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P01009

- A1AT_HUMAN

UniProt

P01009 - A1AT_HUMAN

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Protein

Alpha-1-antitrypsin

Gene

SERPINA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei382 – 3832Reactive bond

GO - Molecular functioni

  1. glycoprotein binding Source: UniProt
  2. identical protein binding Source: IntAct
  3. protease binding Source: UniProtKB
  4. serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. blood coagulation Source: Reactome
  3. negative regulation of endopeptidase activity Source: RefGenome
  4. platelet activation Source: Reactome
  5. platelet degranulation Source: Reactome
  6. regulation of proteolysis Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase, Blood coagulation, Hemostasis

Protein family/group databases

MEROPSiI04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-antitrypsin
Alternative name(s):
Alpha-1 protease inhibitor
Alpha-1-antiproteinase
Serpin A1
Cleaved into the following chain:
Short peptide from AAT
Short name:
SPAAT
Gene namesi
Name:SERPINA1
Synonyms:AAT, PI
ORF Names:PRO0684, PRO2209
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:8941. SERPINA1.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi apparatus Source: UniProt
  6. platelet alpha granule lumen Source: Reactome
  7. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi382 – 3821M → V: Oxidation-resistant inhibitor of therapeutic importance. 1 Publication

Organism-specific databases

MIMi613490. phenotype.
Orphaneti60. Alpha-1-antitrypsin deficiency.
178396. Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation.
PharmGKBiPA35509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 418394Alpha-1-antitrypsin1 PublicationPRO_0000032377Add
BLAST
Peptidei375 – 41844Short peptide from AATPRO_0000364030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...) (complex)9 Publications
Glycosylationi107 – 1071N-linked (GlcNAc...) (complex)5 Publications
Modified residuei256 – 2561S-cysteinyl cysteine
Glycosylationi271 – 2711N-linked (GlcNAc...) (complex)9 Publications

Post-translational modificationi

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.11 Publications
Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP01009.
PaxDbiP01009.
PRIDEiP01009.

2D gel databases

DOSAC-COBS-2DPAGEP01009.
OGPiP01009.
REPRODUCTION-2DPAGEIPI00553177.
P01009.
SWISS-2DPAGEP01009.
UCD-2DPAGEP01009.

PTM databases

PhosphoSiteiP01009.
UniCarbKBiP01009.

Miscellaneous databases

PMAP-CutDBP01009.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in leukocytes and plasma.1 Publication

Gene expression databases

BgeeiP01009.
ExpressionAtlasiP01009. baseline and differential.
GenevestigatoriP01009.

Organism-specific databases

HPAiCAB013211.
CAB016648.
HPA000927.
HPA001292.

Interactioni

Subunit structurei

The variants S and Z interact with CANX AND PDIA3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
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

Protein-protein interaction databases

BioGridi111283. 29 interactions.
DIPiDIP-35493N.
IntActiP01009. 20 interactions.
MINTiMINT-365327.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni48 – 503Combined sources
Helixi51 – 6818Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 8912Combined sources
Helixi94 – 10310Combined sources
Turni108 – 1103Combined sources
Helixi113 – 12715Combined sources
Beta strandi135 – 14511Combined sources
Beta strandi146 – 1483Combined sources
Helixi152 – 16211Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi171 – 1733Combined sources
Helixi174 – 18815Combined sources
Turni189 – 1913Combined sources
Beta strandi206 – 22015Combined sources
Helixi224 – 2263Combined sources
Beta strandi228 – 2358Combined sources
Beta strandi238 – 25619Combined sources
Turni257 – 2604Combined sources
Beta strandi261 – 27919Combined sources
Beta strandi280 – 2823Combined sources
Helixi284 – 2907Combined sources
Helixi293 – 3019Combined sources
Beta strandi306 – 3138Combined sources
Beta strandi315 – 3228Combined sources
Helixi324 – 3296Combined sources
Helixi334 – 3363Combined sources
Turni337 – 3393Combined sources
Turni343 – 3453Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi351 – 36414Combined sources
Beta strandi366 – 38116Combined sources
Beta strandi387 – 3893Combined sources
Beta strandi394 – 4007Combined sources
Turni401 – 4033Combined sources
Beta strandi406 – 4149Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-ray3.30A25-382[»]
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-ray1.50A46-382[»]
B383-418[»]
3NDFX-ray2.70A46-382[»]
B383-418[»]
3NE4X-ray1.81A48-418[»]
3T1PX-ray3.90A48-418[»]
7APIX-ray3.00A36-382[»]
B383-418[»]
8APIX-ray3.10A36-382[»]
B383-418[»]
9APIX-ray3.00A36-382[»]
B383-418[»]
ProteinModelPortaliP01009.
SMRiP01009. Positions 48-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01009.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni368 – 39225RCLAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOVERGENiHBG005957.
InParanoidiP01009.
KOiK03984.
OMAiVVNPTQK.
OrthoDBiEOG7QC7W9.
PhylomeDBiP01009.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P01009-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI
60 70 80 90 100
TPNLAEFAFS LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI
110 120 130 140 150
LEGLNFNLTE IPEAQIHEGF QELLRTLNQP DSQLQLTTGN GLFLSEGLKL
160 170 180 190 200
VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ INDYVEKGTQ GKIVDLVKEL
210 220 230 240 250
DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV KVPMMKRLGM
260 270 280 290 300
FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL
310 320 330 340 350
ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP
360 370 380 390 400
LKLSKAVHKA VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE
410
QNTKSPLFMG KVVNPTQK
Length:418
Mass (Da):46,737
Last modified:October 1, 1996 - v3
Checksum:i7016555F273B7F16
GO
Isoform 2 (identifier: P01009-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:359
Mass (Da):40,263
Checksum:iD16A255538FB2945
GO
Isoform 3 (identifier: P01009-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:306
Mass (Da):34,755
Checksum:i15C708E6C25CE0C4
GO

Sequence cautioni

The sequence CAD62334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD62585.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121Missing in AAA51546. (PubMed:2985281)Curated
Sequence conflicti23 – 231L → P in BAG38005. (PubMed:14702039)Curated
Sequence conflicti26 – 261D → H AA sequence (PubMed:1906855)Curated
Sequence conflicti39 – 391H → L AA sequence (PubMed:1906855)Curated
Sequence conflicti61 – 611L → P in AAF29581. 1 PublicationCurated
Sequence conflicti96 – 961T → A in ABG73380. (PubMed:17650587)Curated
Sequence conflicti139 – 1402GN → DG in AAB59375. (PubMed:6319097)Curated
Sequence conflicti174 – 1741T → H in AAA51546. (PubMed:2985281)Curated
Sequence conflicti229 – 2291E → D in AAA51546. (PubMed:2985281)Curated
Sequence conflicti273 – 2731T → N in AAB59375. (PubMed:6319097)Curated
Sequence conflicti280 – 2801D → G in ABG73380. (PubMed:17650587)Curated
Sequence conflicti326 – 3261V → I in CAA25838. (PubMed:6387509)Curated
Sequence conflicti410 – 4101G → L AA sequence (PubMed:1406456)Curated
Sequence conflicti414 – 4141N → S AA sequence (PubMed:1406456)Curated

Polymorphismi

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%.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41S → L in Z-Wrexham. 1 Publication
VAR_006978
Natural varianti26 – 261D → A in V-Munich. 1 Publication
VAR_006979
Natural varianti37 – 371T → A.
Corresponds to variant rs11558262 [ dbSNP | Ensembl ].
VAR_051938
Natural varianti58 – 581A → T in M5-Karlsruhe.
VAR_006980
Natural varianti63 – 631R → C in I. 1 Publication
Corresponds to variant rs28931570 [ dbSNP | Ensembl ].
VAR_006981
Natural varianti65 – 651L → P in M-Procida. 1 Publication
Corresponds to variant rs28931569 [ dbSNP | Ensembl ].
VAR_006982
Natural varianti69 – 691S → F in M6-Bonn.
VAR_006983
Natural varianti75 – 751Missing 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. 3 Publications
VAR_006984
Natural varianti77 – 771S → F in S-Iiyama. 1 Publication
Corresponds to variant rs55819880 [ dbSNP | Ensembl ].
VAR_006985
Natural varianti84 – 841A → T in M6-Passau.
VAR_006986
Natural varianti91 – 911G → E in M-Mineral springs; causes reduced AAT secretion. 1 Publication
Corresponds to variant rs28931568 [ dbSNP | Ensembl ].
VAR_006987
Natural varianti92 – 921T → I in QO-Lisbon; deficient AAT with very low serum levels.
VAR_006988
Natural varianti109 – 1091T → M in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107. 1 Publication
VAR_011620
Natural varianti112 – 1121P → T in M5-Berlin.
VAR_006989
Natural varianti116 – 1161I → N in QO-Ludwigshafen. 1 Publication
Corresponds to variant rs28931572 [ dbSNP | Ensembl ].
VAR_006990
Natural varianti125 – 1251R → H in M2; associated with D-400.
Corresponds to variant rs709932 [ dbSNP | Ensembl ].
VAR_006991
Natural varianti139 – 1391G → S in QO-Newport. 1 Publication
Corresponds to variant rs11558261 [ dbSNP | Ensembl ].
VAR_006992
Natural varianti172 – 1721G → R in V and M-Nichinan.
VAR_006993
Natural varianti172 – 1721G → W in M2-Obernburg. 1 Publication
VAR_006994
Natural varianti180 – 1801Q → E in L-Frankfurt.
VAR_006995
Natural varianti190 – 1989QGKIVDLVK → GFQNAILVR in Aberrant form.
VAR_036746
Natural varianti228 – 2281E → K in X.
VAR_006996
Natural varianti237 – 2371V → A in M1A and Z; associated with K-366 in Z. 4 Publications
Corresponds to variant rs6647 [ dbSNP | Ensembl ].
VAR_006997
Natural varianti247 – 2471R → C in F. 1 Publication
Corresponds to variant rs28929470 [ dbSNP | Ensembl ].
VAR_006998
Natural varianti280 – 2801D → V in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona. 3 Publications
Corresponds to variant rs28929472 [ dbSNP | Ensembl ].
VAR_006999
Natural varianti288 – 2881E → V in S and T. 2 Publications
Corresponds to variant rs17580 [ dbSNP | Ensembl ].
VAR_007000
Natural varianti305 – 3051Missing in Basque. 1 Publication
VAR_009216
Natural varianti354 – 3541S → F in S-Munich.
VAR_007001
Natural varianti360 – 3601A → T in W-Bethesda. 1 Publication
Corresponds to variant rs1802959 [ dbSNP | Ensembl ].
VAR_007002
Natural varianti365 – 3651D → N in P-St.Albans/P-Donauwoerth.
VAR_007003
Natural varianti366 – 3661E → K in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z. 3 Publications
Corresponds to variant rs28929474 [ dbSNP | Ensembl ].
VAR_007004
Natural varianti382 – 3821M → R in Pittsburgh; has antithrombin activity; causes fatal bleeding diathesis.
VAR_007005
Natural varianti386 – 3861P → H in Sao Tome. 1 Publication
VAR_007006
Natural varianti386 – 3861P → T in L-Offenbach.
VAR_007007
Natural varianti387 – 3871E → K in Christchurch.
Corresponds to variant rs121912712 [ dbSNP | Ensembl ].
VAR_007008
Natural varianti393 – 3931P → L in M-Heerlen. 1 Publication
VAR_007009
Natural varianti400 – 4001E → D in M2 and M3; associated with H-125 in M2. 2 Publications
Corresponds to variant rs1303 [ dbSNP | Ensembl ].
VAR_007010
Natural varianti415 – 4151P → H in Y-Barcelona; associated with V-280. 1 Publication
VAR_007011

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei307 – 418112Missing in isoform 3. 1 PublicationVSP_028890Add
BLAST
Alternative sequencei356 – 41863AVHKA…NPTQK → VRSP in isoform 2. 1 PublicationVSP_028889Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9925.1. [P01009-1]
PIRiA21853. ITHU.
A61391.
RefSeqiNP_000286.3. NM_000295.4. [P01009-1]
NP_001002235.1. NM_001002235.2. [P01009-1]
NP_001002236.1. NM_001002236.2. [P01009-1]
NP_001121172.1. NM_001127700.1. [P01009-1]
NP_001121173.1. NM_001127701.1. [P01009-1]
NP_001121174.1. NM_001127702.1. [P01009-1]
NP_001121175.1. NM_001127703.1. [P01009-1]
NP_001121176.1. NM_001127704.1. [P01009-1]
NP_001121177.1. NM_001127705.1. [P01009-1]
NP_001121178.1. NM_001127706.1. [P01009-1]
NP_001121179.1. NM_001127707.1. [P01009-1]
UniGeneiHs.525557.

Genome annotation databases

EnsembliENST00000355814; 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]
GeneIDi5265.
KEGGihsa:5265.
UCSCiuc001ycx.4. human. [P01009-1]
uc001yda.1. human. [P01009-2]

Polymorphism databases

DMDMi1703025.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Alpha-1 antitrypsin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS9925.1. [P01009-1 ]
PIRi A21853. ITHU.
A61391.
RefSeqi NP_000286.3. NM_000295.4. [P01009-1 ]
NP_001002235.1. NM_001002235.2. [P01009-1 ]
NP_001002236.1. NM_001002236.2. [P01009-1 ]
NP_001121172.1. NM_001127700.1. [P01009-1 ]
NP_001121173.1. NM_001127701.1. [P01009-1 ]
NP_001121174.1. NM_001127702.1. [P01009-1 ]
NP_001121175.1. NM_001127703.1. [P01009-1 ]
NP_001121176.1. NM_001127704.1. [P01009-1 ]
NP_001121177.1. NM_001127705.1. [P01009-1 ]
NP_001121178.1. NM_001127706.1. [P01009-1 ]
NP_001121179.1. NM_001127707.1. [P01009-1 ]
UniGenei Hs.525557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 25-382 [» ]
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 [» ]
3NDD X-ray 1.50 A 46-382 [» ]
B 383-418 [» ]
3NDF X-ray 2.70 A 46-382 [» ]
B 383-418 [» ]
3NE4 X-ray 1.81 A 48-418 [» ]
3T1P X-ray 3.90 A 48-418 [» ]
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 [» ]
ProteinModelPortali P01009.
SMRi P01009. Positions 48-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111283. 29 interactions.
DIPi DIP-35493N.
IntActi P01009. 20 interactions.
MINTi MINT-365327.

Protein family/group databases

MEROPSi I04.001.

PTM databases

PhosphoSitei P01009.
UniCarbKBi P01009.

Polymorphism databases

DMDMi 1703025.

2D gel databases

DOSAC-COBS-2DPAGE P01009.
OGPi P01009.
REPRODUCTION-2DPAGE IPI00553177.
P01009.
SWISS-2DPAGE P01009.
UCD-2DPAGE P01009.

Proteomic databases

MaxQBi P01009.
PaxDbi P01009.
PRIDEi P01009.

Protocols and materials databases

DNASUi 5265.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355814 ; 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 ]
GeneIDi 5265.
KEGGi hsa:5265.
UCSCi uc001ycx.4. human. [P01009-1 ]
uc001yda.1. human. [P01009-2 ]

Organism-specific databases

CTDi 5265.
GeneCardsi GC14M094843.
GeneReviewsi SERPINA1.
HGNCi HGNC:8941. SERPINA1.
HPAi CAB013211.
CAB016648.
HPA000927.
HPA001292.
MIMi 107400. gene.
613490. phenotype.
neXtProti NX_P01009.
Orphaneti 60. Alpha-1-antitrypsin deficiency.
178396. Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation.
PharmGKBi PA35509.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOVERGENi HBG005957.
InParanoidi P01009.
KOi K03984.
OMAi VVNPTQK.
OrthoDBi EOG7QC7W9.
PhylomeDBi P01009.
TreeFami TF343201.

Miscellaneous databases

ChiTaRSi SERPINA1. human.
EvolutionaryTracei P01009.
GeneWikii Alpha_1-antitrypsin.
GenomeRNAii 5265.
NextBioi 20336.
PMAP-CutDB P01009.
PROi P01009.
SOURCEi Search...

Gene expression databases

Bgeei P01009.
ExpressionAtlasi P01009. baseline and differential.
Genevestigatori P01009.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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, IDENTIFICATION BY 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), IDENTIFICATION BY 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. 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. 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. 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. 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, IDENTIFICATION BY 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. 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. Cited for: VARIANTS Z ALA-237 AND LYS-366, VARIANT S VAL-288, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH CANX AND PDIA3.

Entry informationi

Entry nameiA1AT_HUMAN
AccessioniPrimary (citable) accession number: P01009
Secondary accession number(s): A6PX14
, B2RDQ8, Q0PVP5, Q13672, Q53XB8, Q5U0M1, Q7M4R2, Q86U18, Q86U19, Q96BF9, Q96ES1, Q9P1P0, Q9UCE6, Q9UCM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 211 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3