Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01011 (AACT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 177. Feed History...

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

Names and origin

Protein namesRecommended name:
Alpha-1-antichymotrypsin

Short name=ACT
Alternative name(s):
Cell growth-inhibiting gene 24/25 protein
Serpin A3

Cleaved into the following chain:

  1. Alpha-1-antichymotrypsin His-Pro-less
Gene names
Name:SERPINA3
Synonyms:AACT
ORF Names:GIG24, GIG25
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. Ref.14

Subunit structure

Interacts with DNAJC1. Ref.18

Subcellular location

Secreted.

Tissue specificity

Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the amyloid plaques from the hippocampus of Alzheimer disease brains. Ref.7 Ref.8

Domain

The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

Post-translational modification

N- and O-glycosylated. Ref.17 Ref.23

Miscellaneous

Alpha-1-antichymotrypsin can bind DNA.

Sequence similarities

Belongs to the serpin family.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence caution

The sequence AAA51543.1 differs from that shown. Reason: Frameshift at positions 101, 106, 111, 117, 123, 129 and 421.

The sequence AAT08029.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAT08029.1 differs from that shown. Reason: Frameshift at position 4.

The sequence BAD92297.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA48671.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAcute phase
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Non-traceable author statement PubMed 12475184. Source: UniProtKB

maintenance of gastrointestinal epithelium

Non-traceable author statement Ref.13. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of lipid metabolic process

Non-traceable author statement PubMed 11835318. Source: UniProtKB

regulation of proteolysis

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular region

Non-traceable author statement PubMed 14718574Ref.13Ref.8. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

intracellular

Non-traceable author statement Ref.8. Source: UniProtKB

nucleus

Traceable author statement Ref.18. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.18. Source: UniProtKB

serine-type endopeptidase inhibitor activity

Traceable author statement Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DNAJC1Q96KC83EBI-296557,EBI-296550

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01011-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P01011-2)

The sequence of this isoform differs from the canonical sequence as follows:
     215-216: AK → ER
     217-423: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P01011-3)

The sequence of this isoform differs from the canonical sequence as follows:
     64-95: LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT → SPRWSIRLCLMYLRRAQKHLLPQQSKSPSFLH
     96-423: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.10
Chain24 – 423400Alpha-1-antichymotrypsin
PRO_0000032411
Chain26 – 423398Alpha-1-antichymotrypsin His-Pro-less
PRO_0000032412

Regions

DNA binding235 – 2373
Region369 – 39426RCL
Region381 – 3899O-glycosylated at one site

Sites

Site383 – 3842Reactive bond

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Ref.21
Glycosylation931N-linked (GlcNAc...) Ref.17 Ref.20 Ref.21 Ref.22
Glycosylation1061N-linked (GlcNAc...) Ref.17 Ref.21 Ref.22
Glycosylation1271N-linked (GlcNAc...) Ref.21 Ref.22
Glycosylation1861N-linked (GlcNAc...) Ref.21
Glycosylation2711N-linked (GlcNAc...) Ref.21 Ref.22

Natural variations

Alternative sequence64 – 9532LVLKA…AHNTT → SPRWSIRLCLMYLRRAQKHL LPQQSKSPSFLH in isoform 3.
VSP_014225
Alternative sequence96 – 423328Missing in isoform 3.
VSP_014226
Alternative sequence215 – 2162AK → ER in isoform 2.
VSP_014227
Alternative sequence217 – 423207Missing in isoform 2.
VSP_014228
Natural variant91A → T. Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs4934 [ dbSNP | Ensembl ].
VAR_006973
Natural variant781L → P in Bochum-1. Ref.2
Corresponds to variant rs1800463 [ dbSNP | Ensembl ].
VAR_006974
Natural variant1671A → G.
VAR_006975
Natural variant2521P → A in Bonn-1. Ref.2 Ref.29
Corresponds to variant rs17473 [ dbSNP | Ensembl ].
VAR_006976
Natural variant2671K → R. Ref.6
Corresponds to variant rs17853314 [ dbSNP | Ensembl ].
VAR_037902
Natural variant4011M → V Associated with occlusive-cerebrovascular disease; Isehara-1. Ref.28 Ref.30
VAR_006977
Natural variant4071D → G.
Corresponds to variant rs10956 [ dbSNP | Ensembl ].
VAR_011742

Experimental info

Sequence conflict551D → S AA sequence Ref.12
Sequence conflict691P → L in AAA51543. Ref.1
Sequence conflict1011K → R in BAD92297. Ref.5
Sequence conflict1061N → Y in AAT08028. Ref.3
Sequence conflict1981D → N in AAT08029. Ref.3
Sequence conflict1991L → P in AAA51543. Ref.1
Sequence conflict2341S → N in AAT08029. Ref.3
Sequence conflict3391S → G in AAT08028. Ref.3
Sequence conflict3461I → S in AAT08028. Ref.3
Sequence conflict361 – 3633AVL → VVS in AAA51543. Ref.1

Secondary structure

............................................................... 423
Helix Strand Turn

Details...

Sequences

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

Last modified August 1, 1991. Version 2.
Checksum: B002F946C86A8951

FASTA42347,651
        10         20         30         40         50         60 
MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL 

        70         80         90        100        110        120 
YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ 

       130        140        150        160        170        180 
HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI 

       190        200        210        220        230        240 
NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM 

       250        260        270        280        290        300 
VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR 

       310        320        330        340        350        360 
DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK 

       370        380        390        400        410        420 
AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP 


KQA 

« Hide

Isoform 2 [UniParc].

Checksum: 49312EDF91439D4D
Show »

FASTA21624,034
Isoform 3 [UniParc].

Checksum: 15B1759843F9809B
Show »

FASTA9510,717

References

« Hide 'large scale' references
[1]"Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III."
Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.
Biochemistry 22:5055-5061(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease."
Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M., Olek K., Kirchgesser M., Heidtmann H.-H.
Genomics 17:740-743(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS BOCHUM-1 PRO-78 AND BONN-1 ALA-252.
[3]"Identification of a human cell growth inhibiting gene."
Kim J.W.
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-9.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-9.
Tissue: Urinary bladder.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-9.
Tissue: Brain.
[6]"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] (ISOFORMS 1 AND 3), VARIANTS THR-9 AND ARG-267.
Tissue: Brain, Liver and Skin.
[7]"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease."
Abraham C.R., Selkoe D.J., Potter H.
Cell 52:487-501(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, TISSUE SPECIFICITY.
Tissue: Liver.
[8]"Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver."
Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.
J. Biol. Chem. 274:1821-1827(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Hippocampus.
[9]Rubin H.
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1).
[10]"The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide."
Lindmark B., Hilja H., Alan R., Eriksson S.
Biochim. Biophys. Acta 997:90-95(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-34.
[11]"Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose."
Korzus E., Luisetti M., Travis J.
Biol. Chem. Hoppe-Seyler 375:335-341(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-45.
[12]"Structural alterations in alpha 1-antichymotrypsin from normal and acute phase human plasma."
Morii M., Travis J.
Biochem. Biophys. Res. Commun. 111:438-443(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-60.
[13]"Characterisation of the tumour-associated carbohydrate epitope recognised by monoclonal antibody 4D3."
Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C., Preston B.N., Linnane A.W.
Int. J. Cancer 66:636-644(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2).
[14]"Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins."
Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N., Schoenberger O.L., Johnson J.L., Cooperman B.S.
J. Biol. Chem. 265:1199-1207(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), FUNCTION.
Tissue: Liver.
[15]"Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions."
Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.
Nature 311:175-177(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423.
[16]"Amino acid sequence at the reactive site of human alpha 1-antichymotrypsin."
Morii M., Travis J.
J. Biol. Chem. 258:12749-12752(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: REACTIVE SITE.
[17]"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-93 AND ASN-106.
[18]"The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity."
Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., Blond S.Y.
J. Biol. Chem. 279:11432-11443(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJC1.
[19]"Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus."
Horvath A.J., Forsyth S.L., Coughlin P.B.
J. Mol. Evol. 59:488-497(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REGION RCL.
[20]"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-93.
Tissue: Plasma.
[21]"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-33; ASN-93; ASN-106; ASN-127; ASN-186 AND ASN-271.
Tissue: Plasma.
[22]"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-93; ASN-106; ASN-127 AND ASN-271.
Tissue: Liver.
[23]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
[24]"Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A resolution and its comparison with other serpins."
Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.
J. Mol. Biol. 218:595-606(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423.
[25]"Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement."
Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S., Christianson D.W.
Nat. Struct. Biol. 3:888-893(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 AND ARG-372.
[26]"Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction."
Lukacs C.M., Rubin H., Christianson D.W.
Biochemistry 37:3297-3304(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; ARG-372 AND ARG-374.
[27]"Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease."
Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W., Read R.J., Lomas D.A.
Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423.
[28]"Detection of a new mutant alpha-1-antichymotrypsin in patients with occlusive-cerebrovascular disease."
Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.
FEBS Lett. 304:66-68(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ISEHARA-1 VAL-401.
[29]"Mis-sense mutation of alpha 1-antichymotrypsin gene associated with chronic lung disease."
Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K., Olek K., Eriksson S.
Lancet 339:1538-1538(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BONN-1 ALA-252.
[30]"Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is associated with a lacunar type of ischemic cerebrovascular disease."
Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.
J. Hum. Genet. 46:45-47(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-401.
+Additional computationally mapped references.

Web resources

Wikipedia

Alpha-1 antichymotrypsin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01500 mRNA. Translation: AAA51543.1. Frameshift.
X68733 expand/collapse EMBL AC list , X68734, X68735, X68736, X68737 Genomic DNA. Translation: CAA48671.1. Different initiation.
AY513275 mRNA. Translation: AAT08028.1.
AY513276 mRNA. Translation: AAT08029.1. Sequence problems.
AK123091 mRNA. Translation: BAG53869.1.
AB209060 mRNA. Translation: BAD92297.1. Different initiation.
BC003559 mRNA. Translation: AAH03559.3.
BC010530 mRNA. Translation: AAH10530.1.
BC013189 mRNA. Translation: AAH13189.1.
BC034554 mRNA. Translation: AAH34554.1.
BC070265 mRNA. Translation: AAH70265.1.
M18906 mRNA. Translation: AAA51559.1.
AF089747 mRNA. Translation: AAD08810.1.
J05176 mRNA. Translation: AAA51560.1.
X00947 Genomic DNA. Translation: CAA25459.1.
PIRITHUC. A90475.
S62374.
RefSeqNP_001076.2. NM_001085.4.
UniGeneHs.534293.
Hs.710488.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AS4X-ray2.10A43-383[»]
B387-423[»]
1QMNX-ray2.27A26-423[»]
2ACHX-ray2.70A24-383[»]
B384-423[»]
3CAAX-ray2.40A43-383[»]
B387-423[»]
3DLWX-ray2.70A25-423[»]
4CAAX-ray2.90A43-383[»]
B387-423[»]
ProteinModelPortalP01011.
SMRP01011. Positions 48-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106530. 11 interactions.
IntActP01011. 10 interactions.

Chemistry

ChEMBLCHEMBL5960.

Protein family/group databases

MEROPSI04.002.

PTM databases

PhosphoSiteP01011.
UniCarbKBP01011.

Polymorphism databases

DMDM112874.

2D gel databases

DOSAC-COBS-2DPAGEP01011.
SWISS-2DPAGEP01011.

Proteomic databases

PaxDbP01011.
PRIDEP01011.

Protocols and materials databases

DNASU12.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393078; ENSP00000376793; ENSG00000196136. [P01011-1]
ENST00000393080; ENSP00000376795; ENSG00000196136. [P01011-1]
ENST00000467132; ENSP00000450540; ENSG00000196136. [P01011-1]
ENST00000556968; ENSP00000452476; ENSG00000196136. [P01011-2]
GeneID12.
KEGGhsa:12.
UCSCuc001ydp.3. human. [P01011-1]
uc021sbb.2. human. [P01011-3]

Organism-specific databases

CTD12.
GeneCardsGC14P095078.
H-InvDBHIX0079611.
HGNCHGNC:16. SERPINA3.
HPACAB016647.
HPA000893.
HPA002560.
MIM107280. gene.
neXtProtNX_P01011.
Orphanet93594. Alpha-1-antichymotrypsin deficiency.
PharmGKBPA35020.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOVERGENHBG005957.
InParanoidP01011.
KOK04525.
PhylomeDBP01011.
TreeFamTF343201.

Gene expression databases

ArrayExpressP01011.
BgeeP01011.
GenevestigatorP01011.

Family and domain databases

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

Other

ChiTaRSSERPINA3. human.
EvolutionaryTraceP01011.
GeneWikiAlpha_1-antichymotrypsin.
GenomeRNAi12.
NextBio23.
PMAP-CutDBP01011.
PROP01011.
SOURCESearch...

Entry information

Entry nameAACT_HUMAN
AccessionPrimary (citable) accession number: P01011
Secondary accession number(s): B3KVQ7 expand/collapse secondary AC list , Q13703, Q2TU87, Q2TU88, Q59GP9, Q6LBY8, Q6LDT7, Q6NSC9, Q8N177, Q96DW8, Q9UC47, Q9UNU9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: April 16, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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