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SORCN_PONAB
ID   SORCN_PONAB             Reviewed;         198 AA.
AC   Q5R4U9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Sorcin;
GN   Name=SRI;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calcium-binding protein that modulates excitation-contraction
CC       coupling in the heart. Contributes to calcium homeostasis in the heart
CC       sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with GCA, RYR2 and ANXA7 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Note=Relocates to the sarcoplasmic
CC       reticulum membrane in response to elevated calcium levels.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein has been shown to bind calcium with high
CC       affinity. {ECO:0000250}.
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DR   EMBL; CR861142; CAH93217.1; -; mRNA.
DR   RefSeq; NP_001127644.1; NM_001134172.1.
DR   AlphaFoldDB; Q5R4U9; -.
DR   SMR; Q5R4U9; -.
DR   STRING; 9601.ENSPPYP00000019992; -.
DR   PRIDE; Q5R4U9; -.
DR   Ensembl; ENSPPYT00000020780; ENSPPYP00000019992; ENSPPYG00000017838.
DR   GeneID; 100174725; -.
DR   KEGG; pon:100174725; -.
DR   CTD; 6717; -.
DR   eggNOG; KOG0037; Eukaryota.
DR   GeneTree; ENSGT00940000153979; -.
DR   HOGENOM; CLU_051357_4_1_1; -.
DR   InParanoid; Q5R4U9; -.
DR   OMA; RDTGQQG; -.
DR   OrthoDB; 1330600at2759; -.
DR   TreeFam; TF314682; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR   GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:Ensembl.
DR   GO; GO:0055118; P:negative regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0010459; P:negative regulation of heart rate; IEA:Ensembl.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
DR   GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; IEA:Ensembl.
DR   GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
DR   GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IEA:Ensembl.
DR   GO; GO:1901841; P:regulation of high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:1901077; P:regulation of relaxation of muscle; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Calcium; Cytoplasm; Membrane; Metal-binding; Reference proteome; Repeat;
KW   Sarcoplasmic reticulum.
FT   CHAIN           1..198
FT                   /note="Sorcin"
FT                   /id="PRO_0000073727"
FT   DOMAIN          45..64
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          70..98
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          151..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"
SQ   SEQUENCE   198 AA;  21676 MW;  A4829C7650A5E3FA CRC64;
     MAYPGHPGAG GGYYPGGYGG APGGPAFPGQ TQDPLYGYFA AVAGQDGQID ADELQRCLTQ
     SGIAGGYKPF NLETCRLMVS MLDRDMSGTM GFNEFKELWA VLNGWRQHFI SFDTDRSGTV
     DPQELQKALT TMGFRLSPQA VNSIAKRYST NGKITFDDYI ACCVKLRALT DSFRRRDTAQ
     QGVVNFPYDD FIQCVMSV
 
 
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