S10A6_HORSE
ID S10A6_HORSE Reviewed; 92 AA.
AC O77691;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6; Synonyms=CACY;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10331456;
RX DOI=10.1002/(sici)1098-2795(199906)53:2<179::aid-mrd7>3.0.co;2-p;
RA Simpson K.S., Adams M.H., Behrendt-Adam C.Y., Baker C.B., McDowell K.J.;
RT "Identification and initial characterization of calcyclin and phospholipase
RT A2 in equine conceptuses.";
RL Mol. Reprod. Dev. 53:179-187(1999).
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; AF083065; AAC33290.1; -; mRNA.
DR RefSeq; NP_001075310.1; NM_001081841.1.
DR AlphaFoldDB; O77691; -.
DR SMR; O77691; -.
DR STRING; 9796.ENSECAP00000006408; -.
DR PaxDb; O77691; -.
DR PeptideAtlas; O77691; -.
DR PRIDE; O77691; -.
DR Ensembl; ENSECAT00000008544; ENSECAP00000006408; ENSECAG00000008401.
DR GeneID; 100033887; -.
DR KEGG; ecb:100033887; -.
DR CTD; 6277; -.
DR VGNC; VGNC:22655; S100A6.
DR GeneTree; ENSGT00940000161896; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; O77691; -.
DR OMA; LVVICHK; -.
DR OrthoDB; 1581517at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000008401; Expressed in chorionic villus and 23 other tissues.
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; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044548; F:S100 protein binding; IBA:GO_Central.
DR GO; GO:0005523; F:tropomyosin binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
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..92
FT /note="Protein S100-A6"
FT /id="PRO_0000143983"
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"
SQ SEQUENCE 92 AA; 10280 MW; 997A2A9E768CE9F3 CRC64;
MACPLDQAIS LLVAIFHKYS SREGDKNTLS KGELKELIQK ELTIGAELED SEIAKLLDDL
DQNKDQVVNF QEYVTFLGAL AMIYNEVLKA CS
