ID   PRVA_LATCH              Reviewed;         111 AA.
AC   P02629;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Parvalbumin alpha;
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 THR-1.
RX   PubMed=30486; DOI=10.1016/0005-2795(78)90073-9;
RA   Pechere J.-F., Rochat H., Ferraz C.;
RT   "Parvalbumins from coelacanth muscle. II. Amino acid sequence of the two
RT   less acidic components.";
RL   Biochim. Biophys. Acta 536:269-274(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   -!- PTM: Acetylation of Thr-1 converts C1 to C2.
CC   -!- MISCELLANEOUS: Isoelectric points of C1 and C2 are 5.4 and 5.0,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   PIR; A03064; PVLA.
DR   AlphaFoldDB; P02629; -.
DR   SMR; P02629; -.
DR   STRING; 7897.ENSLACP00000004606; -.
DR   iPTMnet; P02629; -.
DR   PRIDE; P02629; -.
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..111
FT                   /note="Parvalbumin alpha"
FT                   /id="PRO_0000073596"
FT   DOMAIN          40..75
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          79..111
FT                   /note="EF-hand 2"
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:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         103
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-acetylthreonine; in form C2"
FT                   /evidence="ECO:0000269|PubMed:30486"
SQ   SEQUENCE   111 AA;  12208 MW;  BAE17D440EECC7D7 CRC64;
     TKKMSEILKA EDIDKALNTF KEAGSFDHHK FFNLVGLKGK PDDTLKEVFG ILDQDKSGYI
     EEEELKFVLK GFAAGGRELT ANETKALLKA GDQDGDDKIG VDEFTNLVKA A