Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-1-antitrypsin

Gene

SERPINA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • glycoprotein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protease binding Source: UniProtKB
  • serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase, Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
SIGNORiP01009.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:8941. SERPINA1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • ER to Golgi transport vesicle Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: GOC
  • platelet alpha granule lumen Source: Reactome
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Alpha-1-antitrypsin deficiency (A1ATD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613490

Mutagenesis

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

Organism-specific databases

MalaCardsiSERPINA1.
MIMi613490. phenotype.
Orphaneti60. Alpha-1-antitrypsin deficiency.
178396. Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation.
PharmGKBiPA35509.

Polymorphism and mutation databases

BioMutaiSERPINA1.
DMDMi1703025.

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
Modified residuei38 – 381Phosphoserine; by FAM20C1 Publication
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
Modified residuei383 – 3831PhosphoserineCombined sources

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, Phosphoprotein

Proteomic databases

EPDiP01009.
MaxQBiP01009.
PaxDbiP01009.
PeptideAtlasiP01009.
PRIDEiP01009.

2D gel databases

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

PTM databases

iPTMnetiP01009.
PhosphoSiteiP01009.
UniCarbKBiP01009.

Miscellaneous databases

PMAP-CutDBP01009.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in leukocytes and plasma.1 Publication

Gene expression databases

BgeeiENSG00000197249.
ExpressionAtlasiP01009. baseline and differential.
GenevisibleiP01009. HS.

Organism-specific databases

HPAiCAB013211.
CAB016648.
CAB073396.
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

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protease binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111283. 36 interactions.
DIPiDIP-35493N.
IntActiP01009. 20 interactions.
MINTiMINT-365327.
STRINGi9606.ENSP00000348068.

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[»]
4PYWX-ray1.91A26-418[»]
5IO1X-ray3.34A/B29-418[»]
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

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118839.
HOVERGENiHBG005957.
InParanoidiP01009.
KOiK03984.
OMAiNITEMSE.
OrthoDBiEOG091G0ION.
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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAD62585 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 (Ref. 8) Curated
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%.1 Publication

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
Corresponds to variant rs199422212 [ dbSNP | Ensembl ].
VAR_006979
Natural varianti37 – 371T → A.
Corresponds to variant rs11558262 [ dbSNP | Ensembl ].
VAR_051938
Natural varianti58 – 581A → T in M5-Karlsruhe.
Corresponds to variant rs149319176 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs199687431 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs111850950 [ dbSNP | Ensembl ].
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
Corresponds to variant rs199422213 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs112030253 [ dbSNP | Ensembl ].
VAR_006993
Natural varianti172 – 1721G → W in M2-Obernburg. 1 Publication
Corresponds to variant rs112030253 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs199422208 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs201788603 [ dbSNP | Ensembl ].
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.
Corresponds to variant rs143370956 [ dbSNP | Ensembl ].
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. 1 Publication
Corresponds to variant rs121912713 [ dbSNP | Ensembl ].
VAR_007005
Natural varianti386 – 3861P → H in Sao Tome. 1 Publication
VAR_007006
Natural varianti386 – 3861P → T in L-Offenbach.
Corresponds to variant rs12233 [ dbSNP | Ensembl ].
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
Corresponds to variant rs199422209 [ dbSNP | Ensembl ].
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.5. human. [P01009-1]

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.
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.

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[»]
4PYWX-ray1.91A26-418[»]
5IO1X-ray3.34A/B29-418[»]
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...

Protein-protein interaction databases

BioGridi111283. 36 interactions.
DIPiDIP-35493N.
IntActiP01009. 20 interactions.
MINTiMINT-365327.
STRINGi9606.ENSP00000348068.

Protein family/group databases

MEROPSiI04.001.

PTM databases

iPTMnetiP01009.
PhosphoSiteiP01009.
UniCarbKBiP01009.

Polymorphism and mutation databases

BioMutaiSERPINA1.
DMDMi1703025.

2D gel databases

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

Proteomic databases

EPDiP01009.
MaxQBiP01009.
PaxDbiP01009.
PeptideAtlasiP01009.
PRIDEiP01009.

Protocols and materials databases

DNASUi5265.
Structural Biology KnowledgebaseSearch...

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.5. human. [P01009-1]

Organism-specific databases

CTDi5265.
GeneCardsiSERPINA1.
GeneReviewsiSERPINA1.
HGNCiHGNC:8941. SERPINA1.
HPAiCAB013211.
CAB016648.
CAB073396.
HPA000927.
HPA001292.
MalaCardsiSERPINA1.
MIMi107400. gene.
613490. phenotype.
neXtProtiNX_P01009.
Orphaneti60. Alpha-1-antitrypsin deficiency.
178396. Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation.
PharmGKBiPA35509.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00760000118839.
HOVERGENiHBG005957.
InParanoidiP01009.
KOiK03984.
OMAiNITEMSE.
OrthoDBiEOG091G0ION.
PhylomeDBiP01009.
TreeFamiTF343201.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
SIGNORiP01009.

Miscellaneous databases

ChiTaRSiSERPINA1. human.
EvolutionaryTraceiP01009.
GeneWikiiAlpha_1-antitrypsin.
GenomeRNAii5265.
PMAP-CutDBP01009.
PROiP01009.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197249.
ExpressionAtlasiP01009. baseline and differential.
GenevisibleiP01009. HS.

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]
ProtoNetiSearch...

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: September 7, 2016
This is version 229 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.