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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)DescriptionActionsGraphical viewLength
Sitei382 – 383Reactive bond2

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

BioCyciZFISH:G66-32386-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
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)DescriptionActionsGraphical viewLength
Mutagenesisi382M → V: Oxidation-resistant inhibitor of therapeutic importance. 1 Publication1

Organism-specific databases

DisGeNETi5265.
MalaCardsiSERPINA1.
MIMi613490. phenotype.
OpenTargetsiENSG00000197249.
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000003237725 – 418Alpha-1-antitrypsin1 PublicationAdd BLAST394
PeptideiPRO_0000364030375 – 418Short peptide from AATAdd BLAST44

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38Phosphoserine; by FAM20C1 Publication1
Glycosylationi70N-linked (GlcNAc...) (complex)9 Publications1
Glycosylationi107N-linked (GlcNAc...) (complex)5 Publications1
Modified residuei256S-cysteinyl cysteine1
Glycosylationi271N-linked (GlcNAc...) (complex)9 Publications1
Modified residuei383PhosphoserineCombined sources1

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.
PhosphoSitePlusiP01009.
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

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

Protein-protein interaction databases

BioGridi111283. 37 interactors.
DIPiDIP-35493N.
IntActiP01009. 20 interactors.
MINTiMINT-365327.
STRINGi9606.ENSP00000348068.

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni48 – 50Combined sources3
Helixi51 – 68Combined sources18
Beta strandi70 – 72Combined sources3
Beta strandi74 – 76Combined sources3
Helixi78 – 89Combined sources12
Helixi94 – 103Combined sources10
Turni108 – 110Combined sources3
Helixi113 – 127Combined sources15
Beta strandi135 – 145Combined sources11
Beta strandi146 – 148Combined sources3
Helixi152 – 162Combined sources11
Beta strandi164 – 169Combined sources6
Beta strandi171 – 173Combined sources3
Helixi174 – 188Combined sources15
Turni189 – 191Combined sources3
Beta strandi206 – 220Combined sources15
Helixi224 – 226Combined sources3
Beta strandi228 – 235Combined sources8
Beta strandi238 – 256Combined sources19
Turni257 – 260Combined sources4
Beta strandi261 – 279Combined sources19
Beta strandi280 – 282Combined sources3
Helixi284 – 290Combined sources7
Helixi293 – 301Combined sources9
Beta strandi306 – 313Combined sources8
Beta strandi315 – 322Combined sources8
Helixi324 – 329Combined sources6
Helixi334 – 336Combined sources3
Turni337 – 339Combined sources3
Turni343 – 345Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi351 – 364Combined sources14
Beta strandi366 – 381Combined sources16
Beta strandi387 – 389Combined sources3
Beta strandi394 – 400Combined sources7
Turni401 – 403Combined sources3
Beta strandi406 – 414Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01009.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni368 – 392RCLAdd BLAST25

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)DescriptionActionsGraphical viewLength
Sequence conflicti12Missing in AAA51546 (PubMed:2985281).Curated1
Sequence conflicti23L → P in BAG38005 (PubMed:14702039).Curated1
Sequence conflicti26D → H AA sequence (PubMed:1906855).Curated1
Sequence conflicti39H → L AA sequence (PubMed:1906855).Curated1
Sequence conflicti61L → P in AAF29581 (Ref. 8) Curated1
Sequence conflicti96T → A in ABG73380 (PubMed:17650587).Curated1
Sequence conflicti139 – 140GN → DG in AAB59375 (PubMed:6319097).Curated2
Sequence conflicti174T → H in AAA51546 (PubMed:2985281).Curated1
Sequence conflicti229E → D in AAA51546 (PubMed:2985281).Curated1
Sequence conflicti273T → N in AAB59375 (PubMed:6319097).Curated1
Sequence conflicti280D → G in ABG73380 (PubMed:17650587).Curated1
Sequence conflicti326V → I in CAA25838 (PubMed:6387509).Curated1
Sequence conflicti410G → L AA sequence (PubMed:1406456).Curated1
Sequence conflicti414N → S AA sequence (PubMed:1406456).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0069784S → L in Z-Wrexham. 1 Publication1
Natural variantiVAR_00697926D → A in V-Munich. 1 PublicationCorresponds to variant rs199422212dbSNPEnsembl.1
Natural variantiVAR_05193837T → A.Corresponds to variant rs11558262dbSNPEnsembl.1
Natural variantiVAR_00698058A → T in M5-Karlsruhe. Corresponds to variant rs149319176dbSNPEnsembl.1
Natural variantiVAR_00698163R → C in I. 1 PublicationCorresponds to variant rs28931570dbSNPEnsembl.1
Natural variantiVAR_00698265L → P in M-Procida. 1 PublicationCorresponds to variant rs28931569dbSNPEnsembl.1
Natural variantiVAR_00698369S → F in M6-Bonn. Corresponds to variant rs199687431dbSNPEnsembl.1
Natural variantiVAR_00698475Missing 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 Publications1
Natural variantiVAR_00698577S → F in S-Iiyama. 1 PublicationCorresponds to variant rs55819880dbSNPEnsembl.1
Natural variantiVAR_00698684A → T in M6-Passau. Corresponds to variant rs111850950dbSNPEnsembl.1
Natural variantiVAR_00698791G → E in M-Mineral springs; causes reduced AAT secretion. 1 PublicationCorresponds to variant rs28931568dbSNPEnsembl.1
Natural variantiVAR_00698892T → I in QO-Lisbon; deficient AAT with very low serum levels. 1
Natural variantiVAR_011620109T → M in Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107. 1 PublicationCorresponds to variant rs199422213dbSNPEnsembl.1
Natural variantiVAR_006989112P → T in M5-Berlin. 1
Natural variantiVAR_006990116I → N in QO-Ludwigshafen. 1 PublicationCorresponds to variant rs28931572dbSNPEnsembl.1
Natural variantiVAR_006991125R → H in M2; associated with D-400. Corresponds to variant rs709932dbSNPEnsembl.1
Natural variantiVAR_006992139G → S in QO-Newport. 1 PublicationCorresponds to variant rs11558261dbSNPEnsembl.1
Natural variantiVAR_006993172G → R in V and M-Nichinan. Corresponds to variant rs112030253dbSNPEnsembl.1
Natural variantiVAR_006994172G → W in M2-Obernburg. 1 PublicationCorresponds to variant rs112030253dbSNPEnsembl.1
Natural variantiVAR_006995180Q → E in L-Frankfurt. 1
Natural variantiVAR_036746190 – 198QGKIVDLVK → GFQNAILVR in Aberrant form. 9
Natural variantiVAR_006996228E → K in X. Corresponds to variant rs199422208dbSNPEnsembl.1
Natural variantiVAR_006997237V → A in M1A and Z; associated with K-366 in Z. 4 PublicationsCorresponds to variant rs6647dbSNPEnsembl.1
Natural variantiVAR_006998247R → C in F. 1 PublicationCorresponds to variant rs28929470dbSNPEnsembl.1
Natural variantiVAR_006999280D → V in P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona. 3 PublicationsCorresponds to variant rs28929472dbSNPEnsembl.1
Natural variantiVAR_007000288E → V in S and T. 2 PublicationsCorresponds to variant rs17580dbSNPEnsembl.1
Natural variantiVAR_009216305Missing in Basque. 1 Publication1
Natural variantiVAR_007001354S → F in S-Munich. Corresponds to variant rs201788603dbSNPEnsembl.1
Natural variantiVAR_007002360A → T in W-Bethesda. 1 PublicationCorresponds to variant rs1802959dbSNPEnsembl.1
Natural variantiVAR_007003365D → N in P-St.Albans/P-Donauwoerth. Corresponds to variant rs143370956dbSNPEnsembl.1
Natural variantiVAR_007004366E → K in Z/Z-Augsburg/Z-Tun; associated with A-237 in Z. 3 PublicationsCorresponds to variant rs28929474dbSNPEnsembl.1
Natural variantiVAR_007005382M → R in Pittsburgh; has antithrombin activity; causes fatal bleeding diathesis. 1 PublicationCorresponds to variant rs121912713dbSNPEnsembl.1
Natural variantiVAR_007006386P → H in Sao Tome. 1 Publication1
Natural variantiVAR_007007386P → T in L-Offenbach. Corresponds to variant rs12233dbSNPEnsembl.1
Natural variantiVAR_007008387E → K in Christchurch. Corresponds to variant rs121912712dbSNPEnsembl.1
Natural variantiVAR_007009393P → L in M-Heerlen. 1 PublicationCorresponds to variant rs199422209dbSNPEnsembl.1
Natural variantiVAR_007010400E → D in M2 and M3; associated with H-125 in M2. 2 PublicationsCorresponds to variant rs1303dbSNPEnsembl.1
Natural variantiVAR_007011415P → H in Y-Barcelona; associated with V-280. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_028890307 – 418Missing in isoform 3. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_028889356 – 418AVHKA…NPTQK → VRSP in isoform 2. 1 PublicationAdd BLAST63

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]
XP_016876859.1. XM_017021370.1. [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]
ENST00000636712; ENSP00000490054; ENSG00000197249. [P01009-1]
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]
XP_016876859.1. XM_017021370.1. [P01009-1]
UniGeneiHs.525557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111283. 37 interactors.
DIPiDIP-35493N.
IntActiP01009. 20 interactors.
MINTiMINT-365327.
STRINGi9606.ENSP00000348068.

Protein family/group databases

MEROPSiI04.001.

PTM databases

iPTMnetiP01009.
PhosphoSitePlusiP01009.
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]
ENST00000636712; ENSP00000490054; ENSG00000197249. [P01009-1]
GeneIDi5265.
KEGGihsa:5265.
UCSCiuc001ycx.5. human. [P01009-1]

Organism-specific databases

CTDi5265.
DisGeNETi5265.
GeneCardsiSERPINA1.
GeneReviewsiSERPINA1.
HGNCiHGNC:8941. SERPINA1.
HPAiCAB013211.
CAB016648.
CAB073396.
HPA000927.
HPA001292.
MalaCardsiSERPINA1.
MIMi107400. gene.
613490. phenotype.
neXtProtiNX_P01009.
OpenTargetsiENSG00000197249.
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

BioCyciZFISH:G66-32386-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
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: November 30, 2016
This is version 232 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.