P02617 (PRVB_RANES) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Parvalbumin beta Alternative name(s): Parvalbumin pI 4.50
Organism	Rana esculenta (Edible frog) (Pelophylax esculentus)
Taxonomic identifier	8401 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Pelophylax

Protein attributes

Sequence length	108 AA.
Sequence status	Complete.
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.
Miscellaneous	This parvalbumin has an isoelectric point of 4.5.
Sequence similarities	Belongs to the parvalbumin family. Contains 2 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Muscle protein
PTM	Acetylation
Technical term	Direct protein sequencing
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
	Chain	1 – 108	108	Parvalbumin beta		PRO_0000073617
Regions
	Domain	38 – 73	36	EF-hand 1
	Domain	77 – 108	32	EF-hand 2
	Calcium binding	51 – 62	12	1 Ref.2
	Calcium binding	90 – 101	12	2 Ref.2
Amino acid modifications
	Modified residue	1	1	N-acetylserine Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P02617 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 99BD9344CF344580	FASTA	108	11,581
	10 20 30 40 50 60 SITDIVSEKD IDAALESVKA AGSFNYKIFF QKVGLAGKSA ADAKKVFEIL DRDKSGFIEQ 70 80 90 100 DELGLFLQNF RASARVLSDA ETSAFLKAGD SDGDGKIGVE EFQALVKA

References

[1]	"The amino-acid sequence of the most acidic major parvalbumin from frog muscle." Capony J.-P., Demaille J.G., Pina C., Pechere J.-F. Eur. J. Biochem. 56:215-227(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Heat capacity and entropy changes of the two major isotypes of bullfrog (Rana catesbeiana) parvalbumins induced by calcium binding." Tanokura M., Yamada K. Biochemistry 26:7668-7674(1987) [PubMed] [Europe PMC] [Abstract] Cited for: CALCIUM-BINDING.

Cross-references

Sequence databases
PIR	PVFG. A03052.
3D structure databases
ProteinModelPortal	P02617.
SMR	P02617. Positions 5-108.
ModBase	Search...
Protein family/group databases
Allergome	893. Ran e 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG107490.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR008080. Parvalbumin. [Graphical view]
PANTHER	PTHR11653. PTHR11653. 1 hit.
Pfam	PF13499. EF_hand_5. 1 hit. [Graphical view]
SMART	SM00054. EFh. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRVB_RANES

Accession

Primary (citable) accession number: P02617

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program