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Protein

Orange carotenoid-binding protein

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

Functioni

Acts as a blue-light photoreceptor and photo-protectant. Essential for inhibiting damaged induced by excess blue-green light via a process known as non-photochemical quenching (NPQ). Binding carotenoids improves OCP's intrinsic photoprotectant activity by broadening its absorption spectrum and facilitating the dissipation of absorbed energy (PubMed:15751975). In the dark or dim light the stable inactive form (OCP-O) is orange, upon illumination with blue-green light it converts to a metastable active red form (OCP-R), inducing energy dissipation, quenching cellular fluorescence via NPQ (By similarity).By similarity1 Publication

Cofactori

Protein has several cofactor binding sites:

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

Manual assertion based on experiment ini

  • Ref.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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei53Carotenoid1 Publication1
Binding sitei227Carotenoid1 Publication1
Binding sitei277Chloride1 Publication1
Binding sitei286Carotenoid1 Publication1
Binding sitei290Carotenoid1 Publication1
Binding sitei305Carotenoid1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Photoreceptor protein, Receptor

Keywords - Biological processi

Sensory transduction

Keywords - Ligandi

Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Orange carotenoid-binding protein1 Publication
Short name:
OCP1 Publication
Cleaved into the following chain:
OrganismiArthrospira maxima (Spirulina maxima)
Taxonomic identifieri129910 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesMicrocoleaceaeArthrospira

Subcellular locationi

  • Cellular thylakoid membrane By similarity1 Publication; Peripheral membrane protein Curated; Cytoplasmic side Curated

  • Note: Associated with the phycobilisome.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002823502 – 317Orange carotenoid-binding protein1 PublicationAdd BLAST316
ChainiPRO_000028235116 – ?Red carotenoid-binding proteinBy similarity

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 similarity1 Publication

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi513049.AmaxDRAFT_3431.

Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Helixi20 – 28Combined sources9
Helixi33 – 50Combined sources18
Helixi58 – 73Combined sources16
Helixi76 – 88Combined sources13
Helixi93 – 99Combined sources7
Helixi103 – 118Combined sources16
Helixi133 – 144Combined sources12
Helixi147 – 159Combined sources13
Helixi184 – 186Combined sources3
Helixi198 – 208Combined sources11
Helixi212 – 216Combined sources5
Beta strandi219 – 226Combined sources8
Beta strandi233 – 235Combined sources3
Helixi236 – 246Combined sources11
Beta strandi251 – 261Combined sources11
Helixi263 – 265Combined sources3
Beta strandi267 – 276Combined sources10
Turni278 – 280Combined sources3
Helixi281 – 283Combined sources3
Beta strandi286 – 294Combined sources9
Beta strandi300 – 310Combined sources11
Helixi311 – 315Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP83689.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 169OCPPROSITE-ProRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 44Carotenoid-binding1 Publication8
Regioni107 – 114Carotenoid-binding1 Publication8
Regioni151 – 158Carotenoid-binding1 Publication8
Regioni203 – 207Carotenoid-binding1 Publication5
Regioni247 – 252Carotenoid-binding1 Publication6
Regioni275 – 280Carotenoid-binding1 Publication6

Sequence similaritiesi

Belongs to the orange carotenoid-binding protein family.PROSITE-ProRule annotationCurated
Contains 1 OCP (orange carotenoid protein) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107CUI. Bacteria.
ENOG410XP5R. LUCA.

Family and domain databases

Gene3Di1.10.2090.10. 1 hit.
3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR015233. Orange_carotenoid-bd_N.
[Graphical view]
PfamiPF09150. Carot_N. 1 hit.
PF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF81930. SSF81930. 1 hit.
PROSITEiPS51773. OCP_N. 1 hit.
[Graphical view]

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M98X-ray2.10A/B1-317[»]
ProteinModelPortaliP83689.
SMRiP83689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi513049.AmaxDRAFT_3431.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107CUI. Bacteria.
ENOG410XP5R. LUCA.

Miscellaneous databases

EvolutionaryTraceiP83689.

Family and domain databases

Gene3Di1.10.2090.10. 1 hit.
3.10.450.50. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR015233. Orange_carotenoid-bd_N.
[Graphical view]
PfamiPF09150. Carot_N. 1 hit.
PF02136. NTF2. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF81930. SSF81930. 1 hit.
PROSITEiPS51773. OCP_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.