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SCP2_BRALA
ID   SCP2_BRALA              Reviewed;         185 AA.
AC   P04570;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Sarcoplasmic calcium-binding proteins II, V, VI, and VII;
DE            Short=SCP II;
DE            Short=SCP V;
DE            Short=SCP VI;
DE            Short=SCP VII;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Takagi T., Konishi K., Cox J.A.;
RT   "Amino acid sequence of two sarcoplasmic calcium-binding proteins from the
RT   protochordate amphioxus.";
RL   Biochemistry 25:3585-3592(1986).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=2209593; DOI=10.1111/j.1432-1033.1990.tb19239.x;
RA   Takagi T., Cox J.A.;
RT   "Amino acid sequences of four isoforms of amphioxus sarcoplasmic calcium-
RT   binding proteins.";
RL   Eur. J. Biochem. 192:387-399(1990).
RN   [3]
RP   PROTEIN SEQUENCE (SCP V TO VII).
RX   PubMed=1633848; DOI=10.1016/0014-5793(92)80429-k;
RA   Takagi T., Valette-Talbi L., Cox J.A.;
RT   "Primary structure of three minor isoforms of amphioxus sarcoplasmic
RT   calcium-binding proteins.";
RL   FEBS Lett. 302:159-160(1992).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX   PubMed=8429557; DOI=10.1006/jmbi.1993.1046;
RA   Cook W.J., Jeffrey L.C., Cox J.A., Vijay-Kumar S.;
RT   "Structure of a sarcoplasmic calcium-binding protein from amphioxus refined
RT   at 2.4-A resolution.";
RL   J. Mol. Biol. 229:461-471(1993).
CC   -!- FUNCTION: Like parvalbumins, SCPs seem to be more abundant in fast
CC       contracting muscles, but no functional relationship can be established
CC       from this distribution.
CC   -!- MISCELLANEOUS: The sarcoplasmic calcium-binding proteins are abundant
CC       in the muscle of arthropods, mollusks, annelids, and protochordates.
CC   -!- MISCELLANEOUS: This protein has three functional calcium-binding sites;
CC       potential site 4 has lost affinity for calcium.
CC   -!- MISCELLANEOUS: There are 7 different SCP's in amphioxus. The sequence
CC       shown here is that of SCP II.
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DR   PIR; S13183; S13183.
DR   PIR; S21153; S21153.
DR   PDB; 2SAS; X-ray; 2.40 A; A=1-185.
DR   PDBsum; 2SAS; -.
DR   AlphaFoldDB; P04570; -.
DR   SMR; P04570; -.
DR   EvolutionaryTrace; P04570; -.
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   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Direct protein sequencing; Metal-binding;
KW   Muscle protein; Repeat.
FT   CHAIN           1..185
FT                   /note="Sarcoplasmic calcium-binding proteins II, V, VI, and
FT                   VII"
FT                   /id="PRO_0000073633"
FT   DOMAIN          5..41
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          57..92
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          102..137
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          138..173
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         23
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         74
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         81
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         115
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         117
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         126
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VARIANT         25
FT                   /note="S -> A (in SCP V)"
FT   VARIANT         28
FT                   /note="D -> W (in SCP V, VI and VII)"
FT   VARIANT         29
FT                   /note="N -> E (in SCP VI)"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           28..42
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           48..69
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           79..91
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           141..149
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   TURN            150..153
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:2SAS"
FT   HELIX           176..181
FT                   /evidence="ECO:0007829|PDB:2SAS"
SQ   SEQUENCE   185 AA;  21286 MW;  76E3307B55C7595B CRC64;
     GLNDFQKQKI KFTFDFFLDM NHDGSIQDND FEDMMTRYKE VNKGSLSDAD YKSMQASLED
     EWRDLKGRAD INKDDVVSWE EYLAMWEKTI ATCKSVADLP AWCQNRIPFL FKGMDVSGDG
     IVDLEEFQNY CKNFQLQCAD VPAVYNVITD GGKVTFDLNR YKELYYRLLT SPAADAGNTL
     MGQKP
 
 
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