S10A6_CHICK
ID S10A6_CHICK Reviewed; 92 AA.
AC Q98953;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gizzard;
RX PubMed=9599662; DOI=10.1139/o97-068;
RA Allen B.G., Andrea J.E., Sutherland C., Schonekess B.O., Walsh M.P.;
RT "Molecular cloning of chicken calcyclin (S100A6) and identification of
RT putative isoforms.";
RL Biochem. Cell Biol. 75:733-738(1997).
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 -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; U76365; AAB18788.1; -; mRNA.
DR RefSeq; NP_989479.1; NM_204148.1.
DR AlphaFoldDB; Q98953; -.
DR SMR; Q98953; -.
DR PaxDb; Q98953; -.
DR Ensembl; ENSGALT00000065566; ENSGALP00000043598; ENSGALG00000041826.
DR GeneID; 373951; -.
DR KEGG; gga:373951; -.
DR CTD; 6277; -.
DR VEuPathDB; HostDB:geneid_373951; -.
DR GeneTree; ENSGT00940000161896; -.
DR InParanoid; Q98953; -.
DR OMA; LVVICHK; -.
DR OrthoDB; 1581517at2759; -.
DR PhylomeDB; Q98953; -.
DR PRO; PR:Q98953; -.
DR Proteomes; UP000000539; Chromosome 25.
DR Bgee; ENSGALG00000041826; Expressed in ovary and 14 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
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; IDA:AgBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
DR GO; GO:0019899; F:enzyme binding; IDA:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
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 GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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 Calcium; Cell cycle; Metal-binding; Mitogen; Reference proteome; Repeat.
FT CHAIN 1..92
FT /note="Protein S100-A6"
FT /id="PRO_0000143988"
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 /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
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 /ligand_note="high affinity"
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 /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
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 /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 92 AA; 10276 MW; 56B3D65BAA7BF7A4 CRC64;
MAAPLDQAIG LLVATFHKYS GKEGDKNSLS KGELKELIQK ELTIGPKLKD AEIAGLMEDL
DRNKDQEVNF QEYVTFLGAL AMIYNEALLQ YK
