Q9NQ38 (ISK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine protease inhibitor Kazal-type 5

Alternative name(s):
Lympho-epithelial Kazal-type-related inhibitor
Short name=LEKTI

Cleaved into the following 2 chains:

1. Hemofiltrate peptide HF6478
2. Hemofiltrate peptide HF7665

Gene names

Name:

SPINK5

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	1064 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	Serine protease inhibitor, probably important for the anti-inflammatory and/or antimicrobial protection of mucous epithelia. Contribute to the integrity and protective barrier function of the skin by regulating the activity of defense-activating and desquamation-involved proteases. Inhibits KLK5, it's major target, in a pH-dependent manner. Inhibits KLK7, KLK14 CASP14, and trypsin. Ref.1 Ref.7 Ref.8
Subcellular location	Secreted.
Tissue specificity	Highly expressed in the thymus and stratum corneum. Also found in the oral mucosa, parathyroid gland, Bartholin's glands, tonsils, and vaginal epithelium. Very low levels are detected in lung, kidney, and prostate. Ref.1
Domain	Contains at least one active inhibitory domain for trypsin (domain 6).
Post-translational modification	Proteolytically processed by furin in individual domains (D1, D5, D6, D8 through D11, and D9 through D15) exhibiting various inhibitory potentials for multiple proteases.
Involvement in disease	Netherton syndrome (NETH) [MIM:256500]: An autosomal recessive congenital ichthyosis associated with hair shaft abnormalities and anomalies of the immune system. Typical features are ichthyosis linearis circumflexa, ichthyosiform erythroderma, trichorrhexis invaginata (bamboo hair), atopic dermatitis, and hayfever. High postnatal mortality is due to failure to thrive, infections and hypernatremic dehydration. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2
Sequence similarities	Contains 15 Kazal-like domains.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ichthyosis
Domain	Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anagen Traceable author statement PubMed 12915442. Source: UniProtKB epithelial cell differentiation Traceable author statement PubMed 12915442. Source: UniProtKB extracellular matrix organization Traceable author statement PubMed 15680911. Source: UniProtKB hair cell differentiation Traceable author statement PubMed 12915442. Source: UniProtKB negative regulation of angiogenesis Traceable author statement PubMed 15680911. Source: UniProtKB negative regulation of immune response Traceable author statement PubMed 12915442. Source: UniProtKB negative regulation of proteolysis Inferred from electronic annotation. Source: Compara regulation of T cell differentiation Traceable author statement PubMed 12915442. Source: UniProtKB regulation of cell adhesion Inferred from electronic annotation. Source: Compara
Cellular_component	cell cortex Inferred from direct assay PubMed 12915442. Source: UniProtKB cytosol Inferred from direct assay PubMed 15680911. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay PubMed 15680911. Source: UniProtKB epidermal lamellar body Inferred from direct assay PubMed 15675955. Source: UniProtKB extracellular region Inferred from direct assay PubMed 15680911. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 15680911. Source: UniProtKB
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from direct assay Ref.1PubMed 15680911. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform f-l (identifier: Q9NQ38-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform short (identifier: Q9NQ38-2)

The sequence of this isoform differs from the canonical sequence as follows:
     914-916: DEC → VIY
     917-1064: Missing.

Isoform long (identifier: Q9NQ38-3)

The sequence of this isoform differs from the canonical sequence as follows:
     914-914: D → DQCRQVQNEAEDAKFRQPGRSLASVARMSTD

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 1064

1042

Serine protease inhibitor Kazal-type 5

PRO_0000016572

Peptide

23 – 77

55

Hemofiltrate peptide HF6478

PRO_0000016573

Peptide

356 – 423

68

Hemofiltrate peptide HF7665

PRO_0000016574

Regions

Domain

28 – 66

39

Kazal-like 1; atypical

Domain

91 – 153

63

Kazal-like 2

Domain

155 – 216

62

Kazal-like 3

Domain

219 – 285

67

Kazal-like 4

Domain

291 – 352

62

Kazal-like 5

Domain

361 – 423

63

Kazal-like 6

Domain

431 – 489

59

Kazal-like 7

Domain

490 – 551

62

Kazal-like 8

Domain

561 – 622

62

Kazal-like 9

Domain

626 – 688

63

Kazal-like 10

Domain

701 – 757

57

Kazal-like 11

Domain

768 – 830

63

Kazal-like 12

Domain

843 – 905

63

Kazal-like 13

Domain

910 – 971

62

Kazal-like 14

Domain

987 – 1048

62

Kazal-like 15

Sites

Site

46 – 47

2

Reactive bond Potential

Amino acid modifications

Disulfide bond

30 ↔ 66

Disulfide bond

44 ↔ 63

Disulfide bond

97 ↔ 133

By similarity

Disulfide bond

111 ↔ 130

By similarity

Disulfide bond

119 ↔ 151

By similarity

Disulfide bond

161 ↔ 197

By similarity

Disulfide bond

175 ↔ 194

By similarity

Disulfide bond

225 ↔ 261

By similarity

Disulfide bond

239 ↔ 258

By similarity

Disulfide bond

297 ↔ 333

By similarity

Disulfide bond

311 ↔ 330

By similarity

Disulfide bond

367 ↔ 403

Disulfide bond

381 ↔ 400

Disulfide bond

437 ↔ 473

By similarity

Disulfide bond

451 ↔ 470

By similarity

Disulfide bond

496 ↔ 532

By similarity

Disulfide bond

510 ↔ 529

By similarity

Disulfide bond

567 ↔ 603

By similarity

Disulfide bond

581 ↔ 600

By similarity

Disulfide bond

632 ↔ 668

By similarity

Disulfide bond

646 ↔ 665

By similarity

Disulfide bond

707 ↔ 743

By similarity

Disulfide bond

721 ↔ 740

By similarity

Disulfide bond

774 ↔ 810

By similarity

Disulfide bond

788 ↔ 807

By similarity

Disulfide bond

849 ↔ 885

By similarity

Disulfide bond

863 ↔ 882

By similarity

Disulfide bond

916 ↔ 952

By similarity

Disulfide bond

930 ↔ 949

By similarity

Disulfide bond

993 ↔ 1028

Disulfide bond

1006 ↔ 1025

Disulfide bond

1014 ↔ 1046

Natural variations

Alternative sequence

914 – 916

3

DEC → VIY in isoform short.

VSP_040019

Alternative sequence

914

1

D → DQCRQVQNEAEDAKFRQPGR SLASVARMSTD in isoform long.

VSP_040020

Alternative sequence

917 – 1064

148

Missing in isoform short.

VSP_040021

Natural variant

267

1

Q → R. Ref.1 Ref.2 Ref.3
Corresponds to variant rs6892205 [ dbSNP | Ensembl ].

VAR_047115

Natural variant

335

1

A → V. Ref.1 Ref.3
Corresponds to variant rs34482796 [ dbSNP | Ensembl ].

VAR_061337

Natural variant

368

1

S → N. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2303063 [ dbSNP | Ensembl ].

VAR_047116

Natural variant

386

1

D → N.
Corresponds to variant rs2303064 [ dbSNP | Ensembl ].

VAR_047117

Natural variant

395

1

V → M.
Corresponds to variant rs17775319 [ dbSNP | Ensembl ].

VAR_047118

Natural variant

420

1

K → E. Ref.1 Ref.3 Ref.11
Corresponds to variant rs2303067 [ dbSNP | Ensembl ].

VAR_015537

Natural variant

441

1

R → H.
Corresponds to variant rs34393923 [ dbSNP | Ensembl ].

VAR_047119

Natural variant

588

1

I → M.
Corresponds to variant rs35877540 [ dbSNP | Ensembl ].

VAR_047120

Natural variant

711

1

R → Q. Ref.1 Ref.3
Corresponds to variant rs3777134 [ dbSNP | Ensembl ].

VAR_047121

Natural variant

825

1

E → D.
Corresponds to variant rs2303070 [ dbSNP | Ensembl ].

VAR_047122

Natural variant

887

1

S → R.
Corresponds to variant rs28408445 [ dbSNP | Ensembl ].

VAR_047123

Natural variant

969

1

K → E.
Corresponds to variant rs3188691 [ dbSNP | Ensembl ].

VAR_047124

Natural variant

972

1

H → R.
Corresponds to variant rs17705005 [ dbSNP | Ensembl ].

VAR_047125

Experimental info

Sequence conflict

19 – 27

9

DAASKNEDQ → GQCEKDSLS in CAB96877. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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.

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.

.

.

.

.

1064

Helix Strand Turn

Details...

Turn

25 – 27

3

Helix

33 – 36

4

Beta strand

37 – 40

4

Helix

48 – 52

5

Helix

54 – 76

23

Helix

363 – 366

4

Helix

367 – 370

4

Turn

371 – 373

3

Beta strand

375 – 377

3

Helix

399 – 413

15

Helix

990 – 993

4

Turn

1000 – 1002

3

Beta strand

1013 – 1015

3

Turn

1016 – 1018

3

Beta strand

1019 – 1024

6

Helix

1025 – 1034

10

Beta strand

1040 – 1045

6

Helix

1047 – 1049

3

Helix

1055 – 1058

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform f-l [UniParc]. Last modified November 4, 2008. Version 2. Checksum: 6CBEF39BB9E6D75D	FASTA	1,064	120,714
	10 20 30 40 50 60 MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF FQSLDGIMFI 70 80 90 100 110 120 NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF KKGERDGDFI CPDYYEAVCG 130 140 150 160 170 180 TDGKTYDNRC ALCAENAKTG SQIGVKSEGE CKSSNPEQDV CSAFRPFVRD GRLGCTREND 190 200 210 220 230 240 PVLGPDGKTH GNKCAMCAEL FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT 250 260 270 280 290 300 RESDPVRGPD GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY 310 320 330 340 350 360 QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR ARNKRESGKA 370 380 390 400 410 420 TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC SMCEVFFQAE EEEKKKKEGK 430 440 450 460 470 480 SRNKRQSKST ASFEELCSEY RKSRKNGRLF CTRENDPIQG PDGKMHGNTC SMCEAFFQQE 490 500 510 520 530 540 ERARAKAKRE AAKEICSEFR DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE 550 560 570 580 590 600 EEKKNDKEEK GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC 610 620 630 640 650 660 SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN DPVRGPDGKT 670 680 690 700 710 720 HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG GNTQDECAEY REQMKNGRLS 730 740 750 760 770 780 CTRESDPVRD ADGKSYNNQC TMCKAKLERE AERKNEYSRS RSNGTGSESG KDTCDEFRSQ 790 800 810 820 830 840 MKNGKLICTR ESDPVRGPDG KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE 850 860 870 880 890 900 RSNDKEDLCR EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD 910 920 930 940 950 960 EEKSSSKPSN NAKDECSEFR NYIRNNELIC PRENDPVHGA DGKFYTNKCY MCRAVFLTEA 970 980 990 1000 1010 1020 LERAKLQEKP SHVRASQEED SPDSFSSLDS EMCKDYRVLP RIGYLCPKDL KPVCGDDGQT 1030 1040 1050 1060 YNNPCMLCHE NLIRQTNTHI RSTGKCEESS TPGTTAASMP PSDE
	Isoform short [UniParc]. Checksum: 82A029D102BD8C26	FASTA	916	104,017
	10 20 30 40 50 60 MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF FQSLDGIMFI 70 80 90 100 110 120 NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF KKGERDGDFI CPDYYEAVCG 130 140 150 160 170 180 TDGKTYDNRC ALCAENAKTG SQIGVKSEGE CKSSNPEQDV CSAFRPFVRD GRLGCTREND 190 200 210 220 230 240 PVLGPDGKTH GNKCAMCAEL FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT 250 260 270 280 290 300 RESDPVRGPD GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY 310 320 330 340 350 360 QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR ARNKRESGKA 370 380 390 400 410 420 TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC SMCEVFFQAE EEEKKKKEGK 430 440 450 460 470 480 SRNKRQSKST ASFEELCSEY RKSRKNGRLF CTRENDPIQG PDGKMHGNTC SMCEAFFQQE 490 500 510 520 530 540 ERARAKAKRE AAKEICSEFR DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE 550 560 570 580 590 600 EEKKNDKEEK GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC 610 620 630 640 650 660 SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN DPVRGPDGKT 670 680 690 700 710 720 HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG GNTQDECAEY REQMKNGRLS 730 740 750 760 770 780 CTRESDPVRD ADGKSYNNQC TMCKAKLERE AERKNEYSRS RSNGTGSESG KDTCDEFRSQ 790 800 810 820 830 840 MKNGKLICTR ESDPVRGPDG KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE 850 860 870 880 890 900 RSNDKEDLCR EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD 910 EEKSSSKPSN NAKVIY
	Isoform long [UniParc]. Checksum: 8EF0D8DE3A62227A	FASTA	1,094	124,076
	10 20 30 40 50 60 MKIATVSVLL PLALCLIQDA ASKNEDQEMC HEFQAFMKNG KLFCPQDKKF FQSLDGIMFI 70 80 90 100 110 120 NKCATCKMIL EKEAKSQKRA RHLARAPKAT APTELNCDDF KKGERDGDFI CPDYYEAVCG 130 140 150 160 170 180 TDGKTYDNRC ALCAENAKTG SQIGVKSEGE CKSSNPEQDV CSAFRPFVRD GRLGCTREND 190 200 210 220 230 240 PVLGPDGKTH GNKCAMCAEL FLKEAENAKR EGETRIRRNA EKDFCKEYEK QVRNGRLFCT 250 260 270 280 290 300 RESDPVRGPD GRMHGNKCAL CAEIFKQRFS EENSKTDQNL GKAEEKTKVK REIVKLCSQY 310 320 330 340 350 360 QNQAKNGILF CTRENDPIRG PDGKMHGNLC SMCQAYFQAE NEEKKKAEAR ARNKRESGKA 370 380 390 400 410 420 TSYAELCSEY RKLVRNGKLA CTRENDPIQG PDGKVHGNTC SMCEVFFQAE EEEKKKKEGK 430 440 450 460 470 480 SRNKRQSKST ASFEELCSEY RKSRKNGRLF CTRENDPIQG PDGKMHGNTC SMCEAFFQQE 490 500 510 520 530 540 ERARAKAKRE AAKEICSEFR DQVRNGTLIC TREHNPVRGP DGKMHGNKCA MCASVFKLEE 550 560 570 580 590 600 EEKKNDKEEK GKVEAEKVKR EAVQELCSEY RHYVRNGRLP CTRENDPIEG LDGKIHGNTC 610 620 630 640 650 660 SMCEAFFQQE AKEKERAEPR AKVKREAEKE TCDEFRRLLQ NGKLFCTREN DPVRGPDGKT 670 680 690 700 710 720 HGNKCAMCKA VFQKENEERK RKEEEDQRNA AGHGSSGGGG GNTQDECAEY REQMKNGRLS 730 740 750 760 770 780 CTRESDPVRD ADGKSYNNQC TMCKAKLERE AERKNEYSRS RSNGTGSESG KDTCDEFRSQ 790 800 810 820 830 840 MKNGKLICTR ESDPVRGPDG KTHGNKCTMC KEKLEREAAE KKKKEDEDRS NTGERSNTGE 850 860 870 880 890 900 RSNDKEDLCR EFRSMQRNGK LICTRENNPV RGPYGKMHIN KCAMCQSIFD REANERKKKD 910 920 930 940 950 960 EEKSSSKPSN NAKDQCRQVQ NEAEDAKFRQ PGRSLASVAR MSTDECSEFR NYIRNNELIC 970 980 990 1000 1010 1020 PRENDPVHGA DGKFYTNKCY MCRAVFLTEA LERAKLQEKP SHVRASQEED SPDSFSSLDS 1030 1040 1050 1060 1070 1080 EMCKDYRVLP RIGYLCPKDL KPVCGDDGQT YNNPCMLCHE NLIRQTNTHI RSTGKCEESS 1090 TPGTTAASMP PSDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"LEKTI, a novel 15-domain type of human serine proteinase inhibitor." Maegert H.-J., Staendker L., Kreutzmann P., Zucht H.-D., Reinecke M., Sommerhoff C.P., Fritz H., Forssmann W.-G. J. Biol. Chem. 274:21499-21502(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS F-L), PARTIAL PROTEIN SEQUENCE, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711, FUNCTION, TISSUE SPECIFICITY. Tissue: Epithelium.
[2]	"Mutations in SPINK5, encoding a serine protease inhibitor, cause Netherton syndrome." Chavanas S., Bodemer C., Rochat A., Hamel-Teillac D., Ali M., Irvine A.D., Bonafe J.-L., Wilkinson J., Taieb A., Barrandon Y., Harper J.I., de Prost Y., Hovnanian A. Nat. Genet. 25:141-142(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NETHERTON SYNDROME, VARIANTS ARG-267 AND ASN-368.
[3]	"SPINK5, the defective gene in netherton syndrome, encodes multiple LEKTI isoforms derived from alternative pre-mRNA processing." Tartaglia-Polcini A., Bonnart C., Micheloni A., Cianfarani F., Andre A., Zambruno G., Hovnanian A., D'Alessio M. J. Invest. Dermatol. 126:315-324(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT; F-L AND LONG), ALTERNATIVE SPLICING, VARIANTS ARG-267; VAL-335; ASN-368; GLU-420 AND GLN-711. Tissue: Keratinocyte.
[4]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The spectrum of pathogenic mutations in SPINK5 in 19 families with Netherton syndrome: implications for mutation detection and first case of prenatal diagnosis." Sprecher E., Chavanas S., DiGiovanna J.J., Amin S., Nielsen K., Prendiville J.S., Silverman R., Esterly N.B., Spraker M.K., Guelig E., de Luna M.L., Williams M.L., Buehler B., Siegfried E.C., Van Maldergem L., Pfendner E., Bale S.J., Uitto J., Hovnanian A., Richard G. J. Invest. Dermatol. 117:179-187(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-222 AND 266-294.
[6]	"Purification and partial amino acid sequence of proteins from human epidermal keratinocyte conditioned medium." Ahmed A., Kandola P., Ziada G., Parenteau N. J. Protein Chem. 20:273-278(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 490-507. Tissue: Foreskin keratinocyte.
[7]	"LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction." Deraison C., Bonnart C., Lopez F., Besson C., Robinson R., Jayakumar A., Wagberg F., Brattsand M., Hachem J.P., Leonardsson G., Hovnanian A. Mol. Biol. Cell 18:3607-3619(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE BY FURIN, INHIBITION OF KLK5; KLK7 AND KLK14.
[8]	"New role for LEKTI in skin barrier formation: label-free quantitative proteomic identification of caspase 14 as a novel target for the protease inhibitor LEKTI." Bennett K., Callard R., Heywood W., Harper J., Jayakumar A., Clayman G.L., Di W.L., Mills K. J. Proteome Res. 9:4289-4294(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INHIBITION OF CASP14.
[9]	"Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI." Lauber T., Schulz A., Schweimer K., Adermann K., Marx U.C. J. Mol. Biol. 328:205-219(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 23-77 AND 356-423.
[10]	"The solution structure of a chimeric LEKTI domain reveals a chameleon sequence." Tidow H., Lauber T., Vitzithum K., Sommerhoff C.P., Rosch P., Marx U.C. Biochemistry 43:11238-11247(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 989-1064.
[11]	"Gene polymorphism in Netherton and common atopic disease." Walley A.J., Chavanas S., Moffatt M.F., Esnouf R.M., Ubhi B., Lawrence R., Wong K., Abecasis G.R., Jones E.Y., Harper J.I., Hovnanian A., Cookson W.O.C.M. Nat. Genet. 29:175-178(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLU-420.
+	Additional computationally mapped references.

Web resources

SPINK5base

SPINK5 mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ228139 mRNA. Translation: CAB40839.1.
AJ391230 , AJ270944, AJ391231, AJ391232, AJ391233, AJ391234, AJ391235, AJ276579, AJ391236, AJ276580, AJ391237, AJ391238, AJ391239, AJ391240, AJ391241, AJ276578, AJ391242, AJ391243, AJ391244, AJ391245, AJ391246, AJ391247, AJ391248, AJ391249, AJ391250, AJ391251, AJ391252, AJ391253, AJ391254, AJ276577 Genomic DNA. Translation: CAB96877.1.
DQ149927 mRNA. Translation: ABA06534.1.
DQ149928 mRNA. Translation: ABA06535.1.
DQ149929 mRNA. Translation: ABA06536.1.
AC008722 Genomic DNA. No translation available.
AC116334 Genomic DNA. No translation available.
AF295784 Genomic DNA. Translation: AAK97139.1.
AF295783 Genomic DNA. Translation: AAK97140.1.

IPI

IPI00478816.
IPI00654656.
IPI00936431.

RefSeq

NP_001121170.1. NM_001127698.1.
NP_001121171.1. NM_001127699.1.
NP_006837.2. NM_006846.3.

UniGene

Hs.331555.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H0Z	NMR	-	A	356-423	[»]
1HDL	NMR	-	A	23-77	[»]
1UUC	NMR	-	A	23-77	[»]
1UVF	NMR	-	A	989-1047	[»]
1UVG	NMR	-	A	989-1064	[»]

ProteinModelPortal

Q9NQ38.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000352936.

Protein family/group databases

MEROPS

I01.013.

PTM databases

PhosphoSite

Q9NQ38.

Polymorphism databases

DMDM

212276440.

Proteomic databases

PaxDb

Q9NQ38.

PRIDE

Q9NQ38.

Protocols and materials databases

DNASU

11005.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256084; ENSP00000256084; ENSG00000133710.
ENST00000359874; ENSP00000352936; ENSG00000133710.
ENST00000398454; ENSP00000381472; ENSG00000133710.

GeneID

11005.

KEGG

hsa:11005.

UCSC

uc003low.2. human.
uc003lox.2. human.
uc003loy.2. human.

Organism-specific databases

CTD

11005.

GeneCards

GC05P147423.

H-InvDB

HIX0005288.

HGNC

HGNC:15464. SPINK5.

HPA

CAB015347.
HPA009067.
HPA011351.

MIM

256500. phenotype.
605010. gene.

neXtProt

NX_Q9NQ38.

Orphanet

634. Netherton syndrome.

PharmGKB

PA37962.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253835.

HOVERGEN

HBG006183.

OMA

NGKLICT.

OrthoDB

EOG4V4371.

Gene expression databases

ArrayExpress

Q9NQ38.

Bgee

Q9NQ38.

CleanEx

HS_SPINK5.

Genevestigator

Q9NQ38.

GermOnline

ENSG00000133710. Homo sapiens.

Family and domain databases

InterPro

IPR002350. Kazal_dom.
[Graphical view]

Pfam

PF00050. Kazal_1. 1 hit.
PF07648. Kazal_2. 13 hits.
[Graphical view]

SMART

SM00280. KAZAL. 14 hits.
[Graphical view]

PROSITE

PS00282. KAZAL_1. 2 hits.
PS51465. KAZAL_2. 14 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NQ38.

GenomeRNAi

11005.

NextBio

41803.

PMAP-CutDB

Q9NQ38.

SOURCE

Search...

Entry information

Entry name

ISK5_HUMAN

Accession

Primary (citable) accession number: Q9NQ38
Secondary accession number(s): A8MYE8 , B7WPB7, D6REN5, O75770, Q3LX95, Q3LX96, Q3LX97, Q96PP2, Q96PP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 4, 2001
Last sequence update:	November 4, 2008
Last modified:	May 1, 2013
This is version 127 of the entry and version 2 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.