DCD_HUMAN
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 03-AUG-2022, entry version 190.
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 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 [16]
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 [17] {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:25946035,
CC 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: Specifically and constitutively expressed in
CC eccrine sweat gland cells (at protein level). Secreted into the sweat
CC at a concentration of 1-10 micrograms/ml.
CC {ECO:0000269|PubMed:11694882}.
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";
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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; 148.
DR ComplexPortal; CPX-6085; Dermcidin antimicrobial peptide complex.
DR IntAct; P81605; 59.
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 GlyGen; P81605; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P81605; -.
DR PhosphoSitePlus; P81605; -.
DR BioMuta; DCD; -.
DR DMDM; 20141302; -.
DR UCD-2DPAGE; P81605; -.
DR EPD; P81605; -.
DR jPOST; P81605; -.
DR MassIVE; P81605; -.
DR MaxQB; P81605; -.
DR PaxDb; P81605; -.
DR PeptideAtlas; P81605; -.
DR PRIDE; P81605; -.
DR ProteomicsDB; 57698; -. [P81605-1]
DR ProteomicsDB; 57699; -. [P81605-2]
DR TopDownProteomics; P81605-1; -. [P81605-1]
DR Antibodypedia; 27554; 215 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 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; 1488134at2759; -.
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 1072 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 84 other tissues.
DR Genevisible; P81605; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0046930; C:pore complex; IPI:ComplexPortal.
DR GO; GO:0005253; F:anion channel activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:ComplexPortal.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0015698; P:inorganic anion transport; IDA:UniProtKB.
DR GO; GO:0051873; P:killing by host of symbiont cells; IDA:CACAO.
DR GO; GO:0031640; P:killing of cells of another organism; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028130; Dermcidin.
DR InterPro; IPR043557; Dermcidin/Lacritin.
DR PANTHER; PTHR40711; PTHR40711; 1.
DR PANTHER; PTHR40711:SF1; PTHR40711:SF1; 1.
DR Pfam; PF15291; Dermcidin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Fungicide; Hydrolase; Manganese; Membrane;
KW Metal-binding; Protease; Reference proteome; Secreted; Signal;
KW 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 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
