Reviewed, UniProtKB/Swiss-Prot P21457 (RECO_BOVIN)

Names and origin

Protein names

Recommended name:
    Recoverin
Alternative name(s):
    p26

Gene names

Name:	RCVRN
Synonyms:	RCV1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	202 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	Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse. Ref.7 Ref.8
Tissue specificity	Retina and pineal gland.
Post-translational modification	The N-terminal glycine is linked to one of four different types of acyl groups. The most abundant is myristoleate (14:1), but 14:0, 14:2, and 12:0 acyl residues are also present. Myristoylation is necessary for recoverin to bind photoreceptor membranes when the calcium concentration is greater than one micromolar.
Miscellaneous	Binds two calcium ions; one with high affinity, the other with low affinity.
Sequence similarities	Belongs to the recoverin family. Contains 4 EF-hand domains.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Domain	Repeat
Ligand	Calcium
PTM	Lipoprotein Myristate
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 202

201

Recoverin

PRO_0000073758

Regions

Domain

24 – 59

36

EF-hand 1

Domain

61 – 96

36

EF-hand 2

Domain

97 – 132

36

EF-hand 3

Domain

147 – 182

36

EF-hand 4

Calcium binding

74 – 85

12

1; low affinity

Calcium binding

110 – 121

12

2; high affinity

Amino acid modifications

Lipidation

2

1

N-myristoyl glycine Ref.5 Ref.6

Experimental info

Sequence conflict

19

1

L → Q AA sequence Ref.4

Sequence conflict

21

1

T → N AA sequence Ref.4

Secondary structure

1

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202

Helix Strand Turn

Details...

Helix

9 – 17

9

Helix

18 – 20

3

Helix

25 – 38

14

Beta strand

42 – 45

4

Helix

46 – 56

11

Helix

63 – 71

9

Turn

72 – 74

3

Beta strand

77 – 82

6

Helix

83 – 94

12

Helix

98 – 100

3

Helix

102 – 109

8

Beta strand

114 – 117

4

Helix

119 – 130

12

Helix

135 – 138

4

Helix

143 – 145

3

Helix

148 – 158

11

Helix

169 – 178

10

Helix

180 – 186

7

Helix

190 – 196

7

Sequences

	Sequence		Length	Mass (Da)
	P21457-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 75504DEBE8288BA8	FASTA	202	23,333
	10 20 30 40 50 60 MGNSKSGALS KEILEELQLN TKFTEEELSS WYQSFLKECP SGRITRQEFQ TIYSKFFPEA 70 80 90 100 110 120 DPKAYAQHVF RSFDANSDGT LDFKEYVIAL HMTSAGKTNQ KLEWAFSLYD VDGNGTISKN 130 140 150 160 170 180 EVLEIVTAIF KMISPEDTKH LPEDENTPEK RAEKIWGFFG KKDDDKLTEK EFIEGTLANK 190 200 EILRLIQFEP QKVKEKLKEK KL

References

[1]	"Recoverin: a calcium sensitive activator of retinal rod guanylate cyclase." Dizhoor A.M., Ray S., Kumar S., Niemi G., Spencer M., Brolley D., Walsh K.A., Philipov P.P., Hurley J.B., Stryer L. Science 251:915-918(1991) [PubMed: 1672047] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 6-195. Tissue: Retina.
[2]	"P26-calcium binding protein from bovine retinal photoreceptor cells." Kutuzov M.A., Shmukler B.E., Suslov O.N., Dergachev A.E., Zargarov A.A., Abdulaev N.G. FEBS Lett. 293:21-24(1991) [PubMed: 1959664] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	"Cloning, expression, and crystallization of recoverin, a calcium sensor in vision." Ray S., Zozulya S., Niemi G.A., Flaherty K.M., Brolley D., Dizhoor A.M., McKay D.B., Hurley J., Stryer L. Proc. Natl. Acad. Sci. U.S.A. 89:5705-5709(1992) [PubMed: 1385864] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[4]	"A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase." Lambrecht H.G., Koch K.W. EMBO J. 10:793-798(1991) [PubMed: 1672637] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-36. Tissue: Retina.
[5]	"The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids." Dizhoor A.M., Ericsson L.H., Johnson R.S., Kumar S., Olshevskaya E., Zozulya S., Neubert T.A., Stryer L., Hurley J.B., Walsh K.A. J. Biol. Chem. 267:16033-16036(1992) [PubMed: 1386601] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[6]	"Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction." Dizhoor A.M., Chen C.-K., Olshevskaya E., Sinelnikova V.V., Phillipov P., Hurley J.B. Science 259:829-832(1993) [PubMed: 8430337] [Abstract] Cited for: ROLE OF MYRISTOYLATION.
[7]	"Recoverin's role: conclusion withdrawn." Hurley J.B., Dizhoor A.M., Stryer L. Science 260:740-740(1993) [PubMed: 8097896] [Abstract] Cited for: RETRACTION ON ORIGINAL PROPOSED FUNCTION.
[8]	"Recoverin has S-modulin activity in frog rods." Kawamura S., Hisatomi O., Kayada S., Tokunaga F., Kuo C.-H. J. Biol. Chem. 268:14579-14582(1993) [PubMed: 8392055] [Abstract] Cited for: FUNCTION.
[9]	"Three-dimensional structure of recoverin, a calcium sensor in vision." Flaherty K.M., Zozulya S., Stryer L., McKay D.B. Cell 75:709-716(1993) [PubMed: 8242744] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[10]	"Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state." Tanaka T., Ames J.B., Harvey T.S., Stryer L., Ikura M. Nature 376:444-446(1995) [PubMed: 7630423] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M95858 mRNA. Translation: AAB59256.1.
X63322 mRNA. Translation: CAA44928.1.

IPI

IPI00701150.

PIR

A46129.

RefSeq

NP_776590.1.

UniGene

Bt.56904

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IKU	NMR	-	A	2-202	[»]
1JSA	NMR	-	A	2-201	[»]
1LA3	NMR	-	A	2-201	[»]
1OMR	X-ray	1.50	A	2-201	[»]
1OMV	X-ray	1.90	A	2-201	[»]
1REC	X-ray	1.90	A	2-202	[»]
2HET	X-ray	3.00	A/B/C/D	2-189	[»]
2I94	NMR	-	A	1-202	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P21457.

Genome annotation databases

Ensembl

ENSBTAT00000035069; ENSBTAP00000034949; ENSBTAG00000025088; Bos taurus. [Genome view]

GeneID

281447.

KEGG

bta:281447.

Organism-specific databases

CTD

281447.

Phylogenomic databases

eggNOG

maNOG16275.

HOVERGEN

P21457.

InParanoid

P21457.

PhylomeDB

P21457.

Family and domain databases

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR001125. Recoverin.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

PRINTS

PR00450. RECOVERIN.

SMART

SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RECO_BOVIN

Accession

Primary (citable) accession number: P21457

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)