ID DCD_HUMAN Reviewed; 110 AA. AC P81605; A5JHP2; A5JHP3; P58461; Q53YJ2; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Dermcidin {ECO:0000303|PubMed:11694882}; DE EC=3.4.-.- {ECO:0000269|PubMed:17448443}; DE AltName: Full=Preproteolysin {ECO:0000303|Ref.3}; DE Contains: DE RecName: Full=Survival-promoting peptide {ECO:0000305|PubMed:9736629}; DE Contains: DE RecName: Full=DCD-1 {ECO:0000303|PubMed:11694882}; DE Flags: Precursor; GN Name=DCD {ECO:0000312|HGNC:HGNC:14669}; GN Synonyms=AIDD, DSEP {ECO:0000303|PubMed:9736629}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 63-109, MASS RP SPECTROMETRY, FUNCTION (DCD-1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Melanoma; RX PubMed=11694882; DOI=10.1038/ni732; RA Schittek B., Hipfel R., Sauer B., Bauer J., Kalbacher H., Stevanovic S., RA Schirle M., Schroeder K., Blin N., Meier F., Rassner G., Garbe C.; RT "Dermcidin: a novel human antibiotic peptide secreted by sweat glands."; RL Nat. Immunol. 2:1133-1137(2001). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Cunningham T.J., Jing H., Akerblom I., Morgan R., Fisher T.S., Neveu M.; RT "Overexpression of new survival/evasion peptide (DSEP) attenuates retinoic RT acid responses and protects cells."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tang X.D., Daggett H., Hoshi T.; RT "Genomic structure and chromosomal mapping of human preproteolysin gene."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Lowrie A.G., Wigmore S.J., Deans D.A.C., Fearon K.C.H., Waddell I., RA Ross J.A.; RT "Structural and functional homologies of human proteolysis inducing RT factor."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 20-41 RP AND 63-91, FUNCTION, AND CATALYTIC ACTIVITY. RC TISSUE=Placenta; RX PubMed=17448443; DOI=10.1016/j.bbrc.2007.03.112; RA Lee Motoyama J.P., Kim-Motoyama H., Kim P., Nakagama H., Miyagawa K., RA Suzuki K.; RT "Identification of dermcidin in human gestational tissue and RT characterization of its proteolytic activity."; RL Biochem. Biophys. Res. Commun. 357:828-833(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [9] RP PROTEIN SEQUENCE OF 20-61 AND 66-110, AND SUBCELLULAR LOCATION. RC TISSUE=Tear; RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179; RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., RA Suarez T., Elortza F.; RT "Human basal tear peptidome characterization by CID, HCD, and ETD followed RT by in silico and in vitro analyses for antimicrobial peptide RT identification."; RL J. Proteome Res. 14:2649-2658(2015). RN [10] RP PROTEIN SEQUENCE OF 20-49, FUNCTION (SURVIVAL-PROMOTING PEPTIDE), COFACTOR RP (SURVIVAL-PROMOTING PEPTIDE), AND SUBCELLULAR LOCATION (SURVIVAL-PROMOTING RP PEPTIDE). RC TISSUE=Retinoblastoma; RX PubMed=9736629; DOI=10.1523/jneurosci.18-18-07047.1998; RA Cunningham T.J., Hodge L., Speicher D., Reim D., Tyler-Polsz C., Levitt P., RA Eagleson K., Kennedy S., Wang Y.; RT "Identification of a survival-promoting peptide in medium conditioned by RT oxidatively stressed cell lines of nervous system origin."; RL J. Neurosci. 18:7047-7060(1998). RN [11] RP PROTEIN SEQUENCE OF 20-34, AND SUBCELLULAR LOCATION. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-30. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-30 AND RP SER-38. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [18] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-30. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). RN [19] RP STRUCTURE BY NMR OF 63-110. RX PubMed=20510021; DOI=10.5483/bmbrep.2010.43.5.362; RA Jung H.H., Yang S.T., Sim J.Y., Lee S., Lee J.Y., Kim H.H., Shin S.Y., RA Kim J.I.; RT "Analysis of the solution structure of the human antibiotic peptide RT dermcidin and its interaction with phospholipid vesicles."; RL BMB Rep. 43:362-368(2010). RN [20] {ECO:0007744|PDB:2YMK} RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 63-110 IN COMPLEX WITH ZINC, RP FUNCTION (DCD-1), COFACTOR (DCD-1), SUBUNIT (DCD-1), SUBCELLULAR LOCATION RP (DCD-1), TOPOLOGY (DCD-1), AND MUTAGENESIS OF HIS-100. RX PubMed=23426625; DOI=10.1073/pnas.1214739110; RA Song C., Weichbrodt C., Salnikov E.S., Dynowski M., Forsberg B.O., RA Bechinger B., Steinem C., de Groot B.L., Zachariae U., Zeth K.; RT "Crystal structure and functional mechanism of a human antimicrobial RT membrane channel."; RL Proc. Natl. Acad. Sci. U.S.A. 110:4586-4591(2013). CC -!- FUNCTION: [DCD-1]: Found in sweat, has an antimicrobial activity during CC early bacterial colonization (PubMed:11694882, PubMed:23426625). The CC secreted peptide assembles into homohexameric complexes that can CC associate with and also insert into pathogen membranes CC (PubMed:23426625). Once inserted in bacteria membranes forms anion CC channels probably altering the transmembrane potential essential for CC bacterial survival (PubMed:23426625). Highly effective against E.coli, CC E.faecalis, S.aureus and C.albicans (PubMed:11694882). Optimal pH and CC salt concentration resemble the conditions in sweat (PubMed:11694882). CC Also exhibits proteolytic activity, cleaving on the C-terminal side of CC Arg and, to a lesser extent, Lys residues (PubMed:17448443). CC {ECO:0000269|PubMed:11694882, ECO:0000269|PubMed:17448443, CC ECO:0000269|PubMed:23426625}. CC -!- FUNCTION: [Survival-promoting peptide]: Promotes survival of neurons CC and displays phosphatase activity (PubMed:9736629). It may bind IgG CC (PubMed:9736629). {ECO:0000269|PubMed:9736629}. CC -!- COFACTOR: [Survival-promoting peptide]: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:9736629}; CC -!- COFACTOR: [DCD-1]: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:23426625}; CC -!- SUBUNIT: [DCD-1]: Homohexamer. {ECO:0000269|PubMed:23426625}. CC -!- INTERACTION: CC P81605; Q92624: APPBP2; NbExp=3; IntAct=EBI-395625, EBI-743771; CC P81605; Q12797-6: ASPH; NbExp=3; IntAct=EBI-395625, EBI-12092171; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11694882, CC ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:36213313, CC ECO:0000269|PubMed:37453717, ECO:0000269|PubMed:9736629}. CC -!- SUBCELLULAR LOCATION: [Survival-promoting peptide]: Secreted CC {ECO:0000269|PubMed:9736629}. CC -!- SUBCELLULAR LOCATION: [DCD-1]: Secreted {ECO:0000305|PubMed:23426625}. CC Membrane {ECO:0000269|PubMed:23426625}; Peripheral membrane protein CC {ECO:0000269|PubMed:23426625}. Membrane {ECO:0000269|PubMed:23426625}; CC Single-pass membrane protein {ECO:0000269|PubMed:23426625}. Note=The CC secreted peptide assembles into homohexameric complexes that can CC probably associate with pathogen membranes and also insert into these CC membranes where they behave as channels. {ECO:0000269|PubMed:23426625}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P81605-1; Sequence=Displayed; CC Name=2; CC IsoId=P81605-2; Sequence=VSP_043767; CC Name=3; CC IsoId=P81605-3; Sequence=VSP_043765, VSP_043766; CC -!- TISSUE SPECIFICITY: Detected in urine (at protein level) CC (PubMed:25326458, PubMed:36213313, PubMed:37453717). Constitutively CC expressed in eccrine sweat gland cells (at protein level). Secreted CC into the sweat at a concentration of 1-10 micrograms/ml. CC {ECO:0000269|PubMed:11694882, ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. CC -!- MASS SPECTROMETRY: [DCD-1]: Mass=4702.57; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:11694882}; CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Smart sweat - Issue 18 of CC January 2002; CC URL="https://web.expasy.org/spotlight/back_issues/018"; 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; AF144011; AAL18349.1; -; mRNA. DR EMBL; AY044239; AAK94785.1; -; Genomic_DNA. DR EMBL; AF418981; AAL25801.1; -; Genomic_DNA. DR EMBL; AY590150; AAS99907.1; -; mRNA. DR EMBL; EF503687; ABQ53649.1; -; mRNA. DR EMBL; EF503688; ABQ53650.1; -; mRNA. DR EMBL; EF503689; ABQ53651.1; -; mRNA. DR EMBL; AC079310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96794.1; -; Genomic_DNA. DR EMBL; BC062682; AAH62682.1; -; mRNA. DR EMBL; BC069108; AAH69108.1; -; mRNA. DR CCDS; CCDS73478.1; -. [P81605-2] DR CCDS; CCDS8884.1; -. [P81605-1] DR RefSeq; NP_001287783.1; NM_001300854.1. [P81605-2] DR RefSeq; NP_444513.1; NM_053283.3. [P81605-1] DR PDB; 2KSG; NMR; -; A=63-110. DR PDB; 2NDK; NMR; -; A=63-110. DR PDB; 2YMK; X-ray; 2.49 A; A/B/C=63-110. DR PDB; 6SHK; X-ray; 1.99 A; A=63-110. DR PDBsum; 2KSG; -. DR PDBsum; 2NDK; -. DR PDBsum; 2YMK; -. DR PDBsum; 6SHK; -. DR AlphaFoldDB; P81605; -. DR BMRB; P81605; -. DR SMR; P81605; -. DR BioGRID; 125564; 195. DR ComplexPortal; CPX-6085; Dermcidin antimicrobial peptide complex. DR IntAct; P81605; 75. DR MINT; P81605; -. DR STRING; 9606.ENSP00000406773; -. DR ChEMBL; CHEMBL4523267; -. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR TCDB; 1.C.108.1.1; the pore-forming dermcidin (dermcidin) family. DR GlyCosmos; P81605; 1 site, 1 glycan. DR GlyGen; P81605; 4 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P81605; -. DR PhosphoSitePlus; P81605; -. DR SwissPalm; P81605; -. DR BioMuta; DCD; -. DR DMDM; 20141302; -. DR EPD; P81605; -. DR jPOST; P81605; -. DR MassIVE; P81605; -. DR MaxQB; P81605; -. DR PaxDb; 9606-ENSP00000406773; -. DR PeptideAtlas; P81605; -. DR ProteomicsDB; 57698; -. [P81605-1] DR ProteomicsDB; 57699; -. [P81605-2] DR TopDownProteomics; P81605-1; -. [P81605-1] DR Antibodypedia; 27554; 240 antibodies from 28 providers. DR DNASU; 117159; -. DR Ensembl; ENST00000293371.11; ENSP00000293371.6; ENSG00000161634.12. [P81605-1] DR Ensembl; ENST00000456047.2; ENSP00000406773.2; ENSG00000161634.12. [P81605-2] DR Ensembl; ENST00000546807.5; ENSP00000450415.1; ENSG00000161634.12. [P81605-3] DR GeneID; 117159; -. DR KEGG; hsa:117159; -. DR MANE-Select; ENST00000293371.11; ENSP00000293371.6; NM_053283.4; NP_444513.1. DR UCSC; uc001sgj.4; human. [P81605-1] DR AGR; HGNC:14669; -. DR CTD; 117159; -. DR DisGeNET; 117159; -. DR GeneCards; DCD; -. DR HGNC; HGNC:14669; DCD. DR HPA; ENSG00000161634; Tissue enriched (skin). DR MIM; 606634; gene. DR neXtProt; NX_P81605; -. DR OpenTargets; ENSG00000161634; -. DR PharmGKB; PA27171; -. DR VEuPathDB; HostDB:ENSG00000161634; -. DR eggNOG; ENOG502RVUN; Eukaryota. DR GeneTree; ENSGT00940000163391; -. DR HOGENOM; CLU_2060627_0_0_1; -. DR InParanoid; P81605; -. DR OMA; EWVLGAP; -. DR OrthoDB; 4739799at2759; -. DR PhylomeDB; P81605; -. DR TreeFam; TF340896; -. DR PathwayCommons; P81605; -. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR SignaLink; P81605; -. DR BioGRID-ORCS; 117159; 13 hits in 1150 CRISPR screens. DR EvolutionaryTrace; P81605; -. DR GeneWiki; Dermcidin; -. DR GenomeRNAi; 117159; -. DR Pharos; P81605; Tbio. DR PRO; PR:P81605; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P81605; Protein. DR Bgee; ENSG00000161634; Expressed in upper leg skin and 85 other cell types or tissues. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008289; F:lipid binding; EXP:DisProt. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005216; F:monoatomic ion channel activity; IDA:DisProt. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IDA:DisProt. DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW. DR GO; GO:0051873; P:killing by host of symbiont cells; IDA:CACAO. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 6.10.140.580; -; 1. DR InterPro; IPR028130; Dermcidin. DR InterPro; IPR043557; Dermcidin/Lacritin. DR PANTHER; PTHR40711:SF1; DERMCIDIN; 1. DR PANTHER; PTHR40711; DERMCIDIN-RELATED; 1. DR Pfam; PF15291; Dermcidin; 1. DR UCD-2DPAGE; P81605; -. DR Genevisible; P81605; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Antibiotic; Antimicrobial; KW Direct protein sequencing; Fungicide; Glycoprotein; Hydrolase; Manganese; KW Membrane; Metal-binding; Protease; Proteoglycan; Reference proteome; KW Secreted; Signal; Transmembrane; Transmembrane helix; Zinc. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:17448443, ECO:0000269|PubMed:25946035, FT ECO:0000269|PubMed:9736629" FT CHAIN 20..110 FT /note="Dermcidin" FT /evidence="ECO:0000269|PubMed:11694882, FT ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:17448443, FT ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:9736629" FT /id="PRO_0000021081" FT PEPTIDE 20..49 FT /note="Survival-promoting peptide" FT /evidence="ECO:0000269|PubMed:9736629" FT /id="PRO_0000021082" FT PROPEP 50..62 FT /evidence="ECO:0000269|PubMed:11694882" FT /id="PRO_0000021083" FT PEPTIDE 63..109 FT /note="DCD-1" FT /evidence="ECO:0000269|PubMed:11694882, FT ECO:0000269|PubMed:17448443" FT /id="PRO_0000021084" FT PROPEP 110 FT /evidence="ECO:0000269|PubMed:11694882, FT ECO:0000269|PubMed:25946035" FT /id="PRO_0000408312" FT TRANSMEM 64..108 FT /note="Helical" FT /evidence="ECO:0000305|PubMed:23426625" FT REGION 24..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural; ligand shared between 2 chains of FT the homohexamer" FT /note="in chain A" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural; ligand shared between 2 chains of FT the homohexamer" FT /note="in chain A" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="structural" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural; ligand shared between 2 chains of FT the homohexamer" FT /note="in chain B" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural; ligand shared between 2 chains of FT the homohexamer" FT /note="in chain B" FT /evidence="ECO:0000269|PubMed:23426625, FT ECO:0007744|PDB:2YMK" FT MOD_RES 68 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CARBOHYD 30 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717" FT CARBOHYD 38 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:36213313" FT VAR_SEQ 33..77 FT /note="PCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAV -> HKQ FT MDCLQLQKPPSETAKFLSSSTNLPRREKLVPSAKPPHTRGLV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17448443" FT /id="VSP_043765" FT VAR_SEQ 78..110 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17448443" FT /id="VSP_043766" FT VAR_SEQ 98..110 FT /note="AVHDVKDVLDSVL -> GEERLVFGAPVNLTSIPLTSVSRP (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_043767" FT MUTAGEN 100 FT /note="H->A: Loss of anion channel activity." FT /evidence="ECO:0000269|PubMed:23426625" FT HELIX 65..105 FT /evidence="ECO:0007829|PDB:6SHK" SQ SEQUENCE 110 AA; 11284 MW; 23666FBD20019465 CRC64; MRFMTLLFLT ALAGALVCAY DPEAASAPGS GNPCHEASAA QKENAGEDPG LARQAPKPRK QRSSLLEKGL DGAKKAVGGL GKLGKDAVED LESVGKGAVH DVKDVLDSVL //