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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.2 Publications

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
Complete GO annotation...

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
Note: Associated with the phycobilisome By similarity.By similarity1 Publication

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 Publication
PRO_0000282350Add
BLAST
Chaini16 – ?Red carotenoid-binding protein By 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.2 Publications

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M98X-ray2.10A/B1-317[»]
ProteinModelPortaliP83689.
SMRiP83689. Positions 2-317.

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

MPFTIDTARS IFPETLAADV VPATIARFKQ LSAEDQLALI WFAYLEMGKT    50
ITIAAPGAAN MQFAENTLQE IRQMTPLQQT QAMCDLANRT DTPICRTYAS 100
WSPNIKLGFW YELGRFMDQG LVAPIPEGYK LSANANAILV TIQGIDPGQQ 150
ITVLRNCVVD MGFDTSKLGS YQRVAEPVVP PQEMSQRTKV QIEGVTNSTV 200
LQYMDNLNAN DFDNLISLFA EDGALQPPFQ KPIVGKENTL RFFREECQNL 250
KLIPERGVSE PTEDGYTQIK VTGKVQTPWF GGNVGMNIAW RFLLNPENKV 300
FFVAIDLLAS PKELLNL 317
Length:317
Mass (Da):35,348
Last modified:December 15, 2003 - v1
Checksum:iD72A95D89DEF52EA
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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...

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: April 16, 2014
This is version 36 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

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