Full text data of DCD
DCD
(AIDD, DSEP)
[Confidence: high (present in two of the MS resources)]
Dermcidin; 3.4.-.- (Preproteolysin; Survival-promoting peptide; DCD-1; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dermcidin; 3.4.-.- (Preproteolysin; Survival-promoting peptide; DCD-1; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P81605
ID DCD_HUMAN Reviewed; 110 AA.
AC P81605; A5JHP2; A5JHP3; P58461; Q53YJ2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2002, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Dermcidin;
DE EC=3.4.-.-;
DE AltName: Full=Preproteolysin;
DE Contains:
DE RecName: Full=Survival-promoting peptide;
DE Contains:
DE RecName: Full=DCD-1;
DE Flags: Precursor;
GN Name=DCD; Synonyms=AIDD, DSEP;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 63-109,
RP AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=11694882; DOI=10.1038/ni732;
RA Schittek B., Hipfel R., Sauer B., Bauer J., Kalbacher H.,
RA Stevanovic S., Schirle M., Schroeder K., Blin N., Meier F.,
RA Rassner G., Garbe C.;
RT "Dermcidin: a novel human antibiotic peptide secreted by sweat
RT 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.,
RA Neveu M.;
RT "Overexpression of new survival/evasion peptide (DSEP) attenuates
RT retinoic 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
RT 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; 3 AND 3), PROTEOLYTIC
RP FUNCTION, AND ALTERNATIVE SPLICING.
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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
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 (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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 20-49.
RC TISSUE=Retinoblastoma;
RX PubMed=9736629;
RA Cunningham T.J., Hodge L., Speicher D., Reim D., Tyler-Polsz C.,
RA Levitt P., Eagleson K., Kennedy S., Wang Y.;
RT "Identification of a survival-promoting peptide in medium conditioned
RT by oxidatively stressed cell lines of nervous system origin.";
RL J. Neurosci. 18:7047-7060(1998).
RN [10]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP STRUCTURE BY NMR OF 63-110.
RX PubMed=20510021;
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).
CC -!- FUNCTION: DCD-1 displays antimicrobial activity thereby limiting
CC skin infection by potential pathogens in the first few hours after
CC bacterial colonization. Highly effective against E.coli,
CC E.faecalis, S.aureus and C.albicans. Optimal pH and salt
CC concentration resemble the conditions in sweat. Also exhibits
CC proteolytic activity.
CC -!- FUNCTION: Survival-promoting peptide promotes survival of neurons
CC and displays phosphatase activity. It may bind IgG.
CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC -!- COFACTOR: Manganese. Required for survival-promoting peptide.
CC -!- SUBCELLULAR LOCATION: Secreted.
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. Secreted into the sweat at a
CC concentration of 1-10 micrograms/ml.
CC -!- MASS SPECTROMETRY: Mass=4702.57; Method=Electrospray; Range=63-
CC 109; Source=PubMed:11694882;
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Smart sweat - Issue 18
CC of January 2002;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt018.shtml";
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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 RefSeq; NP_444513.1; NM_053283.2.
DR RefSeq; XP_005268684.1; XM_005268627.1.
DR UniGene; Hs.350570; -.
DR PDB; 2KSG; NMR; -; A=63-110.
DR PDB; 2YMK; X-ray; 2.49 A; A/B/C=63-110.
DR PDBsum; 2KSG; -.
DR PDBsum; 2YMK; -.
DR ProteinModelPortal; P81605; -.
DR SMR; P81605; 63-110.
DR IntAct; P81605; 10.
DR MINT; MINT-5000551; -.
DR STRING; 9606.ENSP00000293371; -.
DR TCDB; 1.C.108.1.1; the pore-forming dermcidin (dermcidin) family.
DR PhosphoSite; P81605; -.
DR DMDM; 20141302; -.
DR UCD-2DPAGE; P81605; -.
DR PaxDb; P81605; -.
DR PeptideAtlas; P81605; -.
DR PRIDE; P81605; -.
DR DNASU; 117159; -.
DR Ensembl; ENST00000293371; ENSP00000293371; ENSG00000161634.
DR Ensembl; ENST00000456047; ENSP00000406773; ENSG00000161634.
DR Ensembl; ENST00000546807; ENSP00000450415; ENSG00000161634.
DR GeneID; 117159; -.
DR KEGG; hsa:117159; -.
DR UCSC; uc001sgj.3; human.
DR CTD; 117159; -.
DR GeneCards; GC12M055038; -.
DR HGNC; HGNC:14669; DCD.
DR MIM; 606634; gene.
DR neXtProt; NX_P81605; -.
DR PharmGKB; PA27171; -.
DR eggNOG; NOG75451; -.
DR HOGENOM; HOG000280682; -.
DR HOVERGEN; HBG018946; -.
DR InParanoid; P81605; -.
DR OMA; PCHEASA; -.
DR OrthoDB; EOG7J9VSJ; -.
DR PhylomeDB; P81605; -.
DR EvolutionaryTrace; P81605; -.
DR GeneWiki; Dermcidin; -.
DR GenomeRNAi; 117159; -.
DR NextBio; 80125; -.
DR PMAP-CutDB; P81605; -.
DR PRO; PR:P81605; -.
DR Bgee; P81605; -.
DR CleanEx; HS_DCD; -.
DR Genevestigator; P81605; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028130; Dermcidin.
DR Pfam; PF15291; Dermcidin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antibiotic;
KW Antimicrobial; Complete proteome; Direct protein sequencing;
KW Fungicide; Hydrolase; Manganese; Protease; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 19
FT CHAIN 20 110 Dermcidin.
FT /FTId=PRO_0000021081.
FT PEPTIDE 20 49 Survival-promoting peptide.
FT /FTId=PRO_0000021082.
FT PROPEP 50 62
FT /FTId=PRO_0000021083.
FT PEPTIDE 63 109 DCD-1.
FT /FTId=PRO_0000021084.
FT PROPEP 110 110
FT /FTId=PRO_0000408312.
FT MOD_RES 68 68 N6-acetyllysine.
FT VAR_SEQ 33 77 PCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGA
FT KKAV -> HKQMDCLQLQKPPSETAKFLSSSTNLPRREKLV
FT PSAKPPHTRGLV (in isoform 3).
FT /FTId=VSP_043765.
FT VAR_SEQ 78 110 Missing (in isoform 3).
FT /FTId=VSP_043766.
FT VAR_SEQ 98 110 AVHDVKDVLDSVL -> GEERLVFGAPVNLTSIPLTSVSRP
FT (in isoform 2).
FT /FTId=VSP_043767.
FT HELIX 67 107
SQ SEQUENCE 110 AA; 11284 MW; 23666FBD20019465 CRC64;
MRFMTLLFLT ALAGALVCAY DPEAASAPGS GNPCHEASAA QKENAGEDPG LARQAPKPRK
QRSSLLEKGL DGAKKAVGGL GKLGKDAVED LESVGKGAVH DVKDVLDSVL
//
ID DCD_HUMAN Reviewed; 110 AA.
AC P81605; A5JHP2; A5JHP3; P58461; Q53YJ2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2002, sequence version 2.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=Dermcidin;
DE EC=3.4.-.-;
DE AltName: Full=Preproteolysin;
DE Contains:
DE RecName: Full=Survival-promoting peptide;
DE Contains:
DE RecName: Full=DCD-1;
DE Flags: Precursor;
GN Name=DCD; Synonyms=AIDD, DSEP;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 63-109,
RP AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=11694882; DOI=10.1038/ni732;
RA Schittek B., Hipfel R., Sauer B., Bauer J., Kalbacher H.,
RA Stevanovic S., Schirle M., Schroeder K., Blin N., Meier F.,
RA Rassner G., Garbe C.;
RT "Dermcidin: a novel human antibiotic peptide secreted by sweat
RT 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.,
RA Neveu M.;
RT "Overexpression of new survival/evasion peptide (DSEP) attenuates
RT retinoic 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
RT 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; 3 AND 3), PROTEOLYTIC
RP FUNCTION, AND ALTERNATIVE SPLICING.
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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
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 (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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 20-49.
RC TISSUE=Retinoblastoma;
RX PubMed=9736629;
RA Cunningham T.J., Hodge L., Speicher D., Reim D., Tyler-Polsz C.,
RA Levitt P., Eagleson K., Kennedy S., Wang Y.;
RT "Identification of a survival-promoting peptide in medium conditioned
RT by oxidatively stressed cell lines of nervous system origin.";
RL J. Neurosci. 18:7047-7060(1998).
RN [10]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally
RT verified cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP STRUCTURE BY NMR OF 63-110.
RX PubMed=20510021;
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).
CC -!- FUNCTION: DCD-1 displays antimicrobial activity thereby limiting
CC skin infection by potential pathogens in the first few hours after
CC bacterial colonization. Highly effective against E.coli,
CC E.faecalis, S.aureus and C.albicans. Optimal pH and salt
CC concentration resemble the conditions in sweat. Also exhibits
CC proteolytic activity.
CC -!- FUNCTION: Survival-promoting peptide promotes survival of neurons
CC and displays phosphatase activity. It may bind IgG.
CC -!- CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
CC -!- COFACTOR: Manganese. Required for survival-promoting peptide.
CC -!- SUBCELLULAR LOCATION: Secreted.
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. Secreted into the sweat at a
CC concentration of 1-10 micrograms/ml.
CC -!- MASS SPECTROMETRY: Mass=4702.57; Method=Electrospray; Range=63-
CC 109; Source=PubMed:11694882;
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Smart sweat - Issue 18
CC of January 2002;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt018.shtml";
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; 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 RefSeq; NP_444513.1; NM_053283.2.
DR RefSeq; XP_005268684.1; XM_005268627.1.
DR UniGene; Hs.350570; -.
DR PDB; 2KSG; NMR; -; A=63-110.
DR PDB; 2YMK; X-ray; 2.49 A; A/B/C=63-110.
DR PDBsum; 2KSG; -.
DR PDBsum; 2YMK; -.
DR ProteinModelPortal; P81605; -.
DR SMR; P81605; 63-110.
DR IntAct; P81605; 10.
DR MINT; MINT-5000551; -.
DR STRING; 9606.ENSP00000293371; -.
DR TCDB; 1.C.108.1.1; the pore-forming dermcidin (dermcidin) family.
DR PhosphoSite; P81605; -.
DR DMDM; 20141302; -.
DR UCD-2DPAGE; P81605; -.
DR PaxDb; P81605; -.
DR PeptideAtlas; P81605; -.
DR PRIDE; P81605; -.
DR DNASU; 117159; -.
DR Ensembl; ENST00000293371; ENSP00000293371; ENSG00000161634.
DR Ensembl; ENST00000456047; ENSP00000406773; ENSG00000161634.
DR Ensembl; ENST00000546807; ENSP00000450415; ENSG00000161634.
DR GeneID; 117159; -.
DR KEGG; hsa:117159; -.
DR UCSC; uc001sgj.3; human.
DR CTD; 117159; -.
DR GeneCards; GC12M055038; -.
DR HGNC; HGNC:14669; DCD.
DR MIM; 606634; gene.
DR neXtProt; NX_P81605; -.
DR PharmGKB; PA27171; -.
DR eggNOG; NOG75451; -.
DR HOGENOM; HOG000280682; -.
DR HOVERGEN; HBG018946; -.
DR InParanoid; P81605; -.
DR OMA; PCHEASA; -.
DR OrthoDB; EOG7J9VSJ; -.
DR PhylomeDB; P81605; -.
DR EvolutionaryTrace; P81605; -.
DR GeneWiki; Dermcidin; -.
DR GenomeRNAi; 117159; -.
DR NextBio; 80125; -.
DR PMAP-CutDB; P81605; -.
DR PRO; PR:P81605; -.
DR Bgee; P81605; -.
DR CleanEx; HS_DCD; -.
DR Genevestigator; P81605; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028130; Dermcidin.
DR Pfam; PF15291; Dermcidin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antibiotic;
KW Antimicrobial; Complete proteome; Direct protein sequencing;
KW Fungicide; Hydrolase; Manganese; Protease; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 19
FT CHAIN 20 110 Dermcidin.
FT /FTId=PRO_0000021081.
FT PEPTIDE 20 49 Survival-promoting peptide.
FT /FTId=PRO_0000021082.
FT PROPEP 50 62
FT /FTId=PRO_0000021083.
FT PEPTIDE 63 109 DCD-1.
FT /FTId=PRO_0000021084.
FT PROPEP 110 110
FT /FTId=PRO_0000408312.
FT MOD_RES 68 68 N6-acetyllysine.
FT VAR_SEQ 33 77 PCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGA
FT KKAV -> HKQMDCLQLQKPPSETAKFLSSSTNLPRREKLV
FT PSAKPPHTRGLV (in isoform 3).
FT /FTId=VSP_043765.
FT VAR_SEQ 78 110 Missing (in isoform 3).
FT /FTId=VSP_043766.
FT VAR_SEQ 98 110 AVHDVKDVLDSVL -> GEERLVFGAPVNLTSIPLTSVSRP
FT (in isoform 2).
FT /FTId=VSP_043767.
FT HELIX 67 107
SQ SEQUENCE 110 AA; 11284 MW; 23666FBD20019465 CRC64;
MRFMTLLFLT ALAGALVCAY DPEAASAPGS GNPCHEASAA QKENAGEDPG LARQAPKPRK
QRSSLLEKGL DGAKKAVGGL GKLGKDAVED LESVGKGAVH DVKDVLDSVL
//
MIM
606634
*RECORD*
*FIELD* NO
606634
*FIELD* TI
*606634 DERMCIDIN; DCD
*FIELD* TX
CLONING
By screening subtracted primary melanoma and benign melanocytic nevus
read moretissue cDNA libraries with cDNA arrays, Schittek et al. (2001)
identified a cDNA encoding dermcidin, or DCD. The 110-amino acid DCD
protein contains a sequence resembling cancer cachectic factor-1
(601084) and a survival-promoting peptide, Y-P30, but it has no homology
with other antimicrobial peptides. Dot blot analysis showed no
detectable expression of DCD. RT-PCR analysis detected DCD expression in
skin, melanocytic nevus, and cutaneous melanoma tissue, but not in any
other organ systems tested. In situ hybridization and immunodetection
analyses demonstrated expression of DCD in the Golgi complex of dark
mucous cells of secretory coils in dermal eccrine sweat glands,
suggesting that DCD is a secreted protein. High performance liquid
chromatography, mass spectrometry, and microsequence analysis of sweat
showed a processed 47-amino acid DCD peptide with a calculated mass of
4.7 kD, compared with the expected 9.3 kD of full-length DCD without the
signal peptide.
GENE FUNCTION
Schittek et al. (2001) found that a synthetic DCD-derived peptide,
DCD-1L, composed of 48 C-terminal amino acids of DCD had dose- and
time-dependent bactericidal and fungicidal activities in neutral or
acidic (sweat-like) buffers. The fungicidal activity occurred at a
higher but still physiologic concentration of DCD-1L compared with the
bactericidal activity. These results suggested that DCD has a role in
innate immune responses in skin.
Using serial analysis of gene expression (SAGE), Porter et al. (2003)
identified a SAGE tag that was present only in invasive breast
carcinomas and their lymph node metastases. The transcript corresponding
to this SAGE tag, DCD, encodes a secreted protein normally expressed
only in the pons of the brain and sweat glands. Further studies
demonstrated that DCD was overexpressed in approximately 10% of invasive
breast carcinomas; in some cases its overexpression was coupled with a
copy number gain at its locus (12q13.1), and its expression was
associated with advanced clinical stage and poor prognosis. Expression
of DCD in breast cancer cells promoted cell growth and survival and
reduced serum dependency. Putative high- and low-affinity receptors for
DCD were present on the cell surface of breast carcinomas and neurons of
the brain. Based on these data, Porter et al. (2003) hypothesized that
DCD may play a role in tumorigenesis by means of enhancing cell growth
and survival in a subset of breast carcinomas.
Atopic dermatitis (ATOD; see 603165) patients are prone to recurrent
bacterial and viral infections and tend to have pronounced skin
colonization with Staphylococcus aureus. Rieg et al. (2005) collected
exercise-induced sweat from the foreheads of ATOD patients and controls
who had not recently washed or been medicated and found that the levels
of DCD or DCD-derived peptides, such as DCD1 and DCD1L, were
significantly reduced in ATOD patients. Furthermore, DCD levels were
even lower in ATOD patients with a history of infectious complications
compared with ATOD patients without previous infectious complications.
Sweating in healthy subjects led to a 46% reduction of viable skin
surface bacteria, whereas sweating in ATOD patients led to only a 3%
reduction. Rieg et al. (2005) concluded that decreased expression of DCD
and DCD-derived peptides in ATOD patients correlates with clinical
infectious complications that may contribute to the propensity of ATOD
skin to have recurrent bacterial and viral infections.
GENE STRUCTURE
Schittek et al. (2001) determined that the DCD gene contains 5 exons and
is expressed as a single transcript.
MAPPING
By radiation hybrid analysis, Schittek et al. (2001) mapped the DCD gene
to chromosome 12q13. By FISH, Porter et al. (2003) mapped the DCD gene
to chromosome 12q13.1.
*FIELD* RF
1. Porter, D.; Weremowicz, S.; Chin, K.; Seth, P.; Keshaviah, A.;
Lahti-Domenici, J.; Bae, Y. K.; Monitto, C. L.; Merlos-Suarez, A.;
Chan, J.; Hulette, C. M.; Richardson, A.; Morton, C. C.; Marks, J.;
Duyao, M.; Hruban, R.; Gabrielson, E.; Gelman, R.; Polyak, K.: A
neural survival factor is a candidate oncogene in breast cancer. Proc.
Nat. Acad. Sci. 100: 10931-10936, 2003.
2. Rieg, S.; Steffen, H.; Seeber, S.; Humeny, A.; Kalbacher, H.; Dietz,
K.; Garbe, C.; Schittek, B.: Deficiency of dermcidin-derived antimicrobial
peptides in sweat of patients with atopic dermatitis correlates with
an impaired innate defense of human skin in vivo. J. Immun. 174:
8003-8010, 2005.
3. Schittek, B.; Hipfel, R.; Sauer, B.; Bauer, J.; Kalbacher, H.;
Stevanovic, S.; Schirle, M.; Schroeder, K.; Blin, N.; Meier, F.; Rassner,
G.; Garbe, C.: Dermcidin: a novel human antibiotic peptide secreted
by sweat glands. Nature Immun. 2: 1133-1137, 2001.
*FIELD* CN
Paul J. Converse - updated: 10/13/2006
Victor A. McKusick - updated: 12/8/2003
*FIELD* CD
Paul J. Converse: 1/24/2002
*FIELD* ED
mgross: 10/23/2006
terry: 10/13/2006
tkritzer: 12/10/2003
terry: 12/8/2003
mgross: 1/24/2002
*RECORD*
*FIELD* NO
606634
*FIELD* TI
*606634 DERMCIDIN; DCD
*FIELD* TX
CLONING
By screening subtracted primary melanoma and benign melanocytic nevus
read moretissue cDNA libraries with cDNA arrays, Schittek et al. (2001)
identified a cDNA encoding dermcidin, or DCD. The 110-amino acid DCD
protein contains a sequence resembling cancer cachectic factor-1
(601084) and a survival-promoting peptide, Y-P30, but it has no homology
with other antimicrobial peptides. Dot blot analysis showed no
detectable expression of DCD. RT-PCR analysis detected DCD expression in
skin, melanocytic nevus, and cutaneous melanoma tissue, but not in any
other organ systems tested. In situ hybridization and immunodetection
analyses demonstrated expression of DCD in the Golgi complex of dark
mucous cells of secretory coils in dermal eccrine sweat glands,
suggesting that DCD is a secreted protein. High performance liquid
chromatography, mass spectrometry, and microsequence analysis of sweat
showed a processed 47-amino acid DCD peptide with a calculated mass of
4.7 kD, compared with the expected 9.3 kD of full-length DCD without the
signal peptide.
GENE FUNCTION
Schittek et al. (2001) found that a synthetic DCD-derived peptide,
DCD-1L, composed of 48 C-terminal amino acids of DCD had dose- and
time-dependent bactericidal and fungicidal activities in neutral or
acidic (sweat-like) buffers. The fungicidal activity occurred at a
higher but still physiologic concentration of DCD-1L compared with the
bactericidal activity. These results suggested that DCD has a role in
innate immune responses in skin.
Using serial analysis of gene expression (SAGE), Porter et al. (2003)
identified a SAGE tag that was present only in invasive breast
carcinomas and their lymph node metastases. The transcript corresponding
to this SAGE tag, DCD, encodes a secreted protein normally expressed
only in the pons of the brain and sweat glands. Further studies
demonstrated that DCD was overexpressed in approximately 10% of invasive
breast carcinomas; in some cases its overexpression was coupled with a
copy number gain at its locus (12q13.1), and its expression was
associated with advanced clinical stage and poor prognosis. Expression
of DCD in breast cancer cells promoted cell growth and survival and
reduced serum dependency. Putative high- and low-affinity receptors for
DCD were present on the cell surface of breast carcinomas and neurons of
the brain. Based on these data, Porter et al. (2003) hypothesized that
DCD may play a role in tumorigenesis by means of enhancing cell growth
and survival in a subset of breast carcinomas.
Atopic dermatitis (ATOD; see 603165) patients are prone to recurrent
bacterial and viral infections and tend to have pronounced skin
colonization with Staphylococcus aureus. Rieg et al. (2005) collected
exercise-induced sweat from the foreheads of ATOD patients and controls
who had not recently washed or been medicated and found that the levels
of DCD or DCD-derived peptides, such as DCD1 and DCD1L, were
significantly reduced in ATOD patients. Furthermore, DCD levels were
even lower in ATOD patients with a history of infectious complications
compared with ATOD patients without previous infectious complications.
Sweating in healthy subjects led to a 46% reduction of viable skin
surface bacteria, whereas sweating in ATOD patients led to only a 3%
reduction. Rieg et al. (2005) concluded that decreased expression of DCD
and DCD-derived peptides in ATOD patients correlates with clinical
infectious complications that may contribute to the propensity of ATOD
skin to have recurrent bacterial and viral infections.
GENE STRUCTURE
Schittek et al. (2001) determined that the DCD gene contains 5 exons and
is expressed as a single transcript.
MAPPING
By radiation hybrid analysis, Schittek et al. (2001) mapped the DCD gene
to chromosome 12q13. By FISH, Porter et al. (2003) mapped the DCD gene
to chromosome 12q13.1.
*FIELD* RF
1. Porter, D.; Weremowicz, S.; Chin, K.; Seth, P.; Keshaviah, A.;
Lahti-Domenici, J.; Bae, Y. K.; Monitto, C. L.; Merlos-Suarez, A.;
Chan, J.; Hulette, C. M.; Richardson, A.; Morton, C. C.; Marks, J.;
Duyao, M.; Hruban, R.; Gabrielson, E.; Gelman, R.; Polyak, K.: A
neural survival factor is a candidate oncogene in breast cancer. Proc.
Nat. Acad. Sci. 100: 10931-10936, 2003.
2. Rieg, S.; Steffen, H.; Seeber, S.; Humeny, A.; Kalbacher, H.; Dietz,
K.; Garbe, C.; Schittek, B.: Deficiency of dermcidin-derived antimicrobial
peptides in sweat of patients with atopic dermatitis correlates with
an impaired innate defense of human skin in vivo. J. Immun. 174:
8003-8010, 2005.
3. Schittek, B.; Hipfel, R.; Sauer, B.; Bauer, J.; Kalbacher, H.;
Stevanovic, S.; Schirle, M.; Schroeder, K.; Blin, N.; Meier, F.; Rassner,
G.; Garbe, C.: Dermcidin: a novel human antibiotic peptide secreted
by sweat glands. Nature Immun. 2: 1133-1137, 2001.
*FIELD* CN
Paul J. Converse - updated: 10/13/2006
Victor A. McKusick - updated: 12/8/2003
*FIELD* CD
Paul J. Converse: 1/24/2002
*FIELD* ED
mgross: 10/23/2006
terry: 10/13/2006
tkritzer: 12/10/2003
terry: 12/8/2003
mgross: 1/24/2002