ID   PRVB_LATCH              Reviewed;         108 AA.
AC   P02623;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Parvalbumin beta;
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX   PubMed=708767; DOI=10.1016/0005-2795(78)90074-0;
RA   Jauregui-Adell J., Pechere J.-F.;
RT   "Parvalbumins from coelacanth muscle. III. Amino acid sequence of the major
RT   component.";
RL   Biochim. Biophys. Acta 536:275-282(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   -!- MISCELLANEOUS: This is the predominant parvalbumin in latimeria muscle.
CC   -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 4.52.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   PIR; A03058; PVLAB.
DR   AlphaFoldDB; P02623; -.
DR   SMR; P02623; -.
DR   STRING; 7897.ENSLACP00000003476; -.
DR   iPTMnet; P02623; -.
DR   eggNOG; KOG0027; Eukaryota.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
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; Reference proteome; Repeat.
FT   CHAIN           1..108
FT                   /note="Parvalbumin beta"
FT                   /id="PRO_0000073611"
FT   DOMAIN          38..73
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          77..108
FT                   /note="EF-hand 2"
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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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                   ECO:0000255|PROSITE-ProRule:PRU00448"
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         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         101
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:708767"
SQ   SEQUENCE   108 AA;  11732 MW;  A2E5B03ABD1B155D CRC64;
     AVAKLLAAAD VTAALEGCKA DDSFNHKVFF QKTGLAKKSN EELEAIFKIL DQDKSGFIED
     EELELFLQNF SAGARTLTKT ETETFLKAGD SDGDGKIGVD EFQKLVKA