ID   PHEG_AGLNE              Reviewed;         317 AA.
AC   P34784;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=R-phycoerythrin gamma chain, chloroplastic;
DE   Flags: Precursor;
OS   Aglaothamnion neglectum (Red alga).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Callithamniaceae; Aglaothamnion.
OX   NCBI_TaxID=2765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8344905; DOI=10.1016/s0021-9258(19)85407-8;
RA   Apt K.E., Hoffman N.E., Grossman A.R.;
RT   "The gamma subunit of R-phycoerythrin and its possible mode of transport
RT   into the plastid of red algae.";
RL   J. Biol. Chem. 268:16208-16215(1993).
CC   -!- FUNCTION: Critical for the incorporation of phycoerythrin in the
CC       phycobilisome complex.
CC   -!- SUBUNIT: Heteromer of 1 alpha, 1 beta and 2 gamma chains.
CC       {ECO:0000269|PubMed:8344905}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Stromal side. Note=Forms the periphery of
CC       the phycobilisome rod. {ECO:0000250}.
CC   -!- PTM: Contains four covalently linked bilin chromophores.
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DR   EMBL; L13695; AAA32635.1; -; mRNA.
DR   PIR; A47336; A47336.
DR   AlphaFoldDB; P34784; -.
DR   SMR; P34784; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antenna complex; Bile pigment; Chloroplast; Chromophore;
KW   Direct protein sequencing; Electron transport; Membrane; Photosynthesis;
KW   Phycobilisome; Plastid; Thylakoid; Transit peptide; Transport.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT   CHAIN           41..317
FT                   /note="R-phycoerythrin gamma chain, chloroplastic"
FT                   /id="PRO_0000002829"
FT   BINDING         94
FT                   /ligand="phycourobilin"
FT                   /ligand_id="ChEBI:CHEBI:189062"
FT                   /ligand_label="1"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="phycourobilin"
FT                   /ligand_id="ChEBI:CHEBI:189062"
FT                   /ligand_label="2"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="(2R,3E)-phycoerythrobilin"
FT                   /ligand_id="ChEBI:CHEBI:85276"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="phycourobilin"
FT                   /ligand_id="ChEBI:CHEBI:189062"
FT                   /ligand_label="3"
FT                   /note="covalent, via 1 link"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   317 AA;  34641 MW;  1873254B9094F5E2 CRC64;
     MASPAFAVNG MFTPVKLSGS FTASMPVDSK PAASATGVRM VVDPLQRKYQ SIGKIGVDYS
     RPKKLATYVR SGYSVGMEFP NTPSMAGHYS LTDCDKAGGA AKILMKYDEY CAKGMLQVGK
     RAACRTGVYT TKCTEGTQPQ MAFDVRVFNR TQAFRQAQKP VAARLREQYE ARKACFVLAH
     NCSREEAQFK EMPMSCATFL ASKMEATGAC YRTVRPTSVA EDYMAGSVRA QLYTKLNPKG
     VYGVGACEDG HAKGDADQRR VIALASEYRA AAQSPSTVTG QQYKSAQLAT QLFAHDCHHE
     QEQIYEYPAV AAAMCRY