ID   PCP1_AMPCA              Reviewed;         370 AA.
AC   P80484; P51872;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Peridinin-chlorophyll a-binding protein 1, chloroplastic;
DE            Short=PCP;
DE   Flags: Precursor;
OS   Amphidinium carterae (Dinoflagellate).
OC   Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC   Amphidinium.
OX   NCBI_TaxID=2961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=CS21;
RX   PubMed=8816945; DOI=10.1016/0005-2728(96)00066-7;
RA   Sharples F.P., Wrench P.M., Ou K., Hiller R.G.;
RT   "Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium
RT   carterae.";
RL   Biochim. Biophys. Acta 1276:117-123(1996).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8650577; DOI=10.1126/science.272.5269.1788;
RA   Hofmann E., Wrench P.M., Sharples F.P., Hiller R.G., Welte W.,
RA   Diederichs K.;
RT   "Structural basis of light harvesting by carotenoids: peridinin-
RT   chlorophyll-protein from Amphidinium carterae.";
RL   Science 272:1788-1791(1996).
CC   -!- FUNCTION: Water-soluble antenna for capture of solar energy in the
CC       blue-green range. Peridinin is an asymmetric carotenoid.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=~480 nm;
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The mature protein is composed of 2 almost identical repeat
CC       units.
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DR   EMBL; Z50792; CAA90653.1; -; mRNA.
DR   EMBL; X94549; CAA64242.1; -; Genomic_DNA.
DR   PIR; S60187; S60187.
DR   PDB; 1PPR; X-ray; 2.00 A; M/N/O=58-369.
DR   PDB; 2X1Z; X-ray; 1.80 A; M=57-207.
DR   PDB; 2X20; X-ray; 1.95 A; M=57-207.
DR   PDB; 2X21; X-ray; 1.75 A; M=57-207.
DR   PDB; 3IIS; X-ray; 1.40 A; M=57-207.
DR   PDB; 3IIU; X-ray; 1.45 A; M=57-207.
DR   PDBsum; 1PPR; -.
DR   PDBsum; 2X1Z; -.
DR   PDBsum; 2X20; -.
DR   PDBsum; 2X21; -.
DR   PDBsum; 3IIS; -.
DR   PDBsum; 3IIU; -.
DR   AlphaFoldDB; P80484; -.
DR   SMR; P80484; -.
DR   MINT; P80484; -.
DR   EvolutionaryTrace; P80484; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030076; C:light-harvesting complex; IEA:UniProtKB-KW.
DR   GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.40.10.10; -; 2.
DR   InterPro; IPR003376; Peridinin-chlorophyll-bd_prot.
DR   InterPro; IPR036550; Peridinin-chlorophyll-bd_sf.
DR   Pfam; PF02429; PCP; 2.
DR   SUPFAM; SSF48608; SSF48608; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Chlorophyll; Chloroplast; Chromophore;
KW   Direct protein sequencing; Light-harvesting polypeptide; Plastid; Repeat;
KW   Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT   CHAIN           58..370
FT                   /note="Peridinin-chlorophyll a-binding protein 1,
FT                   chloroplastic"
FT                   /id="PRO_0000022026"
FT   REPEAT          58..220
FT                   /note="1"
FT   REPEAT          221..370
FT                   /note="2"
FT   SITE            123
FT                   /note="Chlorophyll a binding"
FT   SITE            286
FT                   /note="Chlorophyll a binding"
FT   CONFLICT        73
FT                   /note="A -> H (in Ref. 1; CAA64242)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="L -> T (in Ref. 1; CAA64242)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="V -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="W -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           83..86
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           94..110
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           113..128
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   TURN            132..135
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           139..154
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           158..171
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           176..182
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           186..205
FT                   /evidence="ECO:0007829|PDB:3IIS"
FT   HELIX           222..240
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           257..273
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           276..291
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           301..315
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           320..333
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           337..344
FT                   /evidence="ECO:0007829|PDB:1PPR"
FT   HELIX           348..368
FT                   /evidence="ECO:0007829|PDB:1PPR"
SQ   SEQUENCE   370 AA;  38160 MW;  7F113EB0DD8F372E CRC64;
     MVRSGKKAVV LAAVAFCATS VVQKSHGFVP SPLRQRAAAA GAAAASAATM FAPAAFADEI
     GDAAKKLGDA SYAFAKEVDW NNGIFLQAPG KLQPLEALKA IDKMIVMGAA ADPKLLKAAA
     EAHHKAIGSV SGPNGVTSRA DWDNVNAALG RVIASVPENM VMDVYDSVSK ITDPKVPAYM
     KSLVSGADAE KAYEGFLAFK DVVKKSQVTS AAGPATVPSG DKIGVAAQQL SEASYPFLKE
     IDWLSDVYMK PLPGVSAQQS LKAIDKMIVM GAQADGNALK AAAEAHHKAI GSIDATGVTS
     AADYAAVNAA LGRVIASVPK STVMDVYNAM AGATDTSIPL NMFSKVNPLD ANAAAKAFYT
     FKDVVQAAQR