OCP_LIMMA
ID OCP_LIMMA Reviewed; 317 AA.
AC P83689;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Orange carotenoid-binding protein {ECO:0000303|PubMed:9398074};
DE Short=OCP {ECO:0000303|PubMed:9398074};
DE Contains:
DE RecName: Full=Red carotenoid-binding protein;
DE Short=RCP;
OS Limnospira maxima (Arthrospira maxima).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Sirenicapillariaceae; Limnospira.
OX NCBI_TaxID=129910;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-29, COFACTOR, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=9398074; DOI=10.1016/s0005-2728(97)00067-4;
RA Wu Y.P., Krogmann D.W.;
RT "The orange carotenoid protein of Synechocystis PCC 6803.";
RL Biochim. Biophys. Acta 1322:1-7(1997).
RN [2] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF CAROTENOID, AND
RP PROTEOLYTIC CLEAVAGE.
RA Holt T.K., Krogmann D.W.;
RT "A carotenoid-protein from cyanobacteria.";
RL Biochim. Biophys. Acta 637:408-414(1981).
RN [3] {ECO:0000305}
RP REVIEW ON FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15325905; DOI=10.1016/j.abb.2004.03.018;
RA Kerfeld C.A.;
RT "Water-soluble carotenoid proteins of cyanobacteria.";
RL Arch. Biochem. Biophys. 430:2-9(2004).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15751975; DOI=10.1021/bi047473t;
RA Polivka T., Kerfeld C.A., Pascher T., Sundstroem V.;
RT "Spectroscopic properties of the carotenoid 3'-hydroxyechinenone in the
RT orange carotenoid protein from the cyanobacterium Arthrospira maxima.";
RL Biochemistry 44:3994-4003(2005).
RN [5] {ECO:0000305}
RP CRYSTALLIZATION.
RX PubMed=15299860; DOI=10.1107/s0907444997006999;
RA Kerfeld C.A., Wu Y.P., Chan C., Krogmann D.W., Yeates T.O.;
RT "Crystals of the carotenoid protein from Arthrospira maxima containing
RT uniformly oriented pigment molecules.";
RL Acta Crystallogr. D 53:720-723(1997).
RN [6] {ECO:0000305, ECO:0000312|PDB:5UI2}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH 3'-HYDROXYECHINENONE
RP CAROTENOID, COFACTOR, AND SUBUNIT.
RX PubMed=12517340; DOI=10.1016/s0969-2126(02)00936-x;
RA Kerfeld C.A., Sawaya M.R., Brahmandam V., Cascio D., Ho K.K.,
RA Trevithick-Sutton C.C., Krogmann D.W., Yeates T.O.;
RT "The crystal structure of a cyanobacterial water-soluble carotenoid binding
RT protein.";
RL Structure 11:55-65(2003).
CC -!- FUNCTION: Acts as a blue-light photoreceptor and photo-protectant.
CC Essential for inhibiting damaged induced by excess blue-green light via
CC a process known as non-photochemical quenching (NPQ). Binding
CC carotenoids improves OCP's intrinsic photoprotectant activity by
CC broadening its absorption spectrum and facilitating the dissipation of
CC absorbed energy (PubMed:15751975). In the dark or dim light the stable
CC inactive form (OCP-O) is orange, upon illumination with blue-green
CC light it converts to a metastable active red form (OCP-R), inducing
CC energy dissipation, quenching cellular fluorescence via NPQ (By
CC similarity). {ECO:0000250|UniProtKB:P74102,
CC ECO:0000269|PubMed:15751975}.
CC -!- COFACTOR:
CC Name=3'-hydroxyechinenone; Xref=ChEBI:CHEBI:80214;
CC Evidence={ECO:0000269|PubMed:12517340};
CC Note=Binds 1 3'-hydroxyechinenone molecule per subunit.
CC {ECO:0000269|PubMed:12517340, ECO:0000269|PubMed:9398074};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=494 nm {ECO:0000269|PubMed:15325905, ECO:0000269|Ref.2};
CC Note=Also shows other maxima at 465 nm and 275 nm. The red form (RCP)
CC shows a broad peak at 500 nm. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12517340,
CC ECO:0000269|PubMed:15325905}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000250|UniProtKB:P74102, ECO:0000269|PubMed:15325905}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC Note=Associated with the phycobilisome. {ECO:0000250|UniProtKB:P74102}.
CC -!- PTM: Proteolytically cleaved into a red 16.7 kDa form named red
CC carotenoid-binding protein (RCP) which lacks 15 residues from the N-
CC terminus and approximately 150 residues from the C-terminus.
CC {ECO:0000250|UniProtKB:P74102, ECO:0000305|PubMed:9398074}.
CC -!- SIMILARITY: Belongs to the orange carotenoid-binding protein family.
CC {ECO:0000255|PROSITE-ProRule:PRU01109, ECO:0000305}.
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DR PDB; 5UI2; X-ray; 2.10 A; A/B=1-317.
DR PDBsum; 5UI2; -.
DR AlphaFoldDB; P83689; -.
DR SMR; P83689; -.
DR DrugBank; DB02772; Sucrose.
DR EvolutionaryTrace; P83689; -.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031404; F:chloride ion binding; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0016037; P:light absorption; IEA:InterPro.
DR Gene3D; 1.10.2090.10; -; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR015233; Orange_carotenoid-bd_N.
DR InterPro; IPR036917; Orange_carotenoid-bd_N_sf.
DR Pfam; PF09150; Carot_N; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF81930; SSF81930; 1.
DR PROSITE; PS51773; OCP_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Chromophore; Direct protein sequencing;
KW Membrane; Photoreceptor protein; Phycobilisome; Receptor;
KW Sensory transduction; Thylakoid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9398074"
FT CHAIN 2..317
FT /note="Orange carotenoid-binding protein"
FT /evidence="ECO:0000269|PubMed:9398074"
FT /id="PRO_0000282350"
FT CHAIN 16..?
FT /note="Red carotenoid-binding protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000282351"
FT DOMAIN 18..169
FT /note="OCP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01109"
FT BINDING 37
FT /ligand="3'-hydroxyechinenone"
FT /ligand_id="ChEBI:CHEBI:80214"
FT /evidence="ECO:0000269|PubMed:12517340,
FT ECO:0007744|PDB:5UI2"
FT BINDING 203
FT /ligand="3'-hydroxyechinenone"
FT /ligand_id="ChEBI:CHEBI:80214"
FT /evidence="ECO:0000269|PubMed:12517340,
FT ECO:0007744|PDB:5UI2"
FT BINDING 290
FT /ligand="3'-hydroxyechinenone"
FT /ligand_id="ChEBI:CHEBI:80214"
FT /evidence="ECO:0000269|PubMed:12517340,
FT ECO:0007744|PDB:5UI2"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:5UI2"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:5UI2"
FT STRAND 300..310
FT /evidence="ECO:0007829|PDB:5UI2"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:5UI2"
SQ SEQUENCE 317 AA; 35348 MW; D72A95D89DEF52EA CRC64;
MPFTIDTARS IFPETLAADV VPATIARFKQ LSAEDQLALI WFAYLEMGKT ITIAAPGAAN
MQFAENTLQE IRQMTPLQQT QAMCDLANRT DTPICRTYAS WSPNIKLGFW YELGRFMDQG
LVAPIPEGYK LSANANAILV TIQGIDPGQQ ITVLRNCVVD MGFDTSKLGS YQRVAEPVVP
PQEMSQRTKV QIEGVTNSTV LQYMDNLNAN DFDNLISLFA EDGALQPPFQ KPIVGKENTL
RFFREECQNL KLIPERGVSE PTEDGYTQIK VTGKVQTPWF GGNVGMNIAW RFLLNPENKV
FFVAIDLLAS PKELLNL
