.
DR   PIR; S42131; S42131.
DR   AlphaFoldDB; Q08584; -.
DR   SMR; Q08584; -.
DR   HOGENOM; CLU_057943_4_1_1; -.
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:0030076; C:light-harvesting complex; 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: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   Chlorophyll; Chloroplast; Chromophore; Light-harvesting polypeptide;
KW   Membrane; Photosynthesis; Photosystem II; Plastid; Thylakoid;
KW   Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..31
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305"
FT   CHAIN           32..196
FT                   /note="Fucoxanthin-chlorophyll a-c binding protein A,
FT                   chloroplastic"
FT                   /id="PRO_0000021234"
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        8
FT                   /note="S -> F (in Ref. 2; CAA38990)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="R -> A (in Ref. 2; CAA38990)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="N -> D (in Ref. 2; CAA38990)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="F -> L (in Ref. 2; CAA38990)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   196 AA;  21272 MW;  C310C35FAFC32A7C CRC64;
     MKFAVFASLL ASRAAFAPAQ QSARTSVATN MAFENEIGAQ QPLGYWDPLG LVADGNQEKF
     DRLRYVEIKH GRICMLAVAG YLTQEAGIRL PGDIDYSGTS FESIPNGFAA LSAVPGAGIA
     QIIAFIGFFE IAVMKDITGG EFVGDFRNNY LDFGWDTFSE DKKLQKRAIE LNQGRAAQMG
     ILALMVHEQL GVSILP
 
 
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