PRVB_SQUCE
ID PRVB_SQUCE Reviewed; 106 AA.
AC P05939;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Parvalbumin beta;
DE AltName: Full=Parvalbumin V;
OS Squalius cephalus (Chub) (Leuciscus cephalus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Leuciscidae; Leuciscinae; Squalius.
OX NCBI_TaxID=8284;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RA Gerday C., Collins S., Piront A.;
RT "Phylogenetic relationships between Cyprinidae Parvalbumins-II. The amino
RT acid sequence of the Parvalbumin V of Chub (Leuciscus cephalus L.).";
RL Comp. Biochem. Physiol. 61B:451-457(1978).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR AlphaFoldDB; P05939; -.
DR SMR; P05939; -.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR008080; Parvalbumin.
DR PANTHER; PTHR11653; PTHR11653; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Repeat.
FT CHAIN 1..106
FT /note="Parvalbumin beta"
FT /id="PRO_0000073612"
FT DOMAIN 36..71
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 75..106
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02621"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 90
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 106 AA; 11263 MW; BF27C2A24AFCCB4D CRC64;
AFGLKEADIT AALEACKAAD SFNHKAFFAK VGMSAKSAGD VKKAFEIIDE DKSGFIEEEE
LKLFLQNFKA GARALTDAET KIFLKAGDAD GDGKIGIDEF AALVKA