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P01009 (A1AT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 203. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1-antitrypsin
Alternative name(s):
Alpha-1 protease inhibitor
Alpha-1-antiproteinase
Serpin A1

Cleaved into the following chain:

  1. Short peptide from AAT
    Short name=SPAAT
Gene names
Name:SERPINA1
Synonyms:AAT, PI
ORF Names:PRO0684, PRO2209
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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: reversible chymotrypsin inhibitor. It also inhibits elastase, but not trypsin. Its major physiological function is the protection of the lower respiratory tract against proteolytic destruction by human leukocyte elastase (HLE). Ref.17 Ref.18 Ref.24

Subunit structure

The variants S and Z interact with CANX AND PDIA3.

Subcellular location

Secreted. Endoplasmic reticulum. Note: The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum. Ref.24 Ref.72

Short peptide from AAT: Secretedextracellular spaceextracellular matrix Ref.24 Ref.72.

Tissue specificity

Ubiquitous. Expressed in leukocytes and plasma. Ref.72

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

N-glycosylated. Differential glycosylation produces a number of isoforms. N-linked glycan at Asn-107 is alternatively di-antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 is di-antennary with trace amounts of tri-antennary. Glycan at Asn-271 is exclusively di-antennary. Structure of glycans at Asn-70 and Asn-271 is Hex5HexNAc4. The structure of the antennae 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 antennae are fucosylated, which forms a Lewis-X determinant. Ref.19 Ref.26 Ref.32 Ref.35 Ref.72

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

Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: A disorder whose most common manifestation is emphysema, which becomes evident by the third to fourth decade. A less common manifestation of the deficiency is liver disease, which occurs in children and adults, and may result in cirrhosis and liver failure. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60 Ref.62 Ref.64

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.

Sequence caution

The sequence CAD62334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAD62585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-986224,EBI-986224
P007605EBI-986224,EBI-986385From a different organism.
CELA1P007722EBI-986224,EBI-986248From a different organism.
espBP712133EBI-986224,EBI-2615322From a different organism.
SSR1P433074EBI-986224,EBI-714168

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. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.15 Ref.16 Ref.17 Ref.18
Chain25 – 418394Alpha-1-antitrypsin Ref.2
PRO_0000032377
Peptide375 – 41844Short peptide from AAT
PRO_0000364030

Regions

Region368 – 39225RCL

Sites

Site382 – 3832Reactive bond

Amino acid modifications

Modified residue2561S-cysteinyl cysteine
Glycosylation701N-linked (GlcNAc...) (complex) Ref.19 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.33 Ref.35
Glycosylation1071N-linked (GlcNAc...) (complex) Ref.19 Ref.29 Ref.31 Ref.32 Ref.33
Glycosylation2711N-linked (GlcNAc...) (complex) Ref.19 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.35

Natural variations

Alternative sequence307 – 418112Missing in isoform 3.
VSP_028890
Alternative sequence356 – 41863AVHKA…NPTQK → VRSP in isoform 2.
VSP_028889
Natural variant41S → L in Z-Wrexham. Ref.64
VAR_006978
Natural variant261D → A in V-Munich. Ref.61
VAR_006979
Natural variant371T → A.
Corresponds to variant rs11558262 [ dbSNP | Ensembl ].
VAR_051938
Natural variant581A → T in M5-Karlsruhe.
VAR_006980
Natural variant631R → C in I. Ref.65
Corresponds to variant rs28931570 [ dbSNP | Ensembl ].
VAR_006981
Natural variant651L → P in M-Procida. Ref.57
Corresponds to variant rs28931569 [ dbSNP | Ensembl ].
VAR_006982
Natural variant691S → F in M6-Bonn.
VAR_006983
Natural variant751Missing in M-Malton, M-Nichinan and M-Palermo; associated with very low serum levels of AAT; homozygosity for allele M-Malton may be associated with a risk for chronic emphysema or infantile liver cirrhosis. Ref.54 Ref.56 Ref.65
VAR_006984
Natural variant771S → F in S-Iiyama. Ref.60
Corresponds to variant rs55819880 [ dbSNP | Ensembl ].
VAR_006985
Natural variant841A → T in M6-Passau.
VAR_006986
Natural variant911G → E in M-Mineral springs; causes reduced AAT secretion. Ref.55
Corresponds to variant rs28931568 [ dbSNP | Ensembl ].
VAR_006987
Natural variant921T → I in QO-Lisbon; deficient AAT with very low serum levels.
VAR_006988
Natural variant1091T → M in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107. Ref.68
VAR_011620
Natural variant1121P → T in M5-Berlin.
VAR_006989
Natural variant1161I → N in QO-Ludwigshafen. Ref.66
Corresponds to variant rs28931572 [ dbSNP | Ensembl ].
VAR_006990
Natural variant1251R → H in M2; associated with D-400.
Corresponds to variant rs709932 [ dbSNP | Ensembl ].
VAR_006991
Natural variant1391G → S in QO-Newport. Ref.64
Corresponds to variant rs11558261 [ dbSNP | Ensembl ].
VAR_006992
Natural variant1721G → R in V and M-Nichinan.
VAR_006993
Natural variant1721G → W in M2-Obernburg. Ref.8
VAR_006994
Natural variant1801Q → E in L-Frankfurt.
VAR_006995
Natural variant190 – 1989QGKIVDLVK → GFQNAILVR in Aberrant form.
VAR_036746
Natural variant2281E → K in X.
VAR_006996
Natural variant2371V → A in M1A and Z; associated with K-366 in Z. Ref.7 Ref.8 Ref.12 Ref.72
Corresponds to variant rs6647 [ dbSNP | Ensembl ].
VAR_006997
Natural variant2471R → C in F. Ref.52
Corresponds to variant rs28929470 [ dbSNP | Ensembl ].
VAR_006998
Natural variant2801D → V in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona. Ref.58 Ref.65 Ref.69
Corresponds to variant rs28929472 [ dbSNP | Ensembl ].
VAR_006999
Natural variant2881E → V in S and T. Ref.17 Ref.72
Corresponds to variant rs17580 [ dbSNP | Ensembl ].
VAR_007000
Natural variant3051Missing in Basque. Ref.71
VAR_009216
Natural variant3541S → F in S-Munich.
VAR_007001
Natural variant3601A → T in W-Bethesda. Ref.62
Corresponds to variant rs1802959 [ dbSNP | Ensembl ].
VAR_007002
Natural variant3651D → N in P-St.Albans/P-Donauwoerth.
VAR_007003
Natural variant3661E → K in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z. Ref.8 Ref.63 Ref.72
Corresponds to variant rs28929474 [ dbSNP | Ensembl ].
VAR_007004
Natural variant3821M → R in Pittsburgh; has antithrombin activity; causes fatal bleeding diathesis. Ref.47 Ref.59
VAR_007005
Natural variant3861P → H in Sao Tome. Ref.70
VAR_007006
Natural variant3861P → T in L-Offenbach.
VAR_007007
Natural variant3871E → K in Christchurch.
Corresponds to variant rs121912712 [ dbSNP | Ensembl ].
VAR_007008
Natural variant3931P → L in M-Heerlen. Ref.53
VAR_007009
Natural variant4001E → D in M2 and M3; associated with H-125 in M2. Ref.7 Ref.51
Corresponds to variant rs1303 [ dbSNP | Ensembl ].
VAR_007010
Natural variant4151P → H in Y-Barcelona; associated with V-280. Ref.69
VAR_007011

Experimental info

Mutagenesis3821M → V: Oxidation-resistant inhibitor of therapeutic importance. Ref.3
Sequence conflict121Missing in AAA51546. Ref.4
Sequence conflict231L → P in BAG38005. Ref.11
Sequence conflict261D → H AA sequence Ref.18
Sequence conflict391H → L AA sequence Ref.18
Sequence conflict611L → P in AAF29581. Ref.9
Sequence conflict961T → A in ABG73380. Ref.7
Sequence conflict139 – 1402GN → DG in AAB59375. Ref.1
Sequence conflict1741T → H in AAA51546. Ref.4
Sequence conflict2291E → D in AAA51546. Ref.4
Sequence conflict2731T → N in AAB59375. Ref.1
Sequence conflict2801D → G in ABG73380. Ref.7
Sequence conflict3261V → I in CAA25838. Ref.3
Sequence conflict4101G → L AA sequence Ref.24
Sequence conflict4141N → S AA sequence Ref.24

Secondary structure

.................................................................. 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 7016555F273B7F16

FASTA41846,737
        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 

« Hide

Isoform 2 [UniParc].

Checksum: D16A255538FB2945
Show »

FASTA35940,263
Isoform 3 [UniParc].

Checksum: 15C708E6C25CE0C4
Show »

FASTA30634,755

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271.
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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271.
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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271.
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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70.
Tissue: Platelet.
[31]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271.
Tissue: Liver.
[32]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-107 AND ASN-271.
[33]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[34]"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].
[35]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-70 AND ASN-271, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[36]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[37]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[38]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 25-418.
[39]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418.
[40]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 45-418.
[41]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418.
[42]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-418 IN COMPLEX WITH BOVINE TRYPSIN.
[43]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 44-418.
[44]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[45]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-418.
[46]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-418.
[47]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-418 OF VARIANT PITTSBURGH ARG-382.
[48]"Alpha 1-antitrypsin: structure, function and molecular biology of the gene."
Kalsheker N.
Biosci. Rep. 9:129-138(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[49]"The molecular genetics of alpha 1 antitrypsin deficiency."
Wu Y., Foreman R.C.
Bioessays 13:163-169(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[50]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT M2.
[51]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M3 ASP-400.
[52]"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] [Europe PMC] [Abstract]
Cited for: VARIANT F CYS-247.
[53]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M-HEERLEN LEU-393.
[54]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M-MALTON PHE-75 DEL.
[55]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M-MINERAL SPRINGS GLU-91.
[56]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M-NICHINAN PHE-75 DEL.
[57]"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] [Europe PMC] [Abstract]
Cited for: VARIANT M-PROCIDA PRO-65.
[58]"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] [Europe PMC] [Abstract]
Cited for: VARIANT P-DUARTE VAL-280.
[59]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT OF VARIANT PITTSBURGH ARG-382 IN BLEEDING DIATHESIS.
[60]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN A1ATD, VARIANT S-IIYAMA PHE-77.
[61]"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] [Europe PMC] [Abstract]
Cited for: VARIANT V-MUNICH ALA-26.
[62]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN A1ATD, VARIANT W-BETHESDA THR-360.
[63]"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] [Europe PMC] [Abstract]
Cited for: VARIANT Z-AUGSBURG LYS-366.
[64]"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] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN A1ATD, VARIANTS Z-WREXHAM LEU-4 AND Q0-NEWPORT SER-139.
[65]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS P-CARDIFF VAL-280; I CYS-63 AND M-MALTON PHE-75 DEL.
[66]"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] [Europe PMC] [Abstract]
Cited for: VARIANT QO-LUDWIGSHAFEN ASN-116.
[67]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS.
[68]"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] [Europe PMC] [Abstract]
Cited for: VARIANT Z-BRISTOL MET-109.
[69]"Identification and molecular characterization 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] [Europe PMC] [Abstract]
Cited for: VARIANTS Y-BARCELONA VAL-280 AND HIS-415.
[70]"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.
[71]"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] [Europe PMC] [Abstract]
Cited for: VARIANT BASQUE ARG-305 DEL.
[72]"SERPINA2 is a novel gene with a divergent function from SERPINA1."
Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I., Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.
PLoS ONE 8:E66889-E66889(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS Z ALA-237 AND LYS-366, VARIANT S VAL-288, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH CANX AND PDIA3.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Alpha-1 antitrypsin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRITHU. A21853.
A61391.
RefSeqNP_000286.3. NM_000295.4.
NP_001002235.1. NM_001002235.2.
NP_001002236.1. NM_001002236.2.
NP_001121172.1. NM_001127700.1.
NP_001121173.1. NM_001127701.1.
NP_001121174.1. NM_001127702.1.
NP_001121175.1. NM_001127703.1.
NP_001121176.1. NM_001127704.1.
NP_001121177.1. NM_001127705.1.
NP_001121178.1. NM_001127706.1.
NP_001121179.1. NM_001127707.1.
UniGeneHs.525557.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATUX-ray2.70A45-418[»]
1D5SX-ray3.00A44-377[»]
B378-418[»]
1EZXX-ray2.60A48-382[»]
B383-418[»]
1HP7X-ray2.10A25-418[»]
1IZ2X-ray2.20A25-418[»]
1KCTX-ray3.46A25-418[»]
1OO8X-ray2.65A26-418[»]
1OPHX-ray2.30A26-418[»]
1PSIX-ray2.92A26-418[»]
1QLPX-ray2.00A26-418[»]
1QMBX-ray2.60A49-376[»]
B377-418[»]
2D26X-ray3.30A26-382[»]
B383-418[»]
2QUGX-ray2.00A25-418[»]
3CWLX-ray2.44A25-418[»]
3CWMX-ray2.51A25-418[»]
3DRMX-ray2.20A26-418[»]
3DRUX-ray3.20A/B/C26-418[»]
3NDDX-ray1.50A46-372[»]
B383-418[»]
3NDFX-ray2.70A46-381[»]
B383-418[»]
3NE4X-ray1.81A1-418[»]
3T1PX-ray3.90A48-418[»]
7APIX-ray3.00A36-382[»]
B383-418[»]
8APIX-ray3.10A36-382[»]
B383-418[»]
9APIX-ray3.00A36-382[»]
B383-418[»]
ProteinModelPortalP01009.
SMRP01009. Positions 48-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111283. 22 interactions.
DIPDIP-35493N.
IntActP01009. 18 interactions.
MINTMINT-365327.

Chemistry

DrugBankDB00058. Alpha-1-proteinase inhibitor.

Protein family/group databases

MEROPSI04.001.

PTM databases

PhosphoSiteP01009.
UniCarbKBP01009.

Polymorphism databases

DMDM1703025.

2D gel databases

DOSAC-COBS-2DPAGEP01009.
OGPP01009.
REPRODUCTION-2DPAGEIPI00553177.
P01009.
SWISS-2DPAGEP01009.
UCD-2DPAGEP01009.

Proteomic databases

PaxDbP01009.
PRIDEP01009.

Protocols and materials databases

DNASU5265.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355814; ENSP00000348068; ENSG00000197249. [P01009-1]
ENST00000393087; ENSP00000376802; ENSG00000197249. [P01009-1]
ENST00000393088; ENSP00000376803; ENSG00000197249. [P01009-1]
ENST00000402629; ENSP00000386094; ENSG00000197249. [P01009-2]
ENST00000404814; ENSP00000385960; ENSG00000197249. [P01009-1]
ENST00000437397; ENSP00000408474; ENSG00000197249. [P01009-1]
ENST00000440909; ENSP00000390299; ENSG00000197249. [P01009-1]
ENST00000448921; ENSP00000416066; ENSG00000197249. [P01009-1]
ENST00000449399; ENSP00000416354; ENSG00000197249. [P01009-1]
ENST00000489769; ENSP00000451525; ENSG00000197249. [P01009-3]
GeneID5265.
KEGGhsa:5265.
UCSCuc001ycx.4. human. [P01009-1]
uc001yda.1. human. [P01009-2]

Organism-specific databases

CTD5265.
GeneCardsGC14M094843.
HGNCHGNC:8941. SERPINA1.
HPACAB013211.
CAB016648.
HPA000927.
HPA001292.
MIM107400. gene.
613490. phenotype.
neXtProtNX_P01009.
Orphanet60. Alpha-1-antitrypsin deficiency.
178396. Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation.
PharmGKBPA35509.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOVERGENHBG005957.
InParanoidP01009.
KOK03984.
OMAVVNPTQK.
OrthoDBEOG7QC7W9.
PhylomeDBP01009.
TreeFamTF343201.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP01009.
BgeeP01009.
GenevestigatorP01009.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPINA1. human.
EvolutionaryTraceP01009.
GeneWikiAlpha_1-antitrypsin.
GenomeRNAi5265.
NextBio20336.
PMAP-CutDBP01009.
PROP01009.
SOURCESearch...

Entry information

Entry nameA1AT_HUMAN
AccessionPrimary (citable) accession number: P01009
Secondary accession number(s): A6PX14 expand/collapse secondary AC list , 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: March 19, 2014
This is version 203 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM