ID S10A8_HUMAN Reviewed; 93 AA. AC P05109; A8K5L3; Q5SY70; Q9UC84; Q9UC92; Q9UCJ0; Q9UCM6; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 03-NOV-2009, entry version 114. DE RecName: Full=Protein S100-A8; DE AltName: Full=S100 calcium-binding protein A8; DE AltName: Full=Calgranulin-A; DE AltName: Full=Migration inhibitory factor-related protein 8; DE Short=MRP-8; DE Short=P8; DE AltName: Full=Cystic fibrosis antigen; DE Short=CFAG; DE AltName: Full=Leukocyte L1 complex light chain; DE AltName: Full=Calprotectin L1L subunit; DE AltName: Full=Urinary stone protein band A; GN Name=S100A8; Synonyms=CAGA, CFAG, MRP8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87173041; PubMed=3561500; DOI=10.1038/326614a0; RA Dorin J.R., Novak M., Hill R.E., Brock D.J.H., Secher D.S., RA van Heyningen V.; RT "A clue to the basic defect in cystic fibrosis from cloning the CF RT antigen gene."; RL Nature 326:614-617(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88039099; PubMed=3313057; DOI=10.1038/330080a0; RA Odink K., Cerletti N., Bruggen J., Clerc R.G., Tarcsay L., Zwaldo G., RA Gerhards G., Schlegel R., Sorg C.; RT "Two calcium-binding proteins in infiltrate macrophages of rheumatoid RT arthritis."; RL Nature 330:80-82(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88302148; PubMed=3405210; RA Lagasse E., Clerc R.G.; RT "Cloning and expression of two human genes encoding calcium-binding RT proteins that are regulated during myeloid differentiation."; RL Mol. Cell. Biol. 8:2402-2410(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-30. RX MEDLINE=91248411; PubMed=2039599; RA Schaefer T., Sachse G.E., Gassen H.G.; RT "The calcium-binding protein MRP-8 is produced by human pulmonary RT tumor cells."; RL Biol. Chem. Hoppe-Seyler 372:1-4(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP PROTEIN SEQUENCE OF 1-19; 24-35 AND 63-89. RX MEDLINE=96192069; PubMed=8619876; DOI=10.1006/bbrc.1996.0616; RA Marti T., Erttmann K.D., Gallin M.Y.; RT "Host-parasite interaction in human onchocerciasis: identification and RT sequence analysis of a novel human calgranulin."; RL Biochem. Biophys. Res. Commun. 221:454-458(1996). RN [12] RP PROTEIN SEQUENCE OF 1-27. RX MEDLINE=93139333; PubMed=8423249; RA Miyasaki K.T., Bodeau A.L., Murthy A.R., Lehrer R.I.; RT "In vitro antimicrobial activity of the human neutrophil cytosolic S- RT 100 protein complex, calprotectin, against Capnocytophaga sputigena."; RL J. Dent. Res. 72:517-523(1993). RN [13] RP PROTEIN SEQUENCE OF 1-25. RC TISSUE=Neutrophil; RX MEDLINE=92406885; PubMed=1326551; RA Lemarchand P., Vaglio M., Mauel J., Markert M.; RT "Translocation of a small cytosolic calcium-binding protein (MRP-8) to RT plasma membrane correlates with human neutrophil activation."; RL J. Biol. Chem. 267:19379-19382(1992). RN [14] RP PROTEIN SEQUENCE OF 1-20. RX MEDLINE=95152434; PubMed=7849642; RA Umekawa T., Kurita T.; RT "Calprotectin-like protein is related to soluble organic matrix in RT calcium oxalate urinary stone."; RL Biochem. Mol. Biol. Int. 34:309-313(1994). RN [15] RP PROTEIN SEQUENCE OF 1-20. RC TISSUE=Ascites; RX MEDLINE=95209785; PubMed=7695842; RA Nakai M., Ishikawa M., Hamada Y., Sugano S.; RT "Isolation of an ascitic oncodevelopmental protein exhibiting high RT sequence homology with calcium-binding protein MRP8."; RL Biol. Chem. Hoppe-Seyler 375:789-792(1994). RN [16] RP PROTEIN SEQUENCE OF 38-47 AND 50-56. RC TISSUE=Keratinocyte; RX MEDLINE=93162043; PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [17] RP SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=9083090; RA Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., Sorg C.; RT "Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins RT of the S100 family, are secreted by activated monocytes via a novel, RT tubulin-dependent pathway."; RL J. Biol. Chem. 272:9496-9502(1997). RN [18] RP FUNCTION, AND INTERACTION WITH TUBULIN. 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., RA Roth J.; RT "MRP8 and MRP14 control microtubule reorganization during RT transendothelial migration of phagocytes."; RL Blood 104:4260-4268(2004). RN [19] RP FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15598812; DOI=10.1182/blood-2004-07-2520; RA Viemann D., Strey A., Janning A., Jurk K., Klimmek K., Vogl T., RA Hirono K., Ichida F., Foell D., Kehrel B., Gerke V., Sorg C., Roth J.; RT "Myeloid-related proteins 8 and 14 induce a specific inflammatory RT response in human microvascular endothelial cells."; RL Blood 105:2955-2962(2005). RN [20] RP FUNCTION, INHIBITION BY ZINC IONS, AND SUBUNIT. RX PubMed=16258195; DOI=10.1155/MI.2005.280; RA Nakatani Y., Yamazaki M., Chazin W.J., Yui S.; RT "Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc RT ion and its implication for apoptosis-inducing activity."; RL Mediators Inflamm. 2005:280-292(2005). RN [21] RP SUBCELLULAR LOCATION, AND INTERACTION WITH ANXA6. RX PubMed=18786929; DOI=10.1074/jbc.M803908200; RA Bode G., Lueken A., Kerkhoff C., Roth J., Ludwig S., Nacken W.; RT "Interaction between S100A8/A9 and annexin A6 is involved in the RT calcium-induced cell surface exposition of S100A8/A9."; RL J. Biol. Chem. 283:31776-31784(2008). RN [22] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [23] RP FUNCTION, AND MUTAGENESIS OF CYS-42. RX PubMed=19087201; DOI=10.1111/j.1574-695X.2008.00498.x; RA Sroussi H.Y., Koehler G.A., Agabian N., Villines D., Palefsky J.M.; RT "Substitution of methionine 63 or 83 in S100A9 and cysteine 42 in RT S100A8 abrogate the antifungal activities of S100A8/A9: potential role RT for oxidative regulation."; RL FEMS Immunol. Med. Microbiol. 55:55-61(2009). RN [24] RP FUNCTION, AND SUBUNIT. RX PubMed=19122197; DOI=10.1074/jbc.M806605200; RA Champaiboon C., Sappington K.J., Guenther B.D., Ross K.F., RA Herzberg M.C.; RT "Calprotectin S100A9 calcium-binding loops I and II are essential for RT keratinocyte resistance to bacterial invasion."; RL J. Biol. Chem. 284:7078-7090(2009). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE=20235649; PubMed=10771424; DOI=10.1107/S0907444900002833; RA Ishikawa K., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.; RT "The structure of human MRP8, a member of the S100 calcium-binding RT protein family, by MAD phasing at 1.9 A resolution."; RL Acta Crystallogr. D 56:559-566(2000). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH S100A9, AND RP SUBUBIT. RX PubMed=17553524; DOI=10.1016/j.jmb.2007.04.065; RA Korndoerfer I.P., Brueckner F., Skerra A.; RT "The crystal structure of the human (S100A8/S100A9)2 heterotetramer, RT calprotectin, illustrates how conformational changes of interacting RT alpha-helices can determine specific association of two EF-hand RT proteins."; RL J. Mol. Biol. 370:887-898(2007). CC -!- FUNCTION: Calcium-binding protein. Has antimicrobial activity CC towards bacteria and fungi. Important for resistance to invasion CC by pathogenic bacteria. Up-regulates transcription of genes that CC are under the control of NF-kappa-B. Plays a role in the CC development of endotoxic shock in response to bacterial CC lipopolysaccharide (LPS) (By similarity). Promotes tubulin CC polymerization. Promotes phagocyte migration and infiltration of CC granulocytes at sites of wounding. Plays a role as pro- CC inflammatory mediator in acute and chronic inflammation and up- CC regulates the release of IL8 and cell-surface expression of ICAM1. CC Extracellular calprotectin binds to target cells and promotes CC apoptosis. Antimicrobial and proapoptotic activity is inhibited by CC zinc ions. CC -!- SUBUNIT: Homodimer. Heterotetramer with S100A9. Component of the CC heterotetrameric calprotectin complex containing two copies each CC of S100A8 and S100A9. Interacts with AGER and with the CC heterodimeric complex formed by TLR4 and LY96. Interacts with CC CEACAM3 and tubulin filaments in a calcium-dependent manner. CC Heterotetrameric calprotectin interacts with ANXA6 and associates CC with tubulin filaments in activated monocytes. May interact with CC components of the intermediate filaments in monocytes and CC epithelial cells. CC -!- INTERACTION: CC Q38SD2:LRRK1; NbExp=1; IntAct=EBI-355281, EBI-1050422; CC Q9H8S9:MOBKL1B; NbExp=1; IntAct=EBI-355281, EBI-748229; CC O60285:NUAK1; NbExp=1; IntAct=EBI-355281, EBI-1046789; CC O75688:PPM1B; NbExp=1; IntAct=EBI-355281, EBI-1047039; CC Q15853:USF2; NbExp=1; IntAct=EBI-355281, EBI-1055994; CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, CC cytoskeleton. Cell membrane; Peripheral membrane protein. CC Note=Associates with tubulin filaments in activated monocytes. CC Targeted to the cell surface upon calcium influx. Released from CC blood leukocytes upon exposure to CSF2/GM-CSF, bacterial CC lipopolysaccharide (LPS) and during inflammatory processes. Serum CC levels are high in patients suffering from chronic inflammation. CC -!- TISSUE SPECIFICITY: Expressed by macrophages in chronic CC inflammations. Also expressed in epithelial cells constitutively CC or induced during dermatoses. CC -!- MISCELLANEOUS: Binds two calcium ions per molecule with an CC affinity similar to that of the S100 proteins. CC -!- SIMILARITY: Belongs to the S-100 family. CC -!- SIMILARITY: Contains 2 EF-hand domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00278; CAA68390.1; -; mRNA. DR EMBL; X06234; CAA29580.1; -; mRNA. DR EMBL; M21005; AAA36327.1; -; Genomic_DNA. DR EMBL; AK291328; BAF84017.1; -; mRNA. DR EMBL; CR407674; CAG28602.1; -; mRNA. DR EMBL; BT007378; AAP36042.1; -; mRNA. DR EMBL; AL591704; CAI19497.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53330.1; -; Genomic_DNA. DR EMBL; BC005928; AAH05928.1; -; mRNA. DR IPI; IPI00007047; -. DR PIR; A31848; BCHUCF. DR RefSeq; NP_002955.2; -. DR UniGene; Hs.416073; -. DR PDB; 1MR8; X-ray; 1.90 A; A/B=1-93. DR PDB; 1XK4; X-ray; 1.80 A; A/B/E/F/I/J=1-93. DR PDBsum; 1MR8; -. DR PDBsum; 1XK4; -. DR DIP; DIP:1165N; -. DR IntAct; P05109; 27. DR STRING; P05109; -. DR SWISS-2DPAGE; P05109; -. DR Aarhus/Ghent-2DPAGE; 1003; IEF. DR PMMA-2DPAGE; P05109; -. DR PeptideAtlas; P05109; -. DR PRIDE; P05109; -. DR Ensembl; ENST00000368732; ENSP00000357721; ENSG00000143546; Homo sapiens. DR Ensembl; ENST00000368733; ENSP00000357722; ENSG00000143546; Homo sapiens. DR GeneID; 6279; -. DR KEGG; hsa:6279; -. DR UCSC; uc001fbs.1; human. DR CTD; 6279; -. DR GeneCards; GC01M151629; -. DR H-InvDB; HIX0001079; -. DR HGNC; HGNC:10498; S100A8. DR HPA; CAB002791; -. DR HPA; HPA024372; -. DR MIM; 123885; gene. DR PharmGKB; PA34910; -. DR HOGENOM; P05109; -. DR HOVERGEN; P05109; -. DR OMA; KDADTWF; -. DR NextBio; 24373; -. DR ArrayExpress; P05109; -. DR Bgee; P05109; -. DR CleanEx; HS_S100A8; -. DR Genevestigator; P05109; -. DR GermOnline; ENSG00000143546; Homo sapiens. DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR018248; EF_hand. DR InterPro; IPR018247; EF_HAND_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR001751; S100_Ca_bd. DR InterPro; IPR013787; S100_Ca_bd_sub. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR Pfam; PF00036; efhand; 1. DR Pfam; PF01023; S_100; 1. DR ProDom; PD003407; CaBP_S100; 1. DR ProDom; PD000012; EF-hand; 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 3D-structure; Antimicrobial; Calcium; Cell membrane; Chemotaxis; KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Membrane; Repeat; Secreted. FT CHAIN 1 93 Protein S100-A8. FT /FTId=PRO_0000143993. FT DOMAIN 12 47 EF-hand 1. FT DOMAIN 46 81 EF-hand 2. FT CA_BIND 20 33 1; low affinity. FT CA_BIND 59 70 2; high affinity. FT MUTAGEN 42 42 C->A: Loss of antifungal activity. FT CONFLICT 80 93 VAAHKKSHEESHKE -> WQPTKKAMKKATKSS (in FT Ref. 1; CAA68390). FT HELIX 4 20 FT STRAND 22 25 FT HELIX 31 41 FT HELIX 44 47 FT HELIX 51 58 FT STRAND 63 66 FT HELIX 68 86 SQ SEQUENCE 93 AA; 10835 MW; 78F589140B9CE166 CRC64; MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE //