P04573 (CAVP_BRALA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Calcium vector protein Short name=CAVP
Organism	Branchiostoma lanceolatum (Common lancelet) (Amphioxus)
Taxonomic identifier	7740 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Cephalochordata › Branchiostomidae › Branchiostoma

Protein attributes

Sequence length	162 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	The exact function of this protein is not yet known. It interacts with CAVPT, a protein also of unknown function, in a calcium-dependent way. This protein binds two calcium ions.
Subcellular location	Cytoplasm.
Sequence similarities	Contains 4 EF-hand domains.
Caution	Was originally (Ref.2) thought to have an internal disulfide bond.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Calcium
Molecular function	Muscle protein
PTM	Acetylation Methylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium 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.2

Chain

2 – 162

161

Calcium vector protein

PRO_0000073578

Regions

Domain

12 – 47

36

EF-hand 1

Domain

49 – 84

36

EF-hand 2

Domain

86 – 121

36

EF-hand 3

Domain

123 – 158

36

EF-hand 4

Calcium binding

99 – 110

12

1

Calcium binding

136 – 147

12

2

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

Modified residue

96

1

N6,N6,N6-trimethyllysine

Modified residue

117

1

N6,N6,N6-trimethyllysine

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

162

Helix Strand Turn

Details...

Helix

13 – 24

12

Turn

26 – 29

4

Helix

34 – 43

10

Helix

50 – 61

12

Helix

74 – 83

10

Helix

89 – 98

10

Helix

102 – 104

3

Helix

108 – 114

7

Turn

117 – 120

4

Helix

125 – 135

11

Helix

139 – 141

3

Beta strand

142 – 144

3

Helix

145 – 153

9

Sequences

	Sequence		Length	Mass (Da)
	P04573 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D26139A009D6A042	FASTA	162	18,356
	10 20 30 40 50 60 MAAPKARALG PEEKDECMKI FDIFDRNAEN IAPVSDTMDM LTKLGQTYTK RETEAIMKEA 70 80 90 100 110 120 RGPKGDKKNI GPEEWLTLCS KWVRQDDEEE ILRAFKVFDA NGDGVIDFDE FKFIMQKVGE 130 140 150 160 EPLTDAEVEE AMKEADEDGN GVIDIPEFMD LIKKSKNALK ES

References

[1]	"Genomic structure of the amphioxus calcium vector protein." Yuasa H.J., Cox J.A., Takagi T. J. Biochem. 126:572-577(1999) [PubMed: 10467174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 154-155.
[2]	"The primary structure of a new Mr 18,000 calcium vector protein from amphioxus." Kobayashi T., Takagi T., Konishi K., Cox J.A. J. Biol. Chem. 262:2613-2623(1987) [PubMed: 3818612] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-162, ACETYLATION AT ALA-2.
[3]	"Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement." Theret I., Baladi S., Cox J.A., Sakamoto H., Craescu C.T. Biochemistry 39:7920-7926(2000) [PubMed: 10891072] [Abstract] Cited for: STRUCTURE BY NMR OF 82-161, CALCIUM BINDING.
[4]	"Solution structure and backbone dynamics of the defunct domain of calcium vector protein." Theret I., Baladi S., Cox J.A., Gallay J., Sakamoto H., Craescu C.T. Biochemistry 40:13888-13897(2001) [PubMed: 11705378] [Abstract] Cited for: STRUCTURE BY NMR OF 2-86, ABSENCE OF CALCIUM BINDING, ABSENCE OF DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB001688 mRNA. Translation: BAA19428.1.

PIR

A29557.
JC7157.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C7V	NMR	-	A	82-161	[»]
1C7W	NMR	-	A	82-161	[»]
1J7Q	NMR	-	A	2-86	[»]
1J7R	NMR	-	A	2-86	[»]

ProteinModelPortal

P04573.

SMR

P04573. Positions 2-155.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG098454.

Family and domain databases

InterPro

IPR018248. EF-hand.
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. 3 hits.

Pfam

PF00036. efhand. 2 hits.
[Graphical view]

PRINTS

PR00450. RECOVERIN.

SMART

SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CAVP_BRALA

Accession

Primary (citable) accession number: P04573
Secondary accession number(s): O01308

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	November 30, 2010
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program