S10A6_PIG
ID S10A6_PIG Reviewed; 90 AA.
AC Q2EN75;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen C.H., Ding S.T.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as calcium sensor and modulator, contributing to
CC cellular calcium signaling. May function by interacting with other
CC proteins, such as TPR-containing proteins, and indirectly play a role
CC in many physiological processes such as the reorganization of the actin
CC cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium
CC binding is cooperative (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts with
CC CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11
CC (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher
CC affinity for TP53 that is phosphorylated on its N-terminal domain, and
CC lower affinity for TP53 that is phosphorylated on its C-terminal
CC domain. Interacts with tropomyosin. Interacts with FKBP4. Interacts
CC with PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with TPPP; this interaction
CC inhibits TPPP dimerization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; DQ372082; ABD18457.1; -; mRNA.
DR RefSeq; NP_001038022.1; NM_001044557.1.
DR AlphaFoldDB; Q2EN75; -.
DR SMR; Q2EN75; -.
DR STRING; 9823.ENSSSCP00000020154; -.
DR PeptideAtlas; Q2EN75; -.
DR PRIDE; Q2EN75; -.
DR Ensembl; ENSSSCT00050026870; ENSSSCP00050011121; ENSSSCG00050019906.
DR GeneID; 733608; -.
DR KEGG; ssc:733608; -.
DR CTD; 6277; -.
DR InParanoid; Q2EN75; -.
DR OrthoDB; 1581517at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IMP:AgBase.
DR CDD; cd05029; S-100A6; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034118; S-100A6.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 3: Inferred from homology;
KW Acetylation; Calcium; Cell membrane; Cytoplasm; Membrane; Metal-binding;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..90
FT /note="Protein S100-A6"
FT /id="PRO_0000236021"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 48..83
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
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 MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06703"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14069"
FT MOD_RES 47
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14069"
SQ SEQUENCE 90 AA; 10060 MW; 8EB98C10F0049FC0 CRC64;
MACPLDQAIG LLVAIFHKYS GQEGDKNTLS KSELKELIQK ELTIGAKLQD AEIAKLMDDL
DRNKDQVVNF QEYVTFLGAL AMIYNDVLRG
