P19957 (ELAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elafin

Alternative name(s):
Elastase-specific inhibitor
Short name=ESI
Peptidase inhibitor 3
Short name=PI-3
Protease inhibitor WAP3
Skin-derived antileukoproteinase
Short name=SKALP
WAP four-disulfide core domain protein 14

Gene names

Name:	PI3
Synonyms:	WAP3, WFDC14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis.
Subcellular location	Secreted.
Domain	Consists of two domains: the transglutaminase substrate domain (cementoin moiety) and the elastase inhibitor domain. The transglutaminase substrate domain serves as an anchor to localize elafin covalently to specific sites on extracellular matrix proteins.
Sequence similarities	Contains 1 WAP domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	copulation Inferred from electronic annotation. Source: InterPro
Cellular_component	proteinaceous extracellular matrix Traceable author statement Ref.3. Source: ProtInc
Molecular_function	serine-type endopeptidase inhibitor activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.2

Propeptide

23 – 60

38

PRO_0000041357

Chain

61 – 117

57

Elafin

PRO_0000041358

Regions

Repeat

29 – 54

26

SVP-1 clotting 1

Repeat

55 – 72

18

SVP-1 clotting 2

Domain

69 – 117

49

WAP

Region

29 – 72

44

2 X tandem repeats of SVP-1 like motif

Amino acid modifications

Disulfide bond

76 ↔ 105

Disulfide bond

83 ↔ 109

Disulfide bond

92 ↔ 104

Disulfide bond

98 ↔ 113

Natural variations

Natural variant

17

1

T → M.
Corresponds to variant rs17333103 [ dbSNP | Ensembl ].

VAR_052947

Natural variant

34

1

T → P.
Corresponds to variant rs2664581 [ dbSNP | Ensembl ].

VAR_024695

Experimental info

Sequence conflict

91 – 92

2

RC → CP AA sequence Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

117

Helix Strand Turn

Details...

Beta strand

65 – 69

5

Beta strand

73 – 75

3

Beta strand

81 – 84

4

Helix

95 – 97

3

Beta strand

98 – 101

4

Beta strand

103 – 106

4

Beta strand

108 – 114

7

Sequences

	Sequence		Length	Mass (Da)
	P19957 [UniParc]. Last modified December 1, 1992. Version 3. Checksum: A51D46257E5B03EF	FASTA	117	12,270
	10 20 30 40 50 60 MRASSFLIVV VFLIAGTLVL EAAVTGVPVK GQDTVKGRVP FNGQDPVKGQ VSVKGQDKVK 70 80 90 100 110 AQEPVKGPVS TKPGSCPIIL IRCAMLNPPN RCLKDTDCPG IKKCCEGSCG MACFVPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of the human elafin precursor preproelafin deduced from the nucleotide sequence of its gene and the presence of unique repetitive sequences in the prosegment." Saheki T., Ito F., Hagiwara H., Saito Y., Kuroki J., Tachibana S., Hirose S. Biochem. Biophys. Res. Commun. 185:240-245(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"SKALP/elafin: an elastase inhibitor from cultured human keratinocytes. Purification, cDNA sequence, and evidence for transglutaminase cross-linking." Molhuizen H.O.F., Alkemade H.A.C., Zeeuwen P.L.J.M., de Jongh G.J., Wieringa B., Schalkwijk J. J. Biol. Chem. 268:12028-12032(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-48 AND 85-100. Tissue: Keratinocyte.
[3]	"Characterization and gene sequence of the precursor of elafin, an elastase-specific inhibitor in bronchial secretions." Sallenave J.-M., Silva A. Am. J. Respir. Cell Mol. Biol. 8:439-445(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[8]	"Elafin: an elastase-specific inhibitor of human skin. Purification, characterization, and complete amino acid sequence." Wiedow O., Schroeder J.-M., Gregory H., Young J.A., Christophers E. J. Biol. Chem. 265:14791-14795(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 61-117. Tissue: Stratum corneum.
[9]	Erratum Wiedow O., Schroeder J.-M., Gregory H., Young J.A., Christophers E. J. Biol. Chem. 266:3356-3356(1991)
[10]	"Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor." Sallenave J.-M., Ryle A.P. Biol. Chem. Hoppe-Seyler 372:13-21(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 70-94. Tissue: Sputum.
[11]	"Isolation of elafin and elastase-specific inhibitor (ESI) from bronchial secretions. Evidence of sequence homology and immunological cross-reactivity." Sallenave J.-M., Marsden M.D., Ryle A.P. Biol. Chem. Hoppe-Seyler 373:27-33(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 61-77. Tissue: Sputum.
[12]	"Skin-derived antileukoproteinase (SKALP), an elastase inhibitor from human keratinocytes. Purification and biochemical properties." Schalkwijk J., de Roo C., de Jongh G.J. Biochim. Biophys. Acta 1096:148-154(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 85-100. Tissue: Keratinocyte.
[13]	"Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9-A resolution." Tsunemi M., Matsuura Y., Sakakibara S., Katsube Y. Biochemistry 35:11570-11576(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[14]	"Solution structure of R-elafin, a specific inhibitor of elastase." Francart C., Dauchez M., Alix A.J.P., Lippens G. J. Mol. Biol. 268:666-677(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z18538 mRNA. Translation: CAA79223.1.
D13156 Genomic DNA. Translation: BAA02441.1.
S58717 Genomic DNA. Translation: AAB26371.1.
L10343 Genomic DNA. Translation: AAA36483.1.
CR542234 mRNA. Translation: CAG47030.1.
AL049767 Genomic DNA. Translation: CAB53524.1.
CH471077 Genomic DNA. Translation: EAW75873.1.
CH471077 Genomic DNA. Translation: EAW75874.1.
BC010952 mRNA. Translation: AAH10952.1.

IPI

IPI00021434.

PIR

JH0614.

RefSeq

NP_002629.1. NM_002638.3.

UniGene

Hs.112341.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FLE	X-ray	1.90	I	61-117	[»]
2REL	NMR	-	A	61-117	[»]

ProteinModelPortal

P19957.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000243924.

Protein family/group databases

MEROPS

I17.002.

PTM databases

PhosphoSite

P19957.

Polymorphism databases

DMDM

119262.

Proteomic databases

PaxDb

P19957.

PeptideAtlas

P19957.

PRIDE

P19957.

Protocols and materials databases

DNASU

5266.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000243924; ENSP00000243924; ENSG00000124102.

GeneID

5266.

KEGG

hsa:5266.

UCSC

uc002xng.3. human.

Organism-specific databases

CTD

5266.

GeneCards

GC20P043803.

HGNC

HGNC:8947. PI3.

HPA

CAB009449.
HPA017737.

MIM

182257. gene.

neXtProt

NX_P19957.

PharmGKB

PA33283.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG72286.

HOGENOM

HOG000115819.

HOVERGEN

HBG018073.

InParanoid

P19957.

OMA

GAKKCCV.

OrthoDB

EOG4RXZ1K.

PhylomeDB

P19957.

Gene expression databases

Bgee

P19957.

CleanEx

HS_PI3.

Genevestigator

P19957.

GermOnline

ENSG00000124102. Homo sapiens.

Family and domain databases

Gene3D

4.10.75.10. 1 hit.

InterPro

IPR002098. SVP_I.
IPR019541. Trappin_transglut-bd_rpt.
IPR008197. WAP-type_4-diS_core.
[Graphical view]

Pfam

PF10511. Cementoin. 2 hits.
PF00095. WAP. 1 hit.
[Graphical view]

PRINTS

PR00003. 4DISULPHCORE.

SMART

SM00217. WAP. 1 hit.
[Graphical view]

SUPFAM

SSF57256. WAP. 1 hit.

PROSITE

PS00313. SVP_I. 2 hits.
PS51390. WAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P19957.

GenomeRNAi

5266.

NextBio

20344.

PMAP-CutDB

P19957.

SOURCE

Search...

Entry information

Entry name

ELAF_HUMAN

Accession

Primary (citable) accession number: P19957
Secondary accession number(s): E1P618, Q6FG74

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.