S10A9_MOUSE
ID S10A9_MOUSE Reviewed; 113 AA.
AC P31725;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein S100-A9;
DE AltName: Full=Calgranulin-B;
DE AltName: Full=Leukocyte L1 complex heavy chain;
DE AltName: Full=Migration inhibitory factor-related protein 14;
DE Short=MRP-14;
DE Short=p14;
DE AltName: Full=S100 calcium-binding protein A9;
GN Name=S100a9; Synonyms=Cagb, Mrp14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1373330;
RA Lagasse E., Weissman I.L.;
RT "Mouse MRP8 and MRP14, two intracellular calcium-binding proteins
RT associated with the development of the myeloid lineage.";
RL Blood 79:1907-1915(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11169745;
RX DOI=10.1002/1097-4644(20010315)80:4<606::aid-jcb1015>3.0.co;2-k;
RA Nacken W.K.F., Lekstrom-Himes J.A., Sorg C., Manitz M.;
RT "Molecular analysis of the mouse S100A9 gene and evidence that the myeloid
RT specific transcription factor C/EBPepsilon is not required for the
RT regulation of the S100A9/A8 gene expression in neutrophils.";
RL J. Cell. Biochem. 80:606-616(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-10; 76-93 AND 95-109, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=8645219; DOI=10.1042/bj3160285;
RA Raftery M.J., Harrison C.A., Alewood P.F., Jones A., Geczy C.L.;
RT "Isolation of the murine S100 protein MRP14 (14 kDa migration-inhibitory-
RT factor-related protein) from activated spleen cells: characterization of
RT post-translational modifications and zinc binding.";
RL Biochem. J. 316:285-293(1996).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12529407; DOI=10.1128/mcb.23.3.1034-1043.2003;
RA Manitz M.-P., Horst B., Seeliger S., Strey A., Skryabin B.V., Gunzer M.,
RA Frings W., Schoenlau F., Roth J., Sorg C., Nacken W.;
RT "Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b
RT surface expression, a polarized microfilament system, and diminished
RT responsiveness to chemoattractants in vitro.";
RL Mol. Cell. Biol. 23:1034-1043(2003).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15331440; DOI=10.1182/blood-2004-02-0446;
RA Vogl T., Ludwig S., Goebeler M., Strey A., Thorey I.S., Reichelt R.,
RA Foell D., Gerke V., Manitz M.P., Nacken W., Werner S., Sorg C., Roth J.;
RT "MRP8 and MRP14 control microtubule reorganization during transendothelial
RT migration of phagocytes.";
RL Blood 104:4260-4268(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH TLR4 AND LY96.
RX PubMed=17767165; DOI=10.1038/nm1638;
RA Vogl T., Tenbrock K., Ludwig S., Leukert N., Ehrhardt C.,
RA van Zoelen M.A.D., Nacken W., Foell D., van der Poll T., Sorg C., Roth J.;
RT "Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4,
RT promoting lethal, endotoxin-induced shock.";
RL Nat. Med. 13:1042-1049(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH ATP2A2 AND AGER.
RX PubMed=18403730; DOI=10.1161/circresaha.107.167544;
RA Boyd J.H., Kan B., Roberts H., Wang Y., Walley K.R.;
RT "S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction via
RT the receptor for advanced glycation end products.";
RL Circ. Res. 102:1239-1246(2008).
RN [10]
RP REVIEW.
RX PubMed=20523765; DOI=10.2174/187152309789838975;
RA Hsu K., Champaiboon C., Guenther B.D., Sorenson B.S., Khammanivong A.,
RA Ross K.F., Geczy C.L., Herzberg M.C.;
RT "Anti-infective protective properties of S100 calgranulins.";
RL Antiinflamm. Antiallergy Agents Med. Chem. 8:290-305(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4; LY96 AND
RP AGER, AND QUINOLINE-3-CARBOXAMIDE BINDING.
RX PubMed=19402754; DOI=10.1371/journal.pbio.1000097;
RA Bjoerk P., Bjoerk A., Vogl T., Stenstroem M., Liberg D., Olsson A.,
RA Roth J., Ivars F., Leanderson T.;
RT "Identification of human S100A9 as a novel target for treatment of
RT autoimmune disease via binding to quinoline-3-carboxamides.";
RL PLoS Biol. 7:E97-E97(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP REVIEW.
RX PubMed=20213444; DOI=10.1007/s00726-010-0528-0;
RA Goyette J., Geczy C.L.;
RT "Inflammation-associated S100 proteins: new mechanisms that regulate
RT function.";
RL Amino Acids 41:821-842(2011).
RN [14]
RP FUNCTION.
RX PubMed=21382888; DOI=10.1161/circulationaha.110.985523;
RA Averill M.M., Barnhart S., Becker L., Li X., Heinecke J.W., Leboeuf R.C.,
RA Hamerman J.A., Sorg C., Kerkhoff C., Bornfeldt K.E.;
RT "S100A9 differentially modifies phenotypic states of neutrophils,
RT macrophages, and dendritic cells: implications for atherosclerosis and
RT adipose tissue inflammation.";
RL Circulation 123:1216-1226(2011).
RN [15]
RP FUNCTION.
RX PubMed=22804476; DOI=10.1111/j.1365-2567.2012.03619.x;
RA Riva M., Kaellberg E., Bjoerk P., Hancz D., Vogl T., Roth J., Ivars F.,
RA Leanderson T.;
RT "Induction of nuclear factor-kappaB responses by the S100A9 protein is
RT Toll-like receptor-4-dependent.";
RL Immunology 137:172-182(2012).
RN [16]
RP METHYLATION AT HIS-107.
RX PubMed=34562450; DOI=10.1016/j.jbc.2021.101230;
RA Daitoku H., Someya M., Kako K., Hayashi T., Tajima T., Haruki H.,
RA Sekiguchi N., Uetake T., Akimoto Y., Fukamizu A.;
RT "siRNA screening identifies METTL9 as a histidine Npi-methyltransferase
RT that targets the proinflammatory protein S100A9.";
RL J. Biol. Chem. 297:101230-101230(2021).
RN [17]
RP METHYLATION AT HIS-107, AND MUTAGENESIS OF HIS-103; HIS-105 AND HIS-107.
RX PubMed=33563959; DOI=10.1038/s41467-020-20670-7;
RA Davydova E., Shimazu T., Schuhmacher M.K., Jakobsson M.E.,
RA Willemen H.L.D.M., Liu T., Moen A., Ho A.Y.Y., Malecki J., Schroer L.,
RA Pinto R., Suzuki T., Groensberg I.A., Sohtome Y., Akakabe M., Weirich S.,
RA Kikuchi M., Olsen J.V., Dohmae N., Umehara T., Sodeoka M., Siino V.,
RA McDonough M.A., Eijkelkamp N., Schofield C.J., Jeltsch A., Shinkai Y.,
RA Falnes P.O.;
RT "The methyltransferase METTL9 mediates pervasive 1-methylhistidine
RT modification in mammalian proteomes.";
RL Nat. Commun. 12:891-891(2021).
CC -!- FUNCTION: S100A9 is a calcium- and zinc-binding protein which plays a
CC prominent role in the regulation of inflammatory processes and immune
CC response (PubMed:15331440, PubMed:17767165, PubMed:18403730,
CC PubMed:19402754, PubMed:22804476, PubMed:34562450). It can induce
CC neutrophil chemotaxis, adhesion, can increase the bactericidal activity
CC of neutrophils by promoting phagocytosis via activation of SYK,
CC PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a
CC MAPK-dependent mechanism (By similarity). Predominantly found as
CC calprotectin (S100A8/A9) which has a wide plethora of intra- and
CC extracellular functions (By similarity). The intracellular functions
CC include: facilitating leukocyte arachidonic acid trafficking and
CC metabolism, modulation of the tubulin-dependent cytoskeleton during
CC migration of phagocytes and activation of the neutrophilic NADPH-
CC oxidase (PubMed:15331440). Activates NADPH-oxidase by facilitating the
CC enzyme complex assembly at the cell membrane, transferring arachidonic
CC acid, an essential cofactor, to the enzyme complex and S100A8
CC contributes to the enzyme assembly by directly binding to NCF2/P67PHOX
CC (By similarity). The extracellular functions involve pro-inflammatory,
CC antimicrobial, oxidant-scavenging and apoptosis-inducing activities
CC (PubMed:21382888). Its pro-inflammatory activity includes recruitment
CC of leukocytes, promotion of cytokine and chemokine production, and
CC regulation of leukocyte adhesion and migration (By similarity). Acts as
CC an alarmin or a danger associated molecular pattern (DAMP) molecule and
CC stimulates innate immune cells via binding to pattern recognition
CC receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced
CC glycation endproducts (AGER) (PubMed:17767165, PubMed:18403730,
CC PubMed:19402754). Binding to TLR4 and AGER activates the MAP-kinase and
CC NF-kappa-B signaling pathways resulting in the amplification of the
CC pro-inflammatory cascade (PubMed:17767165, PubMed:18403730,
CC PubMed:19402754, PubMed:22804476). Has antimicrobial activity towards
CC bacteria and fungi and exerts its antimicrobial activity probably via
CC chelation of Zn(2+) which is essential for microbial growth (By
CC similarity). Can induce cell death via autophagy and apoptosis and this
CC occurs through the cross-talk of mitochondria and lysosomes via
CC reactive oxygen species (ROS) and the process involves BNIP3 (By
CC similarity). Can regulate neutrophil number and apoptosis by an anti-
CC apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a
CC signaling mechanism involving MEK-ERK (By similarity). Its role as an
CC oxidant scavenger has a protective role in preventing exaggerated
CC tissue damage by scavenging oxidants (By similarity). The iNOS-
CC S100A8/A9 transnitrosylase complex is proposed to direct selective
CC inflammatory stimulus-dependent S-nitrosylation of multiple targets
CC such as GAPDH, NXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-
CC [DE] motif (By similarity). {ECO:0000250|UniProtKB:P06702,
CC ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:17767165,
CC ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:19402754,
CC ECO:0000269|PubMed:21382888, ECO:0000269|PubMed:22804476,
CC ECO:0000269|PubMed:34562450}.
CC -!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
CC heterotetramer with S100A8 known as calprotectin (S100A8/A9)
CC (PubMed:34562450). S100A9 interacts with ATP2A2 (PubMed:18403730).
CC S100A9 interacts with AGER, and with the heterodimeric complex formed
CC by TLR4 and LY96 in the presence of calcium and/or zinc ions
CC (PubMed:17767165, PubMed:19402754, PubMed:18403730). S100A9 binds
CC quinoline-3-carboxamides in the presence of calcium and/or zinc ions.
CC S100A9 interacts with amyloid-beta protein 40. Calprotectin (S100A8/9)
CC interacts with CEACAM3 and tubulin filaments in a calcium-dependent
CC manner. Heterotetrameric calprotectin (S100A8/A9) interacts with ANXA6
CC and associates with tubulin filaments in activated monocytes.
CC Calprotectin (S100A8/9) interacts with NCF2/P67PHOX, RAC1, RAC2, CYBA
CC and CYBB. Calprotectin (S100A8/9) interacts with NOS2 to form the iNOS-
CC S100A8/A9 transnitrosylase complex; induced by LDL(ox) (By similarity).
CC {ECO:0000250|UniProtKB:P06702, ECO:0000269|PubMed:17767165,
CC ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:19402754,
CC ECO:0000269|PubMed:34562450}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06702}.
CC Cytoplasm {ECO:0000250|UniProtKB:P06702}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P06702}. Cell membrane
CC {ECO:0000250|UniProtKB:P06702}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P06702}. Note=Predominantly localized in the
CC cytoplasm. Upon elevation of the intracellular calcium level,
CC translocated from the cytoplasm to the cytoskeleton and the cell
CC membrane. Upon neutrophil activation or endothelial adhesion of
CC monocytes, is secreted via a microtubule-mediated, alternative pathway.
CC {ECO:0000250|UniProtKB:P06702}.
CC -!- PTM: Phosphorylated. Phosphorylation inhibits activation of tubulin
CC polymerization. {ECO:0000250|UniProtKB:P06702}.
CC -!- PTM: Methylation at His-107 by METTL9 reduces zinc-binding without
CC affecting heterodimerization with S100A8. {ECO:0000269|PubMed:33563959,
CC ECO:0000269|PubMed:34562450}.
CC -!- MASS SPECTROMETRY: Mass=12972; Mass_error=2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8645219};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Alters response of
CC phagocytes to stimulation with bacterial lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:12529407, ECO:0000269|PubMed:17767165}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; M83219; AAB07228.1; -; mRNA.
DR EMBL; AJ250496; CAC14292.1; -; Genomic_DNA.
DR EMBL; BC027635; AAH27635.1; -; mRNA.
DR CCDS; CCDS17543.1; -.
DR PIR; S68242; S68242.
DR RefSeq; NP_001268781.1; NM_001281852.1.
DR RefSeq; NP_033140.1; NM_009114.3.
DR PDB; 6ZDY; X-ray; 1.45 A; A=1-113.
DR PDB; 6ZFE; X-ray; 2.35 A; A=1-113.
DR PDBsum; 6ZDY; -.
DR PDBsum; 6ZFE; -.
DR AlphaFoldDB; P31725; -.
DR SMR; P31725; -.
DR BioGRID; 203057; 9.
DR ComplexPortal; CPX-40; Calprotectin heterotetramer.
DR ComplexPortal; CPX-41; Calprotectin heterodimer.
DR ComplexPortal; CPX-49; S100A9 complex.
DR ComplexPortal; CPX-53; iNOS-S100A8/A9 complex.
DR IntAct; P31725; 1.
DR STRING; 10090.ENSMUSP00000112843; -.
DR iPTMnet; P31725; -.
DR PhosphoSitePlus; P31725; -.
DR CPTAC; non-CPTAC-3410; -.
DR PaxDb; P31725; -.
DR PeptideAtlas; P31725; -.
DR PRIDE; P31725; -.
DR ProteomicsDB; 253331; -.
DR DNASU; 20202; -.
DR Ensembl; ENSMUST00000069960; ENSMUSP00000070842; ENSMUSG00000056071.
DR Ensembl; ENSMUST00000117167; ENSMUSP00000112843; ENSMUSG00000056071.
DR GeneID; 20202; -.
DR KEGG; mmu:20202; -.
DR UCSC; uc008qde.2; mouse.
DR CTD; 6280; -.
DR MGI; MGI:1338947; S100a9.
DR VEuPathDB; HostDB:ENSMUSG00000056071; -.
DR eggNOG; ENOG502SA01; Eukaryota.
DR GeneTree; ENSGT00940000161606; -.
DR HOGENOM; CLU_138624_6_0_1; -.
DR InParanoid; P31725; -.
DR OMA; NTFHHYS; -.
DR OrthoDB; 1521098at2759; -.
DR PhylomeDB; P31725; -.
DR TreeFam; TF332727; -.
DR Reactome; R-MMU-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
DR BioGRID-ORCS; 20202; 0 hits in 71 CRISPR screens.
DR ChiTaRS; S100a9; mouse.
DR PRO; PR:P31725; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P31725; protein.
DR Bgee; ENSMUSG00000056071; Expressed in granulocyte and 150 other tissues.
DR ExpressionAtlas; P31725; baseline and differential.
DR Genevisible; P31725; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
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:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR GO; GO:0035425; P:autocrine signaling; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0002544; P:chronic inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0035821; P:modulation of process of another organism; ISO:MGI.
DR GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0002790; P:peptide secretion; IDA:MGI.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:UniProtKB.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:CACAO.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0002793; P:positive regulation of peptide secretion; IDA:MGI.
DR GO; GO:0045113; P:regulation of integrin biosynthetic process; IMP:MGI.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antimicrobial; Antioxidant; Apoptosis;
KW Autophagy; Calcium; Cell membrane; Chemotaxis; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Immunity; Inflammatory response;
KW Innate immunity; Membrane; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8645219"
FT CHAIN 2..113
FT /note="Protein S100-A9"
FT /id="PRO_0000143998"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 55..90
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06702"
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:0000250|UniProtKB:P06702"
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:0000250|UniProtKB:P06702"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
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:0000250|UniProtKB:P06702"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06702"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:8645219"
FT MOD_RES 107
FT /note="Pros-methylhistidine"
FT /evidence="ECO:0000269|PubMed:33563959,
FT ECO:0000269|PubMed:34562450"
FT MUTAGEN 103
FT /note="H->A: Reduced histidine methylation by METTL9."
FT /evidence="ECO:0000269|PubMed:33563959"
FT MUTAGEN 105
FT /note="H->A: Reduced histidine methylation by METTL9."
FT /evidence="ECO:0000269|PubMed:33563959"
FT MUTAGEN 107
FT /note="H->A,F: Reduced histidine methylation by METTL9."
FT /evidence="ECO:0000269|PubMed:33563959,
FT ECO:0000269|PubMed:34562450"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:6ZDY"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:6ZDY"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:6ZDY"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6ZDY"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6ZDY"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6ZDY"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6ZDY"
FT HELIX 77..98
FT /evidence="ECO:0007829|PDB:6ZDY"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6ZDY"
SQ SEQUENCE 113 AA; 13049 MW; F4DCFBD1A181F812 CRC64;
MANKAPSQME RSITTIIDTF HQYSRKEGHP DTLSKKEFRQ MVEAQLATFM KKEKRNEALI
NDIMEDLDTN QDNQLSFEEC MMLMAKLIFA CHEKLHENNP RGHGHSHGKG CGK
