PRVB_RANTE
ID PRVB_RANTE Reviewed; 43 AA.
AC P84536;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Parvalbumin beta {ECO:0000303|PubMed:16899539};
DE Flags: Fragments;
OS Rana temporaria (European common frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=8407;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND CALCIUM-BINDING.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:16899539};
RX PubMed=16899539; DOI=10.1074/mcp.m600205-mcp200;
RA Leroy B., Toubeau G., Falmagne P., Wattiez R.;
RT "Identification and characterization of new protein chemoattractants in the
RT frog skin secretome.";
RL Mol. Cell. Proteomics 5:2114-2123(2006).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16899539}. Secreted
CC {ECO:0000269|PubMed:16899539}. Note=Cytoplasmic in muscle. Secreted in
CC cutaneous mucus. {ECO:0000269|PubMed:16899539}.
CC -!- TISSUE SPECIFICITY: Detected in muscle and cutaneous mucus. In the
CC skin, detected in cells in the basal region of the glandular epithelium
CC of the dermal mucus glands (at protein level).
CC {ECO:0000269|PubMed:16899539}.
CC -!- MASS SPECTROMETRY: Mass=11796; Mass_error=0.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16899539};
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000255}.
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DR AlphaFoldDB; P84536; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Direct protein sequencing; Metal-binding; Repeat;
KW Secreted.
FT CHAIN <1..>43
FT /note="Parvalbumin beta"
FT /id="PRO_0000073618"
FT DOMAIN <1..>20
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 22..>43
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT NON_CONS 20..21
FT /evidence="ECO:0000303|PubMed:16899539"
FT NON_CONS 32..33
FT /evidence="ECO:0000303|PubMed:16899539"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:16899539"
FT NON_TER 43
FT /evidence="ECO:0000303|PubMed:16899539"
SQ SEQUENCE 43 AA; 4907 MW; 59734B8C260FA633 CRC64;
KVFEILDMDR SFIEEELKLF ALSSAETAAF LKIGVEEFQA LVK
