P02625 (PRVA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Parvalbumin alpha

Gene names

Name:	Pvalb
Synonyms:	Pva

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	110 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	In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Sequence similarities	Belongs to the parvalbumin family. Contains 2 EF-hand domains.
Mass spectrometry	Molecular mass is 11836.88±1.57 Da from positions 2 - 110. Determined by ESI. Ref.8

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Muscle protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
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.4

Chain

2 – 110

109

Parvalbumin alpha

PRO_0000073592

Regions

Domain

39 – 74

36

EF-hand 1

Domain

78 – 110

33

EF-hand 2

Calcium binding

52 – 63

12

1 Ref.7

Calcium binding

91 – 102

12

2 Ref.7

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.4 Ref.8 Ref.9

Modified residue

73

1

Phosphoserine By similarity

Modified residue

79

1

Phosphoserine By similarity

Modified residue

83

1

Phosphothreonine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

110

Helix Strand Turn

Details...

Helix

3 – 6

4

Helix

9 – 17

9

Helix

27 – 33

7

Helix

41 – 51

11

Beta strand

56 – 59

4

Helix

61 – 64

4

Helix

67 – 71

5

Helix

80 – 90

11

Beta strand

95 – 98

4

Helix

100 – 106

7

Sequences

	Sequence		Length	Mass (Da)
	P02625 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6A1509AC8F012B3D	FASTA	110	11,926
	10 20 30 40 50 60 MSMTDLLSAE DIKKAIGAFT AADSFDHKKF FQMVGLKKKS ADDVKKVFHI LDKDKSGFIE 70 80 90 100 110 EDELGSILKG FSSDARDLSA KETKTLMAAG DKDGDGKIGV EEFSTLVAES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a rat parvalbumin gene and full length cDNA." Epstein P., Means A.R., Berchtold M.W. J. Biol. Chem. 261:5886-5891(1986) [PubMed: 3009434] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structural organization and chromosomal assignment of the parvalbumin gene." Berchtold M.W., Epstein P., Beaudet A.L., Payne M.E., Heizmann C.W., Means A.R. J. Biol. Chem. 262:8696-8701(1987) [PubMed: 3036821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Primary structure of parvalbumin from rat skeletal muscle." Berchtold M.W., Heizmann C.W., Wilson K.J. Eur. J. Biochem. 127:381-389(1982) [PubMed: 6754379] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-110, ACETYLATION AT SER-2.
[5]	Lubec G., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 15-29; 47-69 AND 98-110, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[6]	"The Ca2+-binding protein parvalbumin: molecular cloning and developmental regulation of mRNA abundance." Berchtold M.W., Means A.R. Proc. Natl. Acad. Sci. U.S.A. 82:1414-1418(1985) [PubMed: 3856270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-55 AND 84-92.
[7]	"1H NMR spectroscopic studies of calcium-binding proteins. 3. Solution conformations of rat apo-alpha-parvalbumin and metal-bound rat alpha-parvalbumin." Williams T.C., Corson D.C., Oikawa K., McCubbin W.D., Kay C.M., Sykes B.D. Biochemistry 25:1835-1846(1986) [PubMed: 3707914] [Abstract] Cited for: CALCIUM-BINDING.
[8]	"Electrospray ionization mass spectrometry: analysis of the Ca2+-binding properties of human recombinant alpha-parvalbumin and nine mutant proteins." Troxler H., Kuster T., Rhyner J.A., Gehrig P., Heizmann C.W. Anal. Biochem. 268:64-71(1999) [PubMed: 10036163] [Abstract] Cited for: ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Skeletal muscle.
[9]	Lubec G., Chen W.-Q. Submitted (FEB-2007) to UniProtKB Cited for: ACETYLATION AT SER-2, MASS SPECTROMETRY.
[10]	"Refined crystal structure of rat parvalbumin, a mammalian alpha-lineage parvalbumin, at 2.0-A resolution." McPhalen C.A., Sielecki A.R., Santarsiero B.D., James M.N.G. J. Mol. Biol. 235:718-732(1994) [PubMed: 8289291] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12725 mRNA. Translation: AAA41799.1.
M15457 , M15453, M15454, M15455 Genomic DNA. Translation: AAA41800.1.
BC126090 mRNA. Translation: AAI26091.1.
M10764 mRNA. Translation: AAA41797.1.
M10765 mRNA. Translation: AAA41798.1.

IPI

IPI00231350.

PIR

PVRTA. A29308.

RefSeq

NP_071944.1. NM_022499.2.

UniGene

Rn.2005.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G33	X-ray	1.44	A	39-109	[»]
1RTP	X-ray	2.00	1/2/3	2-110	[»]
1RWY	X-ray	1.05	A/B/C	2-109	[»]
1S3P	X-ray	2.00	A	2-109	[»]
1XVJ	X-ray	1.80	A/B	2-109	[»]
2JWW	NMR	-	A	2-110	[»]
3F45	X-ray	2.00	A	2-110	[»]

ProteinModelPortal

P02625.

SMR

P02625. Positions 2-110.

ModBase

Search...

Protein-protein interaction databases

STRING

P02625.

Proteomic databases

PRIDE

P02625.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000009062; ENSRNOP00000009062; ENSRNOG00000006471.

GeneID

25269.

KEGG

rno:25269.

NMPDR

fig|10116.3.peg.27345.

UCSC

NM_022499. rat.

Organism-specific databases

CTD

5816.

RGD

3457. Pvalb.

Phylogenomic databases

eggNOG

roNOG17132.

GeneTree

ENSGT00390000008690.

HOVERGEN

HBG107490.

InParanoid

P02625.

OMA

DELGFIL.

OrthoDB

EOG4BK55C.

PhylomeDB

P02625.

Gene expression databases

ArrayExpress

P02625.

Genevestigator

P02625.

GermOnline

ENSRNOG00000006471. Rattus norvegicus.

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.
IPR008080. Parvalbumin.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

Pfam

PF00036. efhand. 1 hit.
[Graphical view]

PRINTS

PR01697. PARVALBUMIN.

SMART

SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

NextBio

605949.

Entry information

Entry name

PRVA_RAT

Accession

Primary (citable) accession number: P02625
Secondary accession number(s): A0JN21

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	September 21, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program