P74102 (OCP_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Orange carotenoid-binding protein
Short name=OCP

Cleaved into the following chain:

1. Red carotenoid-binding protein
   Short name=RCP

Gene names

Ordered Locus Names:

slr1963

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › Synechocystis sp. PCC 6803

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.4
Subunit structure	Homodimer By similarity. UniProtKB P83689
Subcellular location	Cellular thylakoid membrane. Note: Associated with the phycobilisome. Ref.4
Post-translational modification	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. Ref.1
Miscellaneous	Binds 1 carotenoid (3'-hydroxyechinenone) molecule and 1 chloride ion per subunit By similarity.
Mass spectrometry	Molecular mass is 34622 Da from positions 2 - 317. Determined by MALDI. OCP. Ref.1 Molecular mass is 16739 Da from positions 16 - ?. Determined by MALDI. RCP. Ref.1

Ontologies

Keywords
Cellular component	Membrane Phycobilisome Thylakoid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	light absorption Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: InterPro
Cellular_component	phycobilisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	chloride ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 317

316

Orange carotenoid-binding protein Ref.1

PRO_0000282352

Chain

16 – ?

Red carotenoid-binding protein

PRO_0000282353

Regions

Region

37 – 44

8

Carotenoid-binding By similarity UniProtKB P83689

Region

107 – 114

8

Carotenoid-binding By similarity UniProtKB P83689

Region

151 – 158

8

Carotenoid-binding By similarity UniProtKB P83689

Region

201 – 205

5

Carotenoid-binding By similarity UniProtKB P83689

Region

245 – 250

6

Carotenoid-binding By similarity UniProtKB P83689

Region

273 – 278

6

Carotenoid-binding By similarity UniProtKB P83689

Sites

Binding site

53

1

Carotenoid By similarity UniProtKB P83689

Binding site

225

1

Carotenoid By similarity UniProtKB P83689

Binding site

277

1

Chloride By similarity UniProtKB P83689

Binding site

284

1

Carotenoid By similarity UniProtKB P83689

Binding site

288

1

Carotenoid By similarity UniProtKB P83689

Binding site

303

1

Carotenoid By similarity UniProtKB P83689

Experimental info

Sequence conflict

73

1

A → G AA sequence Ref.1

Sequence conflict

75

1

G → T AA sequence Ref.1

Sequence conflict

121

1

F → L AA sequence Ref.1

Sequence conflict

165

1

A → V AA sequence Ref.1

Sequence conflict

169

1

G → I AA sequence Ref.1

Secondary structure

1

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317

Helix Strand Turn

Details...

Helix

5 – 8

4

Helix

20 – 29

10

Helix

33 – 47

15

Turn

48 – 50

3

Helix

58 – 73

16

Helix

76 – 88

13

Helix

93 – 99

7

Helix

103 – 118

16

Helix

133 – 143

11

Helix

147 – 159

13

Helix

182 – 184

3

Helix

196 – 206

11

Helix

210 – 214

5

Beta strand

217 – 224

8

Beta strand

231 – 233

3

Helix

234 – 244

11

Beta strand

249 – 259

11

Helix

261 – 263

3

Beta strand

265 – 274

10

Turn

276 – 278

3

Helix

279 – 281

3

Beta strand

284 – 292

9

Beta strand

298 – 308

11

Helix

309 – 311

3

Sequences

	Sequence		Length	Mass (Da)
	P74102 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 8FF633BDE6D530F2	FASTA	317	34,659
	10 20 30 40 50 60 MPFTIDSARG IFPNTLAADV VPATIARFSQ LNAEDQLALI WFAYLEMGKT LTIAAPGAAS 70 80 90 100 110 120 MQLAENALKE IQAMGPLQQT QAMCDLANRA DTPLCRTYAS WSPNIKLGFW YRLGELMEQG 130 140 150 160 170 180 FVAPIPAGYQ LSANANAVLA TIQGLESGQQ ITVLRNAVVD MGFTAGKDGK RIAEPVVPPQ 190 200 210 220 230 240 DTASRTKVSI EGVTNATVLN YMDNLNANDF DTLIELFTSD GALQPPFQRP IVGKENVLRF 250 260 270 280 290 300 FREECQNLKL IPERGVTEPA EDGFTQIKVT GKVQTPWFGG NVGMNIAWRF LLNPEGKIFF 310 VAIDLLASPK ELLNFAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-60, MASS SPECTROMETRY, PROTEOLYTIC CLEAVAGE.
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[3]	"Water-soluble carotenoid proteins of cyanobacteria." Kerfeld C.A. Arch. Biochem. Biophys. 430:2-9(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[4]	"A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria." Wilson A., Ajlani G., Verbavatz J.M., Vass I., Kerfeld C.A., Kirilovsky D. Plant Cell 18:992-1007(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000022 Genomic DNA. Translation: BAA18188.1.

PIR

S75627.

RefSeq

NP_441508.1. NC_000911.1.
YP_005651566.1. NC_017277.1.
YP_007451390.1. NC_020286.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MG1	X-ray	1.65	A/B	1-316	[»]
3MG2	X-ray	2.65	A/B	1-316	[»]
3MG3	X-ray	1.70	A/B	1-316	[»]

ProteinModelPortal

P74102.

SMR

P74102. Positions 2-315.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59343N.

IntAct

P74102. 1 interaction.

STRING

1148.slr1963.

Proteomic databases

PaxDb

P74102.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAA18188; BAA18188; BAA18188.

GeneID

12254218.
14617050.
954888.

KEGG

syn:slr1963.
syy:SYNGTS_1613.

PATRIC

23840439. VBISynSp132158_1777.

Phylogenomic databases

eggNOG

NOG10661.

OMA

FAYLEMG.

ProtClustDB

CLSK893154.

Family and domain databases

Gene3D

1.10.2090.10. 1 hit.

InterPro

IPR002075. NTF2.
IPR015233. Orange_carotenoid-bd_N.
[Graphical view]

Pfam

PF09150. Carot_N. 1 hit.
PF02136. NTF2. 1 hit.
[Graphical view]

SUPFAM

SSF81930. Orange_carotenoid-bd_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P74102.

Entry information

Entry name

OCP_SYNY3

Accession

Primary (citable) accession number: P74102

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program