SERPINA1
entrez
5265
canonical
uniprot
P01009
canonical
ensembl
ENSG00000197249
resolver
ensembl
ENSG00000277377
resolver
ensp
ENSP00000348068
resolver
ensp
ENSP00000376802
resolver
ensp
ENSP00000376803
resolver
ensp
ENSP00000385960
resolver
ensp
ENSP00000390299
resolver
ensp
ENSP00000408474
resolver
ensp
ENSP00000416066
resolver
ensp
ENSP00000416354
resolver
ensp
ENSP00000477615
resolver
ensp
ENSP00000479923
resolver
ensp
ENSP00000480231
resolver
ensp
ENSP00000485908
resolver
ensp
ENSP00000486067
resolver
ensp
ENSP00000486302
resolver
ensp
ENSP00000486957
resolver
ensp
ENSP00000487579
resolver
ensp
ENSP00000536573
resolver
ensp
ENSP00000536579
resolver
ensp
ENSP00000536583
resolver
enst
ENST00000614317
resolver
enst
ENST00000618636
resolver
enst
ENST00000620666
resolver
enst
ENST00000627096
resolver
enst
ENST00000627097
resolver
enst
ENST00000627178
resolver
enst
ENST00000627595
resolver
enst
ENST00000628155
resolver
genesymbol
SERPINA1
resolver
genesymbol_syn
AAT
resolver
genesymbol_syn
PI
resolver
hgnc
HGNC:8941
resolver
uniprot
A0A024R6N5
resolver
uniprot
A0A384MDQ7
resolver
uniprot
A6PX14
resolver
uniprot
B2RDQ8
resolver
uniprot
E9KL23
resolver
uniprot
Q0PVP5
resolver
uniprot
Q13672
resolver
uniprot
Q53XB8
resolver
uniprot
Q5U0M1
resolver
uniprot
Q7M4R2
resolver
uniprot
Q86U18
resolver
uniprot
Q86U19
resolver
uniprot
Q96BF9
resolver
uniprot
Q96ES1
resolver
uniprot
Q9P1P0
resolver
uniprot
Q9UCE6
resolver
uniprot
Q9UCM3
resolver
uniprot_entry
A0A024R6N5_HUMAN
resolver
uniprot_entry
A0A384MDQ7_HUMAN
resolver
uniprot_entry
A1AT_HUMAN
resolver
uniprot_entry
E9KL23_HUMAN
resolver
uniprot_sec
A6PX14
resolver
uniprot_sec
B2RDQ8
resolver
uniprot_sec
Q0PVP5
resolver
uniprot_sec
Q13672
resolver
uniprot_sec
Q53XB8
resolver
uniprot_sec
Q5U0M1
resolver
uniprot_sec
Q7M4R2
resolver
uniprot_sec
Q86U18
resolver
uniprot_sec
Q86U19
resolver
uniprot_sec
Q96BF9
resolver
uniprot_sec
Q96ES1
resolver
uniprot_sec
Q9P1P0
resolver
uniprot_sec
Q9UCE6
resolver
uniprot_sec
Q9UCM3
resolver
amino_acid_sequence
MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
uniprot
proteins
disease_involvement
DISEASE: Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: An autosomal recessive disorder characterized by serum levels of alpha-1-antitrypsin below the normal range, and an increased risk for developing pulmonary emphysema and, to a lesser extent, chronic liver disease. Environmental factors, particularly cigarette smoking, greatly increase the risk of emphysema at an earlier age. {ECO:0000269|PubMed:10651487, ECO:0000269|PubMed:1608473, ECO:0000269|PubMed:1905728, ECO:0000269|PubMed:1967187, ECO:0000269|PubMed:2227940, ECO:0000269|PubMed:2254451, ECO:0000269|PubMed:2309708, ECO:0000269|PubMed:2339709, ECO:0000269|PubMed:2390072, ECO:0000269|PubMed:25181470, ECO:0000269|PubMed:2606478, ECO:0000269|PubMed:2784123, ECO:0000269|PubMed:2786335, ECO:0000269|PubMed:3262617, ECO:0000269|PubMed:7977369, ECO:0000269|PubMed:8364590, ECO:0000269|PubMed:9569237}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.; FUNCTION: [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).
uniprot
proteins
mass_dalton
46737
uniprot
proteins
mutagenesis
MUTAGEN 382; /note="M->V: Oxidation-resistant inhibitor of therapeutic importance."; /evidence="ECO:0000269|PubMed:6387509
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16622833, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23826168}.; PTM: Proteolytic processing may yield the truncated form that ranges from Asp-30 to Lys-418.; PTM: (Microbial infection) Proteolytically processed by Staphylococcus aureus seryl, cysteinyl, and metallo-proteases. {ECO:0000269|PubMed:3533918}.
uniprot
proteins
protein_family
Serpin family
uniprot
proteins
pubmed
10612848
uniprot
proteins
pubmed
10651487
uniprot
proteins
pubmed
10716194
uniprot
proteins
pubmed
10933492
uniprot
proteins
pubmed
11057674
uniprot
proteins
pubmed
11178897
uniprot
proteins
pubmed
12244055
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
12860985
uniprot
proteins
pubmed
1406456
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
15084671
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1608473
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16622833
uniprot
proteins
pubmed
17650587
uniprot
proteins
pubmed
1859394
uniprot
proteins
pubmed
1905728
uniprot
proteins
pubmed
1906855
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
1967187
uniprot
proteins
pubmed
19838169
uniprot
proteins
pubmed
2035534
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
2227940
uniprot
proteins
pubmed
2254451
uniprot
proteins
pubmed
2309708
uniprot
proteins
pubmed
2316526
uniprot
proteins
pubmed
2339709
uniprot
proteins
pubmed
23826168
uniprot
proteins
pubmed
2390072
uniprot
proteins
pubmed
2394452
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25181470
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2606478
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
2669992
uniprot
proteins
pubmed
26797521
uniprot
proteins
pubmed
2784123
uniprot
proteins
pubmed
2785270
uniprot
proteins
pubmed
2786335
uniprot
proteins
pubmed
2901226
uniprot
proteins
pubmed
2985281
uniprot
proteins
pubmed
31142615
uniprot
proteins
pubmed
31358993
uniprot
proteins
pubmed
3262617
uniprot
proteins
pubmed
3491072
uniprot
proteins
pubmed
3533918
uniprot
proteins
pubmed
3873938
uniprot
proteins
pubmed
3876243
uniprot
proteins
pubmed
6093867
uniprot
proteins
pubmed
6319097
uniprot
proteins
pubmed
6332197
uniprot
proteins
pubmed
6387509
uniprot
proteins
pubmed
6604220
uniprot
proteins
pubmed
6979715
uniprot
proteins
pubmed
7031661
uniprot
proteins
pubmed
7045697
uniprot
proteins
pubmed
7977369
uniprot
proteins
pubmed
8323530
uniprot
proteins
pubmed
8364590
uniprot
proteins
pubmed
8543039
uniprot
proteins
pubmed
8756325
uniprot
proteins
pubmed
8939743
uniprot
proteins
pubmed
9459000
uniprot
proteins
pubmed
9466920
uniprot
proteins
pubmed
9569237
uniprot
proteins
sequence_length
418
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum. Note=The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum.; SUBCELLULAR LOCATION: [Short peptide from AAT]: Secreted, extracellular space, extracellular matrix.
uniprot
proteins