P30740 (ILEU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Leukocyte elastase inhibitor
Short name=LEI

Alternative name(s):
Monocyte/neutrophil elastase inhibitor
Short name=EI
Short name=M/NEI
Peptidase inhibitor 2
Short name=PI-2
Serpin B1

Gene names

Name:	SERPINB1
Synonyms:	ELANH2, MNEI, PI2

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	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H. Ref.11
Subunit structure	Monomer. Ref.14
Subcellular location	Cytoplasm By similarity. Cytoplasmic granule Ref.14.
Domain	Reactive bond 1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin, chymase or granzyme H, while reactive bond 2 is specific for reaction with elastase-like protease such as neutrophil elastase, proteinase-3, pancreatic elastase or PSA.
Sequence similarities	Belongs to the serpin family. Ov-serpin subfamily.
Sequence caution	The sequence BAD97090.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Non-traceable author statement. Source: UniProtKB extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL
Molecular_function	serine-type endopeptidase inhibitor activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Leukocyte elastase inhibitor

PRO_0000094101

Sites

Site

343 – 344

2

Reactive bond 1

Site

344 – 345

2

Reactive bond 2

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.8

Modified residue

137

1

N6-acetyllysine Ref.12

Modified residue

177

1

N6-acetyllysine Ref.12

Natural variations

Natural variant

82

1

A → V.
Corresponds to variant rs34825616 [ dbSNP | Ensembl ].

VAR_051945

Experimental info

Sequence conflict

137

1

K → R in AAP35574. Ref.4

Sequence conflict

149

1

A → V in BAF84016. Ref.3

Sequence conflict

264

1

L → F in BAF84016. Ref.3

Sequence conflict

272

1

Missing AA sequence Ref.9

Sequence conflict

329

1

E → K in BAF84016. Ref.3

Secondary structure

1

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379

Helix Strand Turn

Details...

Helix

3 – 22

20

Beta strand

24 – 26

3

Beta strand

28 – 30

3

Helix

32 – 43

12

Helix

48 – 57

10

Helix

60 – 62

3

Helix

66 – 77

12

Beta strand

83 – 95

13

Helix

102 – 111

10

Beta strand

116 – 119

4

Helix

121 – 139

19

Turn

140 – 142

3

Beta strand

159 – 168

10

Beta strand

171 – 173

3

Turn

177 – 179

3

Beta strand

181 – 188

8

Beta strand

191 – 209

19

Turn

210 – 213

4

Beta strand

214 – 221

8

Beta strand

224 – 235

12

Beta strand

238 – 242

5

Helix

244 – 249

6

Helix

252 – 259

8

Helix

261 – 263

3

Beta strand

265 – 274

10

Beta strand

276 – 283

8

Helix

285 – 290

6

Helix

295 – 297

3

Turn

299 – 301

3

Turn

305 – 307

3

Beta strand

315 – 326

12

Beta strand

345 – 347

3

Beta strand

349 – 353

5

Beta strand

358 – 364

7

Turn

365 – 368

4

Beta strand

369 – 376

8

Sequences

	Sequence		Length	Mass (Da)
	P30740 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: BAAE08DFCBCD8CD3	FASTA	379	42,742
	10 20 30 40 50 60 MEQLSSANTR FALDLFLALS ENNPAGNIFI SPFSISSAMA MVFLGTRGNT AAQLSKTFHF 70 80 90 100 110 120 NTVEEVHSRF QSLNADINKR GASYILKLAN RLYGEKTYNF LPEFLVSTQK TYGADLASVD 130 140 150 160 170 180 FQHASEDARK TINQWVKGQT EGKIPELLAS GMVDNMTKLV LVNAIYFKGN WKDKFMKEAT 190 200 210 220 230 240 TNAPFRLNKK DRKTVKMMYQ KKKFAYGYIE DLKCRVLELP YQGEELSMVI LLPDDIEDES 250 260 270 280 290 300 TGLKKIEEQL TLEKLHEWTK PENLDFIEVN VSLPRFKLEE SYTLNSDLAR LGVQDLFNSS 310 320 330 340 350 360 KADLSGMSGA RDIFISKIVH KSFVEVNEEG TEAAAATAGI ATFCMLMPEE NFTADHPFLF 370 FIRHNSSGSI LFLGRFSSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor." Remold-O'Donnell E., Chin J., Alberts M. Proc. Natl. Acad. Sci. U.S.A. 89:5635-5639(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and sequence of human M/NEI (monocyte/neutrophil elastase inhibitor), an Ov-serpin family gene." Zeng W., Silverman G.A., Remold-O'Donnell E. Gene 213:179-187(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Small intestine.
[6]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] 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: Cervix.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10, ACETYLATION AT MET-1. Tissue: Platelet.
[9]	"A serpin from human tumor cells with direct lymphoid immunomodulatory activity: mitogenic stimulation of human tumor-infiltrating lymphocytes." Packard B.Z., Lee S.S., Remold-O'Donnell E., Komoriya A. Biochim. Biophys. Acta 1269:41-50(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 111-129; 216-244 AND 255-274.
[10]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 178-185; 204-210 AND 364-371. Tissue: Keratinocyte.
[11]	"The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites." Cooley J., Takayama T.K., Shapiro S.D., Schechter N.M., Remold-O'Donnell E. Biochemistry 40:15762-15770(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, FUNCTION, REACTIVE SITES.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Identification of SERPINB1 as a physiological inhibitor of human granzyme H." Wang L., Li Q., Wu L., Liu S., Zhang Y., Yang X., Zhu P., Zhang H., Zhang K., Lou J., Liu P., Tong L., Sun F., Fan Z. J. Immunol. 190:1319-1330(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH GZMH, SUBCELLULAR LOCATION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M93056 mRNA. No translation available.
AF053630 Genomic DNA. Translation: AAC31394.1.
AK291327 mRNA. Translation: BAF84016.1.
BT006928 mRNA. Translation: AAP35574.1.
AK223370 mRNA. Translation: BAD97090.1. Different initiation.
AL139092 Genomic DNA. Translation: CAH73667.1.
BC009015 mRNA. Translation: AAH09015.1.

IPI

IPI00027444.

PIR

S27383.

RefSeq

NP_109591.1. NM_030666.3.

UniGene

Hs.381167.
Hs.592409.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GA7	X-ray	2.90	A/B	1-379	[»]

ProteinModelPortal

P30740.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30740. 2 interactions.

STRING

9606.ENSP00000370115.

Protein family/group databases

MEROPS

I04.006.

PTM databases

PhosphoSite

P30740.

Polymorphism databases

DMDM

266344.

2D gel databases

OGP

P30740.

REPRODUCTION-2DPAGE

IPI00027444.

Proteomic databases

PaxDb

P30740.

PeptideAtlas

P30740.

PRIDE

P30740.

Protocols and materials databases

DNASU

1992.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000380739; ENSP00000370115; ENSG00000021355.

GeneID

1992.

KEGG

hsa:1992.

UCSC

uc003mub.3. human.

Organism-specific databases

CTD

1992.

GeneCards

GC06M002833.

HGNC

HGNC:3311. SERPINB1.

HPA

HPA018871.

MIM

130135. gene.

neXtProt

NX_P30740.

PharmGKB

PA35046.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4826.

HOGENOM

HOG000238519.

HOVERGEN

HBG005957.

InParanoid

P30740.

KO

K13963.

OMA

FPYGYIQ.

OrthoDB

EOG49KFQS.

PhylomeDB

P30740.

Gene expression databases

ArrayExpress

P30740.

Bgee

P30740.

CleanEx

HS_SERPINB1.

Genevestigator

P30740.

GermOnline

ENSG00000021355. Homo sapiens.

Family and domain databases

InterPro

IPR023795. Protease_inhib_I4_serpin_CS.
IPR015557. Protease_inhib_serpin_B1.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]

PANTHER

PTHR11461. PTHR11461. 1 hit.
PTHR11461:SF66. PTHR11461:SF66. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

SUPFAM

SSF56574. Prot_inh_serpin. 1 hit.

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SERPINB1. human.

GenomeRNAi

1992.

NextBio

8055.

PMAP-CutDB

P30740.

SOURCE

Search...

Entry information

Entry name

ILEU_HUMAN

Accession

Primary (citable) accession number: P30740
Secondary accession number(s): A8K5L2 , Q53FB9, Q5W0E1, Q9UDF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 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.