S10AB_CHICK
ID S10AB_CHICK Reviewed; 101 AA.
AC P24479;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein S100-A11;
DE AltName: Full=Calgizzarin;
DE AltName: Full=S100 calcium-binding protein A11;
GN Name=S100A11;
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=9599666; DOI=10.1139/o97-092;
RA Schonekess B.O., Walsh M.P.;
RT "Molecular cloning and expression of avian smooth muscle S100A11
RT (calgizzarin, S100C).";
RL Biochem. Cell Biol. 75:771-775(1997).
RN [2]
RP PROTEIN SEQUENCE OF 15-79.
RC TISSUE=Gizzard smooth muscle;
RX PubMed=1917990; DOI=10.1016/s0021-9258(18)55115-2;
RA Todoroki H., Kobayashi R., Watanabe M., Minami H., Hidaka H.;
RT "Purification, characterization, and partial sequence analysis of a newly
RT identified EF-hand type 13-kDa Ca(2+)-binding protein from smooth muscle
RT and non-muscle tissues.";
RL J. Biol. Chem. 266:18668-18673(1991).
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- TISSUE SPECIFICITY: Smooth muscle and non-muscle tissues.
CC -!- MISCELLANEOUS: Binds two calcium ions per molecule with an affinity
CC similar to that of the S100 proteins.
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; U77733; AAB36542.1; -; mRNA.
DR PIR; A41004; A41004.
DR RefSeq; NP_990497.1; NM_205166.2.
DR AlphaFoldDB; P24479; -.
DR SMR; P24479; -.
DR STRING; 9031.ENSGALP00000014912; -.
DR PaxDb; P24479; -.
DR Ensembl; ENSGALT00000066976; ENSGALP00000047847; ENSGALG00000036711.
DR GeneID; 396075; -.
DR KEGG; gga:396075; -.
DR CTD; 6282; -.
DR VEuPathDB; HostDB:geneid_396075; -.
DR eggNOG; ENOG502SS6H; Eukaryota.
DR GeneTree; ENSGT00940000154172; -.
DR HOGENOM; CLU_138624_1_0_1; -.
DR InParanoid; P24479; -.
DR OMA; MACEKCY; -.
DR OrthoDB; 1549220at2759; -.
DR PhylomeDB; P24479; -.
DR TreeFam; TF332727; -.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:P24479; -.
DR Proteomes; UP000000539; Chromosome 25.
DR Bgee; ENSGALG00000036711; Expressed in granulocyte and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0044548; F:S100 protein binding; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028482; S100A11.
DR PANTHER; PTHR11639:SF60; PTHR11639:SF60; 1.
DR Pfam; PF00036; EF-hand_1; 1.
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; 2.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..101
FT /note="Protein S100-A11"
FT /id="PRO_0000144014"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
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 32
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 37
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 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 69
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 71
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 73
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 78
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 101 AA; 11413 MW; BEB255F172C54F76 CRC64;
MSKVSPTETE RCIESLLAVF QRYAGREGDN LKLSKKEFRT FMNTELASFT KNQKDPAVVD
RMMKRLDINS DGQLDFQEFL NLIGGIAVAC HDALLVQPPH P
