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P83689

- OCP_ARTMA

UniProt

P83689 - OCP_ARTMA

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Protein

Orange carotenoid-binding protein

Gene
N/A
Organism
Arthrospira maxima (Spirulina maxima)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a photo-protectant. Essential for inhibiting white and blue-green light non-photochemical quenching (NPQ). Binding carotenoids improves OCP's intrinsic photoprotectant activity by broadening its absorption spectrum and facilitating the dissipation of absorbed energy.1 Publication

Absorptioni

Abs(max)=494 nm2 Publications

Also shows other maxima at 465 nm and 275 nm. The red form (RCP) shows a broad peak at 500 nm.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Carotenoid1 Publication
Binding sitei227 – 2271Carotenoid1 Publication
Binding sitei277 – 2771Chloride1 Publication
Binding sitei286 – 2861Carotenoid1 Publication
Binding sitei290 – 2901Carotenoid1 Publication
Binding sitei305 – 3051Carotenoid1 Publication

GO - Molecular functioni

  1. chloride ion binding Source: InterPro

GO - Biological processi

  1. light absorption Source: InterPro
  2. transport Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Orange carotenoid-binding protein
Short name:
OCP
Cleaved into the following chain:
OrganismiArthrospira maxima (Spirulina maxima)
Taxonomic identifieri129910 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesArthrospira

Subcellular locationi

Cellular thylakoid membrane By similarity1 Publication
Note: Associated with the phycobilisome.By similarity

GO - Cellular componenti

  1. phycobilisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 317316Orange carotenoid-binding protein1 PublicationPRO_0000282350Add
BLAST
Chaini16 – ?Red carotenoid-binding proteinBy similarityPRO_0000282351

Post-translational modificationi

Proteolytically cleaved into a red 16.7 kDa form named red carotenoid-binding protein (RCP) which lacks 15 residues from the N-terminus and approximately 150 residues from the C-terminus.By similarity

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi20 – 289Combined sources
Helixi33 – 5018Combined sources
Helixi58 – 7316Combined sources
Helixi76 – 8813Combined sources
Helixi93 – 997Combined sources
Helixi103 – 11816Combined sources
Helixi133 – 14412Combined sources
Helixi147 – 15913Combined sources
Helixi184 – 1863Combined sources
Helixi198 – 20811Combined sources
Helixi212 – 2165Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi233 – 2353Combined sources
Helixi236 – 24611Combined sources
Beta strandi251 – 26111Combined sources
Helixi263 – 2653Combined sources
Beta strandi267 – 27610Combined sources
Turni278 – 2803Combined sources
Helixi281 – 2833Combined sources
Beta strandi286 – 2949Combined sources
Beta strandi300 – 31011Combined sources
Helixi311 – 3155Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M98X-ray2.10A/B1-317[»]
ProteinModelPortaliP83689.
SMRiP83689. Positions 2-317.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83689.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 448Carotenoid-binding1 Publication
Regioni107 – 1148Carotenoid-binding1 Publication
Regioni151 – 1588Carotenoid-binding1 Publication
Regioni203 – 2075Carotenoid-binding1 Publication
Regioni247 – 2526Carotenoid-binding1 Publication
Regioni275 – 2806Carotenoid-binding1 Publication

Family and domain databases

Gene3Di1.10.2090.10. 1 hit.
InterProiIPR002075. NTF2.
IPR015233. Orange_carotenoid-bd_N.
[Graphical view]
PfamiPF09150. Carot_N. 1 hit.
PF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF81930. SSF81930. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83689-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFTIDTARS IFPETLAADV VPATIARFKQ LSAEDQLALI WFAYLEMGKT
60 70 80 90 100
ITIAAPGAAN MQFAENTLQE IRQMTPLQQT QAMCDLANRT DTPICRTYAS
110 120 130 140 150
WSPNIKLGFW YELGRFMDQG LVAPIPEGYK LSANANAILV TIQGIDPGQQ
160 170 180 190 200
ITVLRNCVVD MGFDTSKLGS YQRVAEPVVP PQEMSQRTKV QIEGVTNSTV
210 220 230 240 250
LQYMDNLNAN DFDNLISLFA EDGALQPPFQ KPIVGKENTL RFFREECQNL
260 270 280 290 300
KLIPERGVSE PTEDGYTQIK VTGKVQTPWF GGNVGMNIAW RFLLNPENKV
310
FFVAIDLLAS PKELLNL
Length:317
Mass (Da):35,348
Last modified:December 15, 2003 - v1
Checksum:iD72A95D89DEF52EA
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M98 X-ray 2.10 A/B 1-317 [» ]
ProteinModelPortali P83689.
SMRi P83689. Positions 2-317.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P83689.

Family and domain databases

Gene3Di 1.10.2090.10. 1 hit.
InterProi IPR002075. NTF2.
IPR015233. Orange_carotenoid-bd_N.
[Graphical view ]
Pfami PF09150. Carot_N. 1 hit.
PF02136. NTF2. 1 hit.
[Graphical view ]
SUPFAMi SSF81930. SSF81930. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The orange carotenoid protein of Synechocystis PCC 6803."
    Wu Y.P., Krogmann D.W.
    Biochim. Biophys. Acta 1322:1-7(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-29.
  2. "A carotenoid-protein from cyanobacteria."
    Holt T.K., Krogmann D.W.
    Biochim. Biophys. Acta 637:408-414(1981)
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION OF CAROTENOID, PROTEOLYTIC CLEAVAGE.
  3. "Water-soluble carotenoid proteins of cyanobacteria."
    Kerfeld C.A.
    Arch. Biochem. Biophys. 430:2-9(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  4. "Spectroscopic properties of the carotenoid 3'-hydroxyechinenone in the orange carotenoid protein from the cyanobacterium Arthrospira maxima."
    Polivka T., Kerfeld C.A., Pascher T., Sundstroem V.
    Biochemistry 44:3994-4003(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Crystals of the carotenoid protein from Arthrospira maxima containing uniformly oriented pigment molecules."
    Kerfeld C.A., Wu Y.P., Chan C., Krogmann D.W., Yeates T.O.
    Acta Crystallogr. D 53:720-723(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  6. "The crystal structure of a cyanobacterial water-soluble carotenoid binding protein."
    Kerfeld C.A., Sawaya M.R., Brahmandam V., Cascio D., Ho K.K., Trevithick-Sutton C.C., Krogmann D.W., Yeates T.O.
    Structure 11:55-65(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CAROTENOID, SUBUNIT.

Entry informationi

Entry nameiOCP_ARTMA
AccessioniPrimary (citable) accession number: P83689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 15, 2003
Last modified: November 26, 2014
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds 1 carotenoid (3'-hydroxyechinenone) molecule and 1 chloride ion per subunit.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3