PRVA_RANTE
ID PRVA_RANTE Reviewed; 63 AA.
AC P84535;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Parvalbumin alpha {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=12122; Mass_error=10.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16899539};
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000255}.
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DR AlphaFoldDB; P84535; -.
DR SMR; P84535; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR008080; Parvalbumin.
DR PANTHER; PTHR11653; PTHR11653; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Direct protein sequencing; Metal-binding; Repeat;
KW Secreted.
FT CHAIN 1..>63
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073600"
FT DOMAIN <28..>38
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN <39..>63
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT NON_CONS 27..28
FT /evidence="ECO:0000303|PubMed:16899539"
FT NON_CONS 38..39
FT /evidence="ECO:0000303|PubMed:16899539"
FT NON_TER 63
FT /evidence="ECO:0000303|PubMed:16899539"
SQ SEQUENCE 63 AA; 6556 MW; 6EF7ABF20DE0E005 CRC64;
PMTDVLAAGD ISKAVAAFAA PESFNHKIEE EELGLILKVL LAAGDKDGDG KIGVDEFVTL
VSE
