SCP_HEDDI
ID SCP_HEDDI Reviewed; 174 AA.
AC P04571;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sarcoplasmic calcium-binding protein;
DE Short=SCP;
OS Hediste diversicolor (Sandworm) (Nereis diversicolor).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Errantia; Phyllodocida; Nereididae; Hediste;
OC Hediste diversicolor species group.
OX NCBI_TaxID=126592;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX PubMed=3170587; DOI=10.1016/s0021-9258(19)37599-4;
RA Collins J.H., Cox J.A., Theibert J.L.;
RT "Amino acid sequence of a sarcoplasmic calcium-binding protein from the
RT sandworm Nereis diversicolor.";
RL J. Biol. Chem. 263:15378-15385(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1985922; DOI=10.1016/s0021-9258(18)52484-4;
RA Cook W.J., Ealick S.E., Babu Y.S., Cox J.A., Vijay-Kumar S.;
RT "Three-dimensional structure of a sarcoplasmic calcium-binding protein from
RT Nereis diversicolor.";
RL J. Biol. Chem. 266:652-656(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1560459; DOI=10.1016/0022-2836(92)91004-9;
RA Vijay-Kumar S., Cook W.J.;
RT "Structure of a sarcoplasmic calcium-binding protein from Nereis
RT diversicolor refined at 2.0-A resolution.";
RL J. Mol. Biol. 224:413-426(1992).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=8849695; DOI=10.1016/0014-5793(96)01007-1;
RA Precheur B., Cox J.A., Petrova T., Mispelter J., Craescu C.T.;
RT "Nereis sarcoplasmic Ca2+-binding protein has a highly unstructured apo
RT state which is switched to the native state upon binding of the first Ca2+
RT ion.";
RL FEBS Lett. 395:89-94(1996).
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 2 has lost affinity for calcium.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A31989; A31989.
DR PDB; 1Q80; NMR; -; A=1-174.
DR PDB; 2SCP; X-ray; 2.00 A; A/B=1-174.
DR PDBsum; 1Q80; -.
DR PDBsum; 2SCP; -.
DR AlphaFoldDB; P04571; -.
DR BMRB; P04571; -.
DR SMR; P04571; -.
DR iPTMnet; P04571; -.
DR EvolutionaryTrace; P04571; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
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; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Muscle protein; Repeat.
FT CHAIN 1..174
FT /note="Sarcoplasmic calcium-binding protein"
FT /id="PRO_0000073628"
FT DOMAIN 3..38
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 55..90
FT /note="EF-hand 2"
FT DOMAIN 91..126
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..160
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3170587"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:2SCP"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2SCP"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2SCP"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:2SCP"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:2SCP"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2SCP"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1Q80"
SQ SEQUENCE 174 AA; 19486 MW; 9569B2FD57AC449B CRC64;
SDLWVQKMKT YFNRIDFDKD GAITRMDFES MAERFAKESE MKAEHAKVLM DSLTGVWDNF
LTAVAGGKGI DETTFINSMK EMVKNPEAKS VVEGPLPLFF RAVDTNEDNN ISRDEYGIFF
GMLGLDKTMA PASFDAIDTN NDGLLSLEEF VIAGSDFFMN DGDSTNKVFW GPLV
