ID A0A444UVB6_ACIRT Unreviewed; 286 AA.
AC A0A444UVB6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein S100-A1 {ECO:0000256|ARBA:ARBA00014215};
DE AltName: Full=S-100 protein alpha chain {ECO:0000256|ARBA:ARBA00030052};
DE AltName: Full=S-100 protein subunit alpha {ECO:0000256|ARBA:ARBA00032463};
DE AltName: Full=S100 calcium-binding protein A1 {ECO:0000256|ARBA:ARBA00032803};
GN ORFNames=EOD39_20526 {ECO:0000313|EMBL:RXM92067.1};
OS Acipenser ruthenus (Sterlet sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7906 {ECO:0000313|EMBL:RXM92067.1, ECO:0000313|Proteomes:UP000289886};
RN [1] {ECO:0000313|EMBL:RXM92067.1, ECO:0000313|Proteomes:UP000289886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WHYD16114868_AA {ECO:0000313|EMBL:RXM92067.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RXM92067.1};
RA Wei Q.;
RT "Draft Genome and Complete Hox-Cluster Characterization of the Sterlet
RT Sturgeon (Acipenser ruthenus).";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00004369}.
CC -!- SIMILARITY: Belongs to the S-100 family.
CC {ECO:0000256|ARBA:ARBA00007323}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXM92067.1}.
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DR EMBL; SCEB01007066; RXM92067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444UVB6; -.
DR Proteomes; UP000289886; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR CDD; cd05025; S-100A1; 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; IPR028486; S100-A1.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR11639:SF131; PROTEIN S100; 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000289886};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT DOMAIN 50..85
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 136..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 286 AA; 31646 MW; 9384F4E8CBEC4433 CRC64;
MVSELEQAME SLIKVFHTYS GKEGDKYKLS KAEMKSLLQG ELGCFLSASK DPNVVDQIMR
DLDENKDGEV DFQEYVVLVA SLTVACNEFF TRPETIAFME QPAVDRIEMN LKHKQIEKQR
GVVTMYKKSM ALMIPKAPPL PPRMNHASMS DLPPRRDGNG MASQMMSADR EPCTSTALGK
TAYPPERNAA KKGKDPDPRN KGQLPAQKRR AGVSRDSGGN LSPGEKKGAT GGPHEPPCFS
IRLSVTVCNS ICKLRLLNRK SSDSFKQKAG LALSITMKLY QMKAFI
//
