Reviewed, UniProtKB/Swiss-Prot P01009 (A1AT_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-1-antitrypsin
Alternative name(s):
    Alpha-1 protease inhibitor
    Alpha-1-antiproteinase
Cleaved into the following chain:
    1- Recommended name:
            Short peptide from AAT
                Short name=SPAAT

Gene names

Name:	SERPINA1
Synonyms:	AAT, PI
ORF Names:	PRO0684, PRO2209

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	418 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	Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Ref.17 Ref.18 Ref.24 Short peptide from AAT (SPAAT) is a reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Ref.17 Ref.18 Ref.24
Subcellular location	Secreted. Ref.24 Short peptide from AAT: Secreted › extracellular space › extracellular matrix. Ref.24
Tissue specificity	Plasma.
Domain	The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
Post-translational modification	Several isomers are observed, resulting from the combination of different N-linked glycan structures and mature N-terminus. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary, whereas glycan at Asn-70 is di-antennary with trace amounts of tri-antennary, and glycan at Asn-271 is exclusively di-antennary. The structure of the antennas is Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. Some antennas are fucosylated, which forms a Lewis-X determinant. Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.
Polymorphism	The sequence shown is that of the M1V allele which is the most common form of PI (44 to 49%). Other frequent alleles are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%.
Involvement in disease	The major physiological function of AAT is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). A hereditary deficiency of AAT, is associated with a 20-30 fold increased risk of developing chronic obstructive pulmonary disease. Deficiency of the normal inhibitor in individuals homozygous for allele Z or M-Malton can result in the development of chronic emphysema or infantile liver cirrhosis. Variant Pittsburgh is the cause of bleeding diathesis.
Miscellaneous	The aberrant form is found in the plasma of chronic smokers, and persists after smoking is ceased. It can still be found ten years after smoking has ceased.
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Biological process	Acute phase Blood coagulation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Hydrolase Protease Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from mutant phenotype. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA platelet alpha granule lumen Inferred from Experiment. Source: Reactome proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW protease binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase inhibitor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P00760	1	EBI-986224,EBI-986385	From a different organism.
ELA1	P00772	1	EBI-986224,EBI-986248	From a different organism.

Alternative products

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

Isoform 1 (identifier: P01009-1)

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 2 (identifier: P01009-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-418: AVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK → VRSP

Note: No experimental confirmation available.

Isoform 3 (identifier: P01009-3)

The sequence of this isoform differs from the canonical sequence as follows:
     307-418: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.17 Ref.18 Ref.15 Ref.16

Chain

25 – 418

394

Alpha-1-antitrypsin Ref.2

PRO_0000032377

Peptide

375 – 418

44

Short peptide from AAT

PRO_0000364030

Regions

Region

368 – 392

25

RCL

Sites

Binding site

256

1

Cysteine (covalent)

Site

382 – 383

2

Reactive bond

Amino acid modifications

Glycosylation

70

1

N-linked (GlcNAc...) Ref.19 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.2

Glycosylation

107

1

N-linked (GlcNAc...) Ref.19 Ref.29 Ref.2

Glycosylation

271

1

N-linked (GlcNAc...) Ref.19 Ref.26 Ref.27 Ref.28 Ref.29 Ref.2

Natural variations

Alternative sequence

307 – 418

112

Missing in isoform 3.

VSP_028890

Alternative sequence

356 – 418

63

AVHKA…NPTQK → VRSP in isoform 2.

VSP_028889

Natural variant

4

1

S → L in Z-Wrexham.

VAR_006978

Natural variant

26

1

D → A in V-Munich.

VAR_006979

Natural variant

37

1

T → A: dbSNP rs11558262.

VAR_051938

Natural variant

58

1

A → T in M5-Karlsruhe.

VAR_006980

Natural variant

63

1

R → C in I.

VAR_006981

Natural variant

65

1

L → P in M-Procida.

VAR_006982

Natural variant

69

1

S → F in M6-Bonn.

VAR_006983

Natural variant

75

1

Missing in M-Malton, M-Nichinan and M-Palermo; associated with very low serum levels of AAT.

VAR_006984

Natural variant

77

1

S → F in S-Iiyama.

VAR_006985

Natural variant

84

1

A → T in M6-Passau.

VAR_006986

Natural variant

91

1

G → E in M-Mineral springs; causes reduced AAT secretion.

VAR_006987

Natural variant

92

1

T → I in QO-Lisbon; deficient AAT with very low serum levels.

VAR_006988

Natural variant

109

1

T → M in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107.

VAR_011620

Natural variant

112

1

P → T in M5-Berlin.

VAR_006989

Natural variant

116

1

I → N in QO-Ludwigshafen.

VAR_006990

Natural variant

125

1

R → H in M2; associated with D-400. dbSNP rs709932.

VAR_006991

Natural variant

139

1

G → S in QO-Newport. dbSNP rs11558261.

VAR_006992

Natural variant

172

1

G → R in V and M-Nichinan.

VAR_006993

Natural variant

172

1

G → W in M2-Obernburg.

VAR_006994

Natural variant

180

1

Q → E in L-Frankfurt.

VAR_006995

Natural variant

190 – 198

9

QGKIVDLVK → GFQNAILVR in Aberrant form.

VAR_036746

Natural variant

228

1

E → K in X.

VAR_006996

Natural variant

237

1

V → A in M1A and Z; associated with K-366 in Z. dbSNP rs6647.

VAR_006997

Natural variant

247

1

R → C in F. Ref.49

VAR_006998

Natural variant

280

1

D → V in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona.

VAR_006999

Natural variant

288

1

E → V in S and T. dbSNP rs17580.

VAR_007000

Natural variant

305

1

Missing in Basque.

VAR_009216

Natural variant

354

1

S → F in S-Munich.

VAR_007001

Natural variant

360

1

A → T in W-Bethesda. dbSNP rs1802959.

VAR_007002

Natural variant

365

1

D → N in P-St.Albans/P-Donauwoerth.

VAR_007003

Natural variant

366

1

E → K in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z.

VAR_007004

Natural variant

382

1

M → R in Pittsburgh; has antithrombin activity.

VAR_007005

Natural variant

386

1

P → H in Sao Tome.

VAR_007006

Natural variant

386

1

P → T in L-Offenbach.

VAR_007007

Natural variant

387

1

E → K in Christchurch.

VAR_007008

Natural variant

393

1

P → L in M-Heerlen.

VAR_007009

Natural variant

400

1

E → D in M2 and M3; associated with H-125 in M2. dbSNP rs1303.

VAR_007010

Natural variant

415

1

P → H in Y-Barcelona; associated with V-280.

VAR_007011

Experimental info

Mutagenesis

382

1

M → V: Oxidation-resistant inhibitor of therapeutic importance. Ref.3

Sequence conflict

12

1

Missing in AAA51546. Ref.4

Sequence conflict

23

1

L → P in BAG38005. Ref.11

Sequence conflict

26

1

D → H AA sequence Ref.18

Sequence conflict

39

1

H → L AA sequence Ref.18

Sequence conflict

61

1

L → P in AAF29581. Ref.9

Sequence conflict

96

1

T → A in ABG73380. Ref.7

Sequence conflict

139 – 140

2

GN → DG in AAB59375. Ref.1

Sequence conflict

174

1

T → H in AAA51546. Ref.4

Sequence conflict

229

1

E → D in AAA51546. Ref.4

Sequence conflict

273

1

T → N in AAB59375. Ref.1

Sequence conflict

280

1

D → G in ABG73380. Ref.7

Sequence conflict

326

1

V → I in CAA25838. Ref.3

Sequence conflict

410

1

G → L AA sequence Ref.24

Sequence conflict

414

1

N → S AA sequence Ref.24

Secondary structure

1

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418

Helix Strand Turn

Details...

Turn

48 – 50

3

Helix

51 – 68

18

Beta strand

70 – 72

3

Beta strand

74 – 76

3

Helix

78 – 89

12

Helix

94 – 103

10

Turn

108 – 110

3

Helix

113 – 127

15

Beta strand

135 – 145

11

Helix

152 – 160

9

Beta strand

165 – 169

5

Helix

174 – 188

15

Turn

189 – 191

3

Beta strand

206 – 215

10

Beta strand

218 – 220

3

Helix

224 – 226

3

Beta strand

228 – 237

10

Beta strand

239 – 256

18

Turn

257 – 260

4

Beta strand

261 – 268

8

Turn

269 – 271

3

Beta strand

272 – 279

8

Helix

284 – 290

7

Helix

293 – 299

7

Beta strand

306 – 313

8

Beta strand

315 – 322

8

Helix

323 – 329

7

Helix

334 – 336

3

Turn

343 – 345

3

Beta strand

346 – 349

4

Beta strand

355 – 364

10

Beta strand

387 – 389

3

Beta strand

394 – 400

7

Turn

401 – 403

3

Beta strand

406 – 413

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 7016555F273B7F16	FASTA	418	46,737
	10 20 30 40 50 60 MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS 70 80 90 100 110 120 LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF 130 140 150 160 170 180 QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ 190 200 210 220 230 240 INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV 250 260 270 280 290 300 KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL 310 320 330 340 350 360 ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA 370 380 390 400 410 VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFMG KVVNPTQK
	Isoform 2. Checksum: D16A255538FB2945	FASTA	359	40,263
	10 20 30 40 50 60 MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS 70 80 90 100 110 120 LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF 130 140 150 160 170 180 QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ 190 200 210 220 230 240 INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV 250 260 270 280 290 300 KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL 310 320 330 340 350 ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP LKLSKVRSP
	Isoform 3. Checksum: 15C708E6C25CE0C4	FASTA	306	34,755
	10 20 30 40 50 60 MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS 70 80 90 100 110 120 LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF 130 140 150 160 170 180 QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ 190 200 210 220 230 240 INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV 250 260 270 280 290 300 KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL ENEDRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression in Escherichia coli of full-length complementary DNA coding for human alpha 1-antitrypsin." Bollen A., Herzog A., Cravador A., Herion P., Chuchana P., van der Straten A., Loriau R., Jacobs P., van Elsen A. DNA 2:255-264(1983) [PubMed: 6319097] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Complete sequence of the cDNA for human alpha 1-antitrypsin and the gene for the S variant." Long G.L., Chandra T., Woo S.L.C., Davie E.W., Kurachi K. Biochemistry 23:4828-4837(1984) [PubMed: 6093867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Synthesis in yeast of a functional oxidation-resistant mutant of human alpha-antitrypsin." Rosenberg S., Barr P.J., Najarian R.C., Hallewell R.A. Nature 312:77-80(1984) [PubMed: 6387509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF MET-382.
[4]	"Cell-specific expression of a transfected human alpha 1-antitrypsin gene." Ciliberto G., Dente L., Cortese R. Cell 41:531-540(1985) [PubMed: 2985281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Identification of a second mutation in the protein-coding sequence of the Z type alpha 1-antitrypsin gene." Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., Crystal R.G. J. Biol. Chem. 261:15989-15994(1986) [PubMed: 3491072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION OF VARIANT Z.
[6]	Erratum Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., Crystal R.G. J. Biol. Chem. 262:10412-10412(1987)
[7]	"An alpha-1 antitrypsin genetic variant from India." Shasany A.K., Shukla A.K., Darokar M.P., Saraiya M., Chaturvedi N., Tewari L., Khanuja S.P. Indian J. Biochem. Biophys. 44:176-178(2007) [PubMed: 17650587] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ALA-237 AND ASP-400. Tissue: Liver.
[8]	"Characterization of a new variant of alpha1 antitrypsin M Lille (p.Gly148Trp)." Balduyck M., Porchet N., Aubert J.-P., Zerimech F., Douchain F., Verchain S. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-172; ALA-237 AND LYS-366. Tissue: Lymphocyte.
[9]	"Functional prediction of the coding sequences of 32 new genes deduced by analysis of cDNA clones from human fetal liver." Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W., Bi J., Zhang Y., Liu M., He F. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Fetal liver.
[10]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Fetal liver and Placenta.
[11]	"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] (ISOFORM 1). Tissue: Synovium.
[12]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-237.
[13]	"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] (ISOFORM 1). Tissue: Colon and Ovary.
[14]	"Sequence homology and structural comparison between the chromosomal human alpha 1-antitrypsin and chicken ovalbumin genes." Leicht M., Long G.L., Chandra T., Kurachi K., Kidd V.J., Mace M. Jr., Davie E.W., Woo S.L.C. Nature 297:655-659(1982) [PubMed: 6979715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67; 196-255 AND 387-418.
[15]	"The covalent structure of human alpha1-protease inhibitor." Chan S.K. Fed. Proc. 41:1016-1016(1982) Cited for: PRELIMINARY PROTEIN SEQUENCE OF 25-418 (ISOFORM 1).
[16]	"Structure and variation of human alpha 1-antitrypsin." Carrell R.W., Jeppsson J.-O., Laurell C.-B., Brennan S.O., Owen M.C., Vaughan L., Boswell D.R. Nature 298:329-334(1982) [PubMed: 7045697] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-418 (ISOFORM 1).
[17]	"Appearance of an aberrant form of alpha-antitrypsin in the circulation of chronic cigarette smokers and its effect on the insulin induced NO synthesis in blood platelets." Sinha A.K., Girish G.V. Submitted (AUG-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 25-418 (ISOFORM 1), VARIANTS ABERRANT FORM 190-GLY--ARG-198 AND VAL-288, FUNCTION. Tissue: Blood.
[18]	"Characterization of a 54 kDa, alpha 1-antitrypsin-like protein isolated from ascitic fluid of an endometrial cancer patient." Tanaka N., Sekiya S., Takamizawa H., Kato N., Moriyama Y., Fujimura S. Jpn. J. Cancer Res. 82:693-700(1991) [PubMed: 1906855] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-39, FUNCTION. Tissue: Ascites.
[19]	"Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms." Kolarich D., Weber A., Turecek P.L., Schwarz H.P., Altmann F. Proteomics 6:3369-3380(2006) [PubMed: 16622833] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-48 AND 248-257 (ISOFORMS 1/2/3), GLYCOSYLATION AT ASN-70; ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES, CYSTEINE BINDING, MASS SPECTROMETRY.
[20]	"Sequencing of a urinary stone protein, identical to alpha-one antitrypsin, which lacks 22 amino acids." Umekawa T., Kohri K., Amasaki N., Yamate T., Yoshida K., Yamamoto K., Suzuki Y., Sinohara H., Kurita T. Biochem. Biophys. Res. Commun. 193:1049-1053(1993) [PubMed: 8323530] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-66. Tissue: Urine.
[21]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 50-63 AND 161-178 (ISOFORMS 1/2/3), MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[22]	"Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, acute phase and ZZ human liver." Riley J.H., Bathurst I.C., Edbrooke M.R., Carrell R.W., Craig R.K. FEBS Lett. 189:361-366(1985) [PubMed: 3876243] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 292-418 (ISOFORM 1).
[23]	"Cloning and sequence of cDNA coding for alpha 1-antitrypsin." Kurachi K., Chandra T., Friezner Degen S.J., White T.T., Marchioro T.L., Woo S.L.C., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981) [PubMed: 7031661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 350-418 (ISOFORM 1).
[24]	"Isolation and serine protease inhibitory activity of the 44-residue, C-terminal fragment of alpha 1-antitrypsin from human placenta." Niemann M.A., Narkates A.J., Miller E.J. Matrix 12:233-241(1992) [PubMed: 1406456] [Abstract] Cited for: PROTEIN SEQUENCE OF 375-414, IDENTIFICATION OF SPAAT, FUNCTION, SUBCELLULAR LOCATION. Tissue: Placenta.
[25]	"Construction and partial characterization of a human liver cDNA library." Coutelle C., Speer A., Rogers J., Kalsheker N., Humphries S., Williamson R. Biomed. Biochim. Acta 44:421-431(1985) [PubMed: 3873938] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 387-418 (ISOFORM 1).
[26]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-70 AND ASN-271.
[27]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, MASS SPECTROMETRY. Tissue: Bile.
[28]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271, MASS SPECTROMETRY. Tissue: Plasma.
[29]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, MASS SPECTROMETRY. Tissue: Plasma.
[30]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70, MASS SPECTROMETRY. Tissue: Platelet.
[31]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[32]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, MASS SPECTROMETRY. Tissue: Liver.
[33]	"Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function." Loebermann H., Tokuoka R., Deisenhofer J., Huber R. J. Mol. Biol. 177:531-556(1984) [PubMed: 6332197] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[34]	"The S variant of human alpha 1-antitrypsin, structure and implications for function and metabolism." Engh R., Loebermann H., Schneider M., Wiegand G., Huber R., Laurell C.-B. Protein Eng. 2:407-415(1989) [PubMed: 2785270] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[35]	"Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop." Song H.K., Lee K.N., Kwon K.-S., Yu M.-H., Suh S.W. FEBS Lett. 377:150-154(1995) [PubMed: 8543039] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 25-418.
[36]	"Inhibitory conformation of the reactive loop of alpha 1-antitrypsin." Elliott P.R., Lomas D.A., Carrell R.W., Abrahams J.P. Nat. Struct. Biol. 3:676-681(1996) [PubMed: 8756325] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418.
[37]	"The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A." Ryu S.-E., Choi H.-J., Kwon K.-S., Lee K.N., Yu M.-H. Structure 4:1181-1192(1996) [PubMed: 8939743] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 45-418.
[38]	"Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation." Elliott P.R., Abrahams J.P., Lomas D.A. J. Mol. Biol. 275:419-425(1998) [PubMed: 9466920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418.
[39]	"Structure of a serpin-protease complex shows inhibition by deformation." Huntington J.A., Read R.J., Carrell R.W. Nature 407:923-926(2000) [PubMed: 11057674] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-418 IN COMPLEX WITH BOVINE TRYPSIN.
[40]	"Cleaved antitrypsin polymers at atomic resolution." Dunstone M.A., Dai W., Whisstock J.C., Rossjohn J., Pike R.N., Feil S.C., Le Bonniec B.F., Parker M.W., Bottomley S.P. Protein Sci. 9:417-420(2000) [PubMed: 10716194] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 44-418.
[41]	"Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets for rational drug design to prevent conformational disease." Elliott P.R., Pei X.Y., Dafforn T.R., Lomas D.A. Protein Sci. 9:1274-1281(2000) [PubMed: 10933492] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[42]	"A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops." Kim S.-J., Woo J.-R., Seo E.J., Yu M.-H., Ryu S.-E. J. Mol. Biol. 306:109-119(2001) [PubMed: 11178897] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-418.
[43]	"Interactions causing the kinetic trap in serpin protein folding." Im H., Woo M.-S., Hwang K.Y., Yu M.-H. J. Biol. Chem. 277:46347-46354(2002) [PubMed: 12244055] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-418.
[44]	"Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases." Dementiev A., Simonovic M., Volz K., Gettins P.G. J. Biol. Chem. 278:37881-37887(2003) [PubMed: 12860985] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-418 OF VARIANT PITTSBURGH ARG-382.
[45]	"Alpha 1-antitrypsin: structure, function and molecular biology of the gene." Kalsheker N. Biosci. Rep. 9:129-138(1989) [PubMed: 2669992] [Abstract] Cited for: REVIEW.
[46]	"The molecular genetics of alpha 1 antitrypsin deficiency." Wu Y., Foreman R.C. Bioessays 13:163-169(1991) [PubMed: 1859394] [Abstract] Cited for: REVIEW.
[47]	"Characterization of the gene and protein of the common alpha 1-antitrypsin normal M2 allele." Nukiwa T., Brantly M.L., Ogushi F., Fells G.A., Crystal R.G. Am. J. Hum. Genet. 43:322-330(1988) [PubMed: 2901226] [Abstract] Cited for: CHARACTERIZATION OF VARIANT M2.
[48]	"Characterisation of the alpha-1-antitrypsin M3 gene, a normal variant." Graham A., Hayes K., Weidinger S., Newton C.R., Markham A.F., Kalsheker N.A. Hum. Genet. 85:381-382(1990) [PubMed: 2394452] [Abstract] Cited for: VARIANT M3 ASP-400.
[49]	"Characterization of the molecular basis of the alpha 1-antitrypsin F allele." Okayama H., Brantly M., Holmes M., Crystal R.G. Am. J. Hum. Genet. 48:1154-1158(1991) [PubMed: 2035534] [Abstract] Cited for: VARIANT F CYS-247.
[50]	"A Pro-->Leu substitution in codon 369 of the alpha-1-antitrypsin deficiency variant PI M-Heerlen." Hofker M.H., Nukiwa T., van Paassen H.M.B., Nelen M., Kramps J.A., Klasen E.C., Frants R.R., Crystal R.G. Hum. Genet. 81:264-268(1989) [PubMed: 2784123] [Abstract] Cited for: VARIANT M-HEERLEN LEU-393.
[51]	"In-frame single codon deletion in the M-Malton deficiency allele of alpha 1-antitrypsin." Fraizer G.C., Harrold T.R., Hofker M.H., Cox D.W. Am. J. Hum. Genet. 44:894-902(1989) [PubMed: 2786335] [Abstract] Cited for: VARIANT M-MALTON PHE-75 DEL.
[52]	"Molecular basis of alpha 1-antitrypsin deficiency and emphysema associated with the alpha 1-antitrypsin M-Mineral springs allele." Curiel D.T., Vogelmeier C., Hubbard R.C., Stier L.E., Crystal R.G. Mol. Cell. Biol. 10:47-56(1990) [PubMed: 1967187] [Abstract] Cited for: VARIANT M-MINERAL SPRINGS GLU-91.
[53]	"Molecular analysis of the gene of the alpha 1-antitrypsin deficiency variant, M-Nichinan." Matsunaga E., Shiokawa S., Nakamura H., Maruyama T., Tsuda K., Fukumaki Y. Am. J. Hum. Genet. 46:602-612(1990) [PubMed: 2309708] [Abstract] Cited for: VARIANT M-NICHINAN PHE-75 DEL.
[54]	"Characterization of the gene and protein of the alpha 1-antitrypsin 'deficiency' allele M-Procida." Takahashi H., Nukiwa T., Satoh K., Ogushi F., Brantly M., Fells G., Stier L., Courtney M., Crystal R.G. J. Biol. Chem. 263:15528-15534(1988) [PubMed: 3262617] [Abstract] Cited for: VARIANT M-PROCIDA PRO-65.
[55]	"Genetic diversity from a limited repertoire of mutations on different common allelic backgrounds: alpha 1-antitrypsin deficiency variant P-Duarte." Hildesheim J., Kinsley G., Bissell M., Pierce J., Brantly M. Hum. Mutat. 2:221-228(1993) [PubMed: 8364590] [Abstract] Cited for: VARIANT P-DUARTE VAL-280.
[56]	"Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder." Owen M.C., Brennan S.O., Lewis J.H., Carrell R.W. N. Engl. J. Med. 309:694-698(1983) [PubMed: 6604220] [Abstract] Cited for: VARIANT PITTSBURGH ARG-382.
[57]	"Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone." Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S. J. Biol. Chem. 266:12627-12632(1991) [PubMed: 1905728] [Abstract] Cited for: VARIANT S-IIYAMA PHE-77.
[58]	"Characterization of the normal alpha 1-antitrypsin allele V-Munich: a variant associated with a unique protein isoelectric focusing pattern." Holmes M.D., Brantly M.L., Curiel D.T., Weidinger S., Crystal R.G. Am. J. Hum. Genet. 46:810-816(1990) [PubMed: 2316526] [Abstract] Cited for: VARIANT V-MUNICH ALA-26.
[59]	"Alpha 1-antitrypsin W-Bethesda: molecular basis of an unusual alpha 1-antitrypsin deficiency variant." Holmes M.D., Brantly M.L., Fells G.A., Crystal R.G. Biochem. Biophys. Res. Commun. 170:1013-1020(1990) [PubMed: 2390072] [Abstract] Cited for: VARIANT W-BETHESDA THR-360.
[60]	"Sequence data of the rare deficient alpha 1-antitrypsin variant PI Zaugsburg." Faber J.-P., Weidinger S., Olek K. Am. J. Hum. Genet. 46:1158-1162(1990) [PubMed: 2339709] [Abstract] Cited for: VARIANT Z-AUGSBURG LYS-366.
[61]	"Molecular characterisation of two alpha-1-antitrypsin deficiency variants: proteinase inhibitor (Pi) Null(Newport) (Gly115-->Ser) and (Pi) Z Wrexham (Ser-19-->Leu)." Graham A., Kalsheker N.A., Bamforth F.J., Newton C.R., Markham A.F. Hum. Genet. 85:537-540(1990) [PubMed: 2227940] [Abstract] Cited for: VARIANTS Z-WREXHAM LEU-4 AND Q0-NEWPORT SER-139.
[62]	"Molecular characterisation of three alpha-1-antitrypsin deficiency variants: proteinase inhibitor (Pi) nullcardiff (Asp256-->Val); PiM-Malton (Phe51-->deletion) and PiI (Arg39-->Cys)." Graham A., Kalsheker N.A., Newton C.R., Bamforth F.J., Powell S.J., Markham A.F. Hum. Genet. 84:55-58(1989) [PubMed: 2606478] [Abstract] Cited for: VARIANTS P-CARDIFF VAL-280; I CYS-63 AND M-MALTON PHE-75 DEL.
[63]	"A null deficiency allele of alpha 1-antitrypsin, QO-Ludwigshafen, with altered tertiary structure." Fraizer G.C., Siewertsen M.A., Hofker M.H., Brubacher M.G., Cox D.W. J. Clin. Invest. 86:1878-1884(1990) [PubMed: 2254451] [Abstract] Cited for: VARIANT QO-LUDWIGSHAFEN ASN-116.
[64]	"Identification and DNA sequence analysis of 15 new alpha 1-antitrypsin variants, including two PI*Q0 alleles and one deficient PI*M allele." Faber J.-P., Poller W., Weidinger S., Kirchgesser M., Schwaab R., Bidlingmaier F., Olek K. Am. J. Hum. Genet. 55:1113-1121(1994) [PubMed: 7977369] [Abstract] Cited for: VARIANTS.
[65]	"A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI ZBristol) associated with novel electrophoretic properties." Lovegrove J.U., Jeremiah S., Gillett G.T., Temple I.K., Povey S., Whitehouse D.B. Ann. Hum. Genet. 61:385-391(1997) [PubMed: 9459000] [Abstract] Cited for: VARIANT Z-BRISTOL MET-109.
[66]	"Identification and molecular charaterization of the new alpha-1-antitrypsin deficient allele PI YBarcelona (Asp256Val and Pro391His)." Jardi R., Rodriguez F., Miravitlles M., Vidal R., Cotrina M., Quer J., Pascual C., Weidinger S. Hum. Mutat. 12:213-213(1998) [PubMed: 10651487] [Abstract] Cited for: VARIANTS Y-BARCELONA VAL-280 AND HIS-415.
[67]	"A novel alpha-1-antitrypsin P362H variant found in a population sample from Sao Tome e Principe (Gulf of Guinea, West Africa)." Seixas S., Trovoada M.J., Santos M.T., Rocha J. Hum. Mutat. 13:414-414(1999) Cited for: VARIANT SAO TOME HIS-386.
[68]	"A novel alpha-1-antitrypsin r281del variant found in a population sample from the Basque country." Seixas S., Garcia O., Amorim A., Rocha J. Hum. Mutat. 15:121-122(2000) [PubMed: 10612848] [Abstract] Cited for: VARIANT BASQUE ARG-305 DEL.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Alpha-1 antitrypsin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

K01396 mRNA. Translation: AAB59375.1.
K02212 Genomic DNA. Translation: AAB59495.1.
X01683 mRNA. Translation: CAA25838.1.
M11465 mRNA. Translation: AAA51546.1.
J02619 Genomic DNA. Translation: AAA51547.1.
DQ682455 mRNA. Translation: ABG73380.1.
AM048838 Genomic DNA. Translation: CAJ15161.1.
AF113676 mRNA. Translation: AAF29581.1.
AF130068 mRNA. Translation: AAG35496.1.
BX161449 mRNA. Translation: CAD61914.1.
BX247968 mRNA. Translation: CAD62306.1.
BX248002 mRNA. Translation: CAD62334.1. Different initiation.
BX248257 mRNA. Translation: CAD62585.1. Different initiation.
AK315637 mRNA. Translation: BAG38005.1.
BT019455 mRNA. Translation: AAV38262.1.
BC011991 mRNA. Translation: AAH11991.1.
BC015642 mRNA. Translation: AAH15642.1.
J00064 Genomic DNA. Translation: AAB59369.1.
J00066, J00065 Genomic DNA. Translation: AAB59370.1.
J00067 Genomic DNA. Translation: AAB59371.1.
X02920 mRNA. Translation: CAA26677.1.
V00496 mRNA. Translation: CAA23755.1.
M26123 mRNA. Translation: AAA51545.1.

IPI

IPI00553177.
IPI00790784.
IPI00869004.

PIR

ITHU. A21853.
A61391.

RefSeq

NP_000286.3.
NP_001002235.1.
NP_001002236.1.
NP_001121172.1.
NP_001121173.1.
NP_001121174.1.
NP_001121175.1.
NP_001121176.1.
NP_001121177.1.
NP_001121178.1.
NP_001121179.1.

UniGene

Hs.525557

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ATU	X-ray	2.70	A	45-418	[»]
1D5S	X-ray	3.00	A	44-377	[»]
			B	378-418	[»]
1EZX	X-ray	2.60	A	48-382	[»]
			B	383-418	[»]
1HP7	X-ray	2.10	A	25-418	[»]
1IZ2	X-ray	2.20	A	25-418	[»]
1KCT	X-ray	3.46	A	25-418	[»]
1OO8	X-ray	2.65	A	26-418	[»]
1OPH	X-ray	2.30	A	26-418	[»]
1PSI	X-ray	2.92	A	26-418	[»]
1QLP	X-ray	2.00	A	26-418	[»]
1QMB	X-ray	2.60	A	49-376	[»]
			B	377-418	[»]
2D26	X-ray	3.30	A	26-382	[»]
			B	383-418	[»]
2QUG	X-ray	2.00	A	25-418	[»]
3CWL	X-ray	2.44	A	25-418	[»]
3CWM	X-ray	2.51	A	25-418	[»]
3DRM	X-ray	2.20	A	26-418	[»]
3DRU	X-ray	3.20	A/B/C	26-418	[»]
7API	X-ray	3.00	A	36-382	[»]
			B	383-418	[»]
8API	X-ray	3.10	A	36-382	[»]
			B	383-418	[»]
9API	X-ray	3.00	A	36-382	[»]
			B	383-418	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P01009. 6 interactions.

Protein family/group databases

MEROPS

I04.001.

PTM databases

GlycoSuiteDB

P01009.

PhosphoSite

P01009.

2-D gel databases

SWISS-2DPAGE

P01009.

Cornea-2DPAGE

P01009.

DOSAC-COBS-2DPAGE

P01009.

HSC-2DPAGE

P01009.

OGP

P01009.

REPRODUCTION-2DPAGE

IPI00553177.
P01009.

Siena-2DPAGE

P01009.

Proteomic databases

PRIDE

P01009.

Genome annotation databases

Ensembl

ENSG00000197249. Homo sapiens. [Contig view]

GeneID

5265.

KEGG

hsa:5265.

Organism-specific databases

GeneCards

GC14M093914.

H-InvDB

HIX0011929.

HGNC

HGNC:8941. SERPINA1.

HPA

CAB013211.
CAB016648.
HPA000927.
HPA001292.

MIM

107400. gene+phenotype.

Orphanet

60. Alpha-1 antitrypsin deficiency.

PharmGKB

PA35509.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P01009.

HOVERGEN

P01009.

OMA

P01009. AGAMFLE.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P01009.

Bgee

P01009.

GermOnline

ENSG00000197249. Homo sapiens.

Family and domain databases

InterPro

IPR000215. Protease_inhib_I4_serpin.
[Graphical view]

PANTHER

PTHR11461. Prot_inh_serpin. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00058. Alpha-1-proteinase inhibitor.

NextBio

20336.

PMAP-CutDB

P01009.

SOURCE

Search...

Entry information

Entry name

A1AT_HUMAN

Accession

Primary (citable) accession number: P01009
Secondary accession number(s): A6PX14 , B2RDQ8, Q0PVP5, Q13672, Q53XB8, Q5U0M1, Q7M4R2, Q86U18, Q86U19, Q96BF9, Q96ES1, Q9P1P0, Q9UCE6, Q9UCM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 150 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)