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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Ref.11
Subcellular location	Cytoplasm By similarity.
Domain	Reactive bond 1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin or chymase, while reactive bond 2 is specific for reaction with elastase-like protease such as neutrophyl 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 Phosphoprotein
Technical term	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. 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.13
	Modified residue	177	1	N6-acetyllysine Ref.13
	Modified residue	282	1	Phosphotyrosine Ref.12
	Modified residue	286	1	Phosphoserine 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

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: 1376927] [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: 9630619] [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: 14702039] [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: 14574404] [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: 15489334] [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: 12665801] [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: 7578269] [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: 1286667] [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: 11747453] [Abstract] Cited for: MASS SPECTROMETRY, FUNCTION, ACTIVE SITES.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-282 AND SER-286, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-177, MASS SPECTROMETRY.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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_030666.2.
UniGene	Hs.381167.
3D structure databases
ProteinModelPortal	P30740.
SMR	P30740. Positions 1-327, 349-379.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30740. 2 interactions.
STRING	P30740.
Protein family/group databases
MEROPS	I04.006.
PTM databases
PhosphoSite	P30740.
Polymorphism databases
DMDM	266344.
2D gel databases
Aarhus/Ghent-2DPAGE	4314. IEF.
OGP	P30740.
REPRODUCTION-2DPAGE	IPI00027444.
Proteomic databases
PeptideAtlas	P30740.
PRIDE	P30740.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380739; ENSP00000370115; ENSG00000021355.
GeneID	1992.
KEGG	hsa:1992.
UCSC	uc003mub.1. human.
Organism-specific databases
CTD	1992.
GeneCards	GC06M002778.
H-InvDB	HIX0005531.
HGNC	HGNC:3311. SERPINB1.
HPA	HPA018871.
MIM	130135. gene.
neXtProt	NX_P30740.
PharmGKB	PA35046.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05725.
GeneTree	ENSGT00580000081427.
HOGENOM	HBG714743.
HOVERGEN	HBG005957.
InParanoid	P30740.
OMA	STQKTYG.
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	IPR000215. Protease_inhib_I4_serpin. IPR023795. Protease_inhib_I4_serpin_CS. IPR015557. Protease_inhib_serpin_B1. IPR023796. Sepin_dom. [Graphical view]
KO	K13963.
PANTHER	PTHR11461. Prot_inh_serpin. 1 hit. PTHR11461:SF66. Serpin_LEI. 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
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:	January 25, 2012
This is version 114 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.