S10A6_RAT
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 03-AUG-2022, entry version 155.
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}.
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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; P05964; -.
DR PRIDE; P05964; -.
DR Ensembl; ENSRNOT00000015612; ENSRNOP00000015612; ENSRNOG00000011647.
DR GeneID; 85247; -.
DR KEGG; rno:85247; -.
DR UCSC; RGD:620264; rat.
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; 1581517at2759; -.
DR PhylomeDB; P05964; -.
DR TreeFam; TF332727; -.
DR PRO; PR:P05964; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011647; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; P05964; baseline and differential.
DR Genevisible; P05964; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; 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: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 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 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
