ID S10A6_RAT Reviewed; 89 AA. AC P05964; Q9R2B7; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 3. DT 24-JAN-2024, entry version 162. DE RecName: Full=Protein S100-A6; DE AltName: Full=Calcyclin; DE AltName: Full=Prolactin receptor-associated protein; DE AltName: Full=S100 calcium-binding protein A6; GN Name=S100a6; Synonyms=Cacy; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2448309; DOI=10.1016/s0021-9258(18)69220-8; RA Murphy L.C., Murphy L.J., Tsuyuki D., Duckworth M.L., Shiu R.P.C.; RT "Cloning and characterization of a cDNA encoding a highly conserved, RT putative calcium binding protein, identified by an anti-prolactin receptor RT antiserum."; RL J. Biol. Chem. 263:2397-2401(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RX PubMed=10673048; DOI=10.1016/s0167-4781(99)00208-0; RA Konrad L., Aumueller G.; RT "Calcyclin is differentially expressed in rat testicular cells."; RL Biochim. Biophys. Acta 1489:440-444(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; RA Kizawa K.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 48-55, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Lubec G., Kang S.U., Lubec S.; RL Submitted (SEP-2007) to UniProtKB. 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 -!- MISCELLANEOUS: This protein co-purified with the prolactin receptor. CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ132717; CAB42002.1; -; mRNA. DR EMBL; AF140232; AAK28306.1; -; mRNA. DR PIR; B28363; B28363. DR RefSeq; NP_445937.1; NM_053485.2. DR RefSeq; XP_006232841.1; XM_006232779.3. DR AlphaFoldDB; P05964; -. DR SMR; P05964; -. DR BioGRID; 250051; 2. DR IntAct; P05964; 2. DR STRING; 10116.ENSRNOP00000015612; -. DR iPTMnet; P05964; -. DR PhosphoSitePlus; P05964; -. DR jPOST; P05964; -. DR PaxDb; 10116-ENSRNOP00000015612; -. DR Ensembl; ENSRNOT00000015612.6; ENSRNOP00000015612.2; ENSRNOG00000011647.6. DR Ensembl; ENSRNOT00055038728; ENSRNOP00055031443; ENSRNOG00055022563. DR Ensembl; ENSRNOT00060056250; ENSRNOP00060046456; ENSRNOG00060032478. DR Ensembl; ENSRNOT00065047307; ENSRNOP00065038793; ENSRNOG00065027442. DR GeneID; 85247; -. DR KEGG; rno:85247; -. DR UCSC; RGD:620264; rat. DR AGR; RGD:620264; -. DR CTD; 6277; -. DR RGD; 620264; S100a6. DR eggNOG; ENOG502S6IN; Eukaryota. DR GeneTree; ENSGT00940000161896; -. DR HOGENOM; CLU_138624_2_0_1; -. DR InParanoid; P05964; -. DR OMA; LVVICHK; -. DR OrthoDB; 4638795at2759; -. DR PhylomeDB; P05964; -. DR TreeFam; TF332727; -. DR PRO; PR:P05964; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000011647; Expressed in stomach and 19 other cell types or tissues. DR ExpressionAtlas; P05964; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD. DR GO; GO:0001726; C:ruffle; ISO:RGD. DR GO; GO:0005509; F:calcium ion binding; IDA:RGD. DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD. DR GO; GO:0015075; F:monoatomic ion transmembrane transporter activity; IDA:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0044548; F:S100 protein binding; ISO:RGD. DR GO; GO:0005523; F:tropomyosin binding; ISO:RGD. DR GO; GO:0008270; F:zinc ion binding; ISO:RGD. DR CDD; cd05029; S-100A6; 1. DR Gene3D; 1.10.238.10; EF-hand; 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 PANTHER; PTHR11639:SF80; PROTEIN S100-A6; 1. DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 1. DR Pfam; PF01023; S_100; 1. DR SMART; SM00054; EFh; 1. DR SMART; SM01394; S_100; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR PROSITE; PS00303; S100_CABP; 1. DR Genevisible; P05964; RN. PE 1: Evidence at protein level; KW Acetylation; Calcium; Cell membrane; Cytoplasm; Direct protein sequencing; KW Membrane; Metal-binding; Nucleus; Reference proteome; Repeat. FT CHAIN 1..89 FT /note="Protein S100-A6" FT /id="PRO_0000143987" 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 67 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" FT CONFLICT 89 FT /note="K -> KG (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" SQ SEQUENCE 89 AA; 10035 MW; 2AA1A4163D57DC87 CRC64; MACPLDQAIG LLVAIFHKYS GKEGDKHTLS KKELKELIQK ELTIGAKLQD AEIARLMDDL DRNKDQEVNF QEYVAFLGAL ALIYNEALK //