SORCN_CRIGR
ID SORCN_CRIGR Reviewed; 198 AA.
AC P05044;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Sorcin;
DE AltName: Full=22 kDa protein;
DE AltName: Full=CP-22;
DE AltName: Full=V19;
GN Name=SRI;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=3028774;
RA van der Bliek A.M., Meyers M.B., Biedler J.L., Hes E., Borst P.;
RT "A 22-kd protein (sorcin/V19) encoded by an amplified gene in multidrug-
RT resistant cells, is homologous to the calcium-binding light chain of
RT calpain.";
RL EMBO J. 5:3201-3208(1986).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-178, MUTAGENESIS OF
RP SER-178, AND TISSUE SPECIFICITY.
RX PubMed=15754088; DOI=10.1007/s00395-005-0518-7;
RA Matsumoto T., Hisamatsu Y., Ohkusa T., Inoue N., Sato T., Suzuki S.,
RA Ikeda Y., Matsuzaki M.;
RT "Sorcin interacts with sarcoplasmic reticulum Ca(2+)-ATPase and modulates
RT excitation-contraction coupling in the heart.";
RL Basic Res. Cardiol. 100:250-262(2005).
RN [3]
RP MUTAGENESIS OF TRP-99; TRP-105 AND GLU-124, CALCIUM-BINDING, FUNCTION,
RP INTERACTION WITH ANXA7, AND SUBUNIT.
RX PubMed=17029407; DOI=10.1021/bi060416a;
RA Colotti G., Zamparelli C., Verzili D., Mella M., Loughrey C.M., Smith G.L.,
RA Chiancone E.;
RT "The W105G and W99G sorcin mutants demonstrate the role of the D helix in
RT the Ca(2+)-dependent interaction with annexin VII and the cardiac ryanodine
RT receptor.";
RL Biochemistry 45:12519-12529(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 33-198.
RX PubMed=11922676; DOI=10.1006/jmbi.2002.5417;
RA Ilari A., Johnson K.A., Nastopoulos V., Verzili D., Zamparelli C.,
RA Colotti G., Tsernoglou D., Chiancone E.;
RT "The crystal structure of the sorcin calcium binding domain provides a
RT model of Ca2+-dependent processes in the full-length protein.";
RL J. Mol. Biol. 317:447-458(2002).
CC -!- FUNCTION: Calcium-binding protein that modulates excitation-contraction
CC coupling in the heart. Contributes to calcium homeostasis in the
CC sarcoplasmic reticulum in the heart. Modulates the activity of RYR2
CC calcium channels. {ECO:0000269|PubMed:15754088,
CC ECO:0000269|PubMed:17029407}.
CC -!- SUBUNIT: Homodimer. Interacts with GCA and RYR2 (By similarity).
CC Interacts with ANXA7. {ECO:0000250, ECO:0000269|PubMed:17029407}.
CC -!- INTERACTION:
CC P05044; Q07076: Anxa7; Xeno; NbExp=2; IntAct=EBI-10816377, EBI-10824194;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15754088}.
CC Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:15754088};
CC Peripheral membrane protein {ECO:0000269|PubMed:15754088}; Cytoplasmic
CC side {ECO:0000269|PubMed:15754088}. Note=Relocates to the sarcoplasmic
CC reticulum membrane in response to elevated calcium levels and
CC phosphorylation.
CC -!- TISSUE SPECIFICITY: Detected in myocardium.
CC {ECO:0000269|PubMed:15754088}.
CC -!- PTM: Phosphorylated; partially. {ECO:0000269|PubMed:15754088}.
CC -!- MISCELLANEOUS: This protein is encoded by an amplified gene in
CC multidrug-resistant cells.
CC -!- MISCELLANEOUS: This protein has been shown to bind calcium with high
CC affinity.
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DR EMBL; X04656; CAA28354.1; -; mRNA.
DR PDB; 1GJY; X-ray; 2.20 A; A/B/C/D=33-198.
DR PDBsum; 1GJY; -.
DR AlphaFoldDB; P05044; -.
DR SMR; P05044; -.
DR IntAct; P05044; 2.
DR STRING; 10029.XP_007613221.1; -.
DR iPTMnet; P05044; -.
DR PRIDE; P05044; -.
DR eggNOG; KOG0037; Eukaryota.
DR EvolutionaryTrace; P05044; -.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Membrane; Metal-binding; Phosphoprotein;
KW Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..198
FT /note="Sorcin"
FT /id="PRO_0000073724"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 70..103
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 100..135
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
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 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15754088"
FT MUTAGEN 99
FT /note="W->G: No significant effect."
FT /evidence="ECO:0000269|PubMed:17029407"
FT MUTAGEN 105
FT /note="W->G: Reduced affinity for calcium, resulting in
FT reduced interaction with ANXA7 and strongly reduced
FT modulation of RYR2 channel activity."
FT /evidence="ECO:0000269|PubMed:17029407"
FT MUTAGEN 124
FT /note="E->A: Strongly reduced modulation of RYR2 channel
FT activity."
FT /evidence="ECO:0000269|PubMed:17029407"
FT MUTAGEN 178
FT /note="S->D: Increases calcium-sensitivity and promotes
FT interaction with sarcoplasmic reticulum membranes."
FT /evidence="ECO:0000269|PubMed:15754088"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:1GJY"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:1GJY"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:1GJY"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 156..176
FT /evidence="ECO:0007829|PDB:1GJY"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1GJY"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1GJY"
SQ SEQUENCE 198 AA; 21746 MW; DA2AF8A9707561C5 CRC64;
MAYPGHPGAG GGYYPGGYGG APGGPSFPGQ TQDPLYGYFA SVAGQDGQID ADELQRCLTQ
SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA VLNGWRQHFI SFDSDRSGTV
DPQELQKALT TMGFRLNPQT VNSIAKRYST SGKITFDDYI ACCVKLRALT DSFRRRDSAQ
QGMVNFSYDD FIQCVMTV
