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P01011

- AACT_HUMAN

UniProt

P01011 - AACT_HUMAN

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Protein

Alpha-1-antichymotrypsin

Gene

SERPINA3

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

Functioni

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-2.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei383 – 3842Reactive bond

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi235 – 2373

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. inflammatory response Source: UniProtKB
  3. maintenance of gastrointestinal epithelium Source: UniProtKB
  4. negative regulation of endopeptidase activity Source: RefGenome
  5. regulation of lipid metabolic process Source: UniProtKB
  6. regulation of proteolysis Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase

Protein family/group databases

MEROPSiI04.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-antichymotrypsin
Short name:
ACT
Alternative name(s):
Cell growth-inhibiting gene 24/25 protein
Serpin A3
Cleaved into the following chain:
Gene namesi
Name:SERPINA3
Synonyms:AACT
ORF Names:GIG24, GIG25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:16. SERPINA3.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProtKB
  5. intracellular Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Keywords - Diseasei

Disease mutation

Organism-specific databases

Orphaneti93594. Alpha-1-antichymotrypsin deficiency.
PharmGKBiPA35020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 423400Alpha-1-antichymotrypsinPRO_0000032411Add
BLAST
Chaini26 – 423398Alpha-1-antichymotrypsin His-Pro-lessPRO_0000032412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)1 Publication
Glycosylationi93 – 931N-linked (GlcNAc...)4 Publications
Glycosylationi106 – 1061N-linked (GlcNAc...)3 Publications
Glycosylationi127 – 1271N-linked (GlcNAc...)2 Publications
Glycosylationi186 – 1861N-linked (GlcNAc...)1 Publication
Glycosylationi271 – 2711N-linked (GlcNAc...)2 Publications

Post-translational modificationi

N- and O-glycosylated.5 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP01011.
PaxDbiP01011.
PRIDEiP01011.

2D gel databases

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

PTM databases

PhosphoSiteiP01011.
UniCarbKBiP01011.

Miscellaneous databases

PMAP-CutDBP01011.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiP01011.
ExpressionAtlasiP01011. baseline.
GenevestigatoriP01011.

Organism-specific databases

HPAiCAB016647.
HPA000893.
HPA002560.

Interactioni

Subunit structurei

Interacts with DNAJC1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DNAJC1Q96KC83EBI-296557,EBI-296550

Protein-protein interaction databases

BioGridi106530. 14 interactions.
IntActiP01011. 10 interactions.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 6719
Beta strandi69 – 713
Beta strandi73 – 753
Helixi77 – 8812
Helixi93 – 10210
Turni107 – 1093
Helixi112 – 12615
Beta strandi130 – 1323
Beta strandi134 – 14411
Helixi151 – 16111
Beta strandi164 – 1685
Helixi170 – 1723
Helixi173 – 18715
Turni188 – 1903
Beta strandi203 – 21917
Helixi223 – 2253
Beta strandi227 – 2348
Beta strandi237 – 25620
Turni257 – 2604
Beta strandi261 – 27919
Turni281 – 2833
Helixi284 – 2896
Helixi293 – 30210
Beta strandi304 – 31411
Beta strandi316 – 3238
Helixi325 – 3306
Helixi335 – 3373
Helixi344 – 3474
Beta strandi348 – 3503
Beta strandi352 – 36514
Beta strandi367 – 38216
Beta strandi391 – 3944
Beta strandi399 – 4057
Beta strandi412 – 4187

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP01011.
SMRiP01011. Positions 48-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01011.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni369 – 39426RCLAdd
BLAST
Regioni381 – 3899O-glycosylated at one site

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.
InParanoidiP01011.
KOiK04525.
PhylomeDBiP01011.
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: P01011-1) [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
MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA
60 70 80 90 100
SANVDFAFSL YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL
110 120 130 140 150
KGLKFNLTET SEAEIHQSFQ HLLRTLNQSS DELQLSMGNA MFVKEQLSLL
160 170 180 190 200
DRFTEDAKRL YGSEAFATDF QDSAAAKKLI NDYVKNGTRG KITDLIKDLD
210 220 230 240 250
SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM VPMMSLHHLT
260 270 280 290 300
IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR
310 320 330 340 350
DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR
360 370 380 390 400
NLAVSQVVHK AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL
410 420
MIIVPTDTQN IFFMSKVTNP KQA
Length:423
Mass (Da):47,651
Last modified:August 1, 1991 - v2
Checksum:iB002F946C86A8951
GO
Isoform 2 (identifier: P01011-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     215-216: AK → ER
     217-423: Missing.

Note: No experimental confirmation available.

Show »
Length:216
Mass (Da):24,034
Checksum:i49312EDF91439D4D
GO
Isoform 3 (identifier: P01011-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     64-95: LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT → SPRWSIRLCLMYLRRAQKHLLPQQSKSPSFLH
     96-423: Missing.

Note: No experimental confirmation available.

Show »
Length:95
Mass (Da):10,717
Checksum:i15B1759843F9809B
GO

Sequence cautioni

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: Frameshift at position 4.
The sequence AAT08029.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551D → S AA sequence (PubMed:6687683)Curated
Sequence conflicti69 – 691P → L in AAA51543. (PubMed:6606438)Curated
Sequence conflicti101 – 1011K → R in BAD92297. 1 PublicationCurated
Sequence conflicti106 – 1061N → Y in AAT08028. 1 PublicationCurated
Sequence conflicti198 – 1981D → N in AAT08029. 1 PublicationCurated
Sequence conflicti199 – 1991L → P in AAA51543. (PubMed:6606438)Curated
Sequence conflicti234 – 2341S → N in AAT08029. 1 PublicationCurated
Sequence conflicti339 – 3391S → G in AAT08028. 1 PublicationCurated
Sequence conflicti346 – 3461I → S in AAT08028. 1 PublicationCurated
Sequence conflicti361 – 3633AVL → VVS in AAA51543. (PubMed:6606438)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91A → T.4 Publications
Corresponds to variant rs4934 [ dbSNP | Ensembl ].
VAR_006973
Natural varianti78 – 781L → P in Bochum-1. 1 Publication
Corresponds to variant rs1800463 [ dbSNP | Ensembl ].
VAR_006974
Natural varianti167 – 1671A → G.
VAR_006975
Natural varianti252 – 2521P → A in Bonn-1. 2 Publications
Corresponds to variant rs17473 [ dbSNP | Ensembl ].
VAR_006976
Natural varianti267 – 2671K → R.1 Publication
Corresponds to variant rs17853314 [ dbSNP | Ensembl ].
VAR_037902
Natural varianti401 – 4011M → V Associated with occlusive-cerebrovascular disease; Isehara-1. 2 Publications
VAR_006977
Natural varianti407 – 4071D → G.
Corresponds to variant rs10956 [ dbSNP | Ensembl ].
VAR_011742

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei64 – 9532LVLKA…AHNTT → SPRWSIRLCLMYLRRAQKHL LPQQSKSPSFLH in isoform 3. 1 PublicationVSP_014225Add
BLAST
Alternative sequencei96 – 423328Missing in isoform 3. 1 PublicationVSP_014226Add
BLAST
Alternative sequencei215 – 2162AK → ER in isoform 2. 1 PublicationVSP_014227
Alternative sequencei217 – 423207Missing in isoform 2. 1 PublicationVSP_014228Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K01500 mRNA. Translation: AAA51543.1. Frameshift.
X68733
, 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.
CCDSiCCDS32150.1. [P01011-1]
PIRiA90475. ITHUC.
S62374.
RefSeqiNP_001076.2. NM_001085.4. [P01011-1]
UniGeneiHs.534293.
Hs.710488.

Genome annotation databases

EnsembliENST00000393080; ENSP00000376795; ENSG00000196136. [P01011-1]
ENST00000467132; ENSP00000450540; ENSG00000196136. [P01011-1]
ENST00000556968; ENSP00000452476; ENSG00000196136. [P01011-2]
GeneIDi12.
KEGGihsa:12.
UCSCiuc001ydp.3. human. [P01011-1]
uc021sbb.2. human. [P01011-3]

Polymorphism databases

DMDMi112874.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Alpha-1 antichymotrypsin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K01500 mRNA. Translation: AAA51543.1 . Frameshift.
X68733
, 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 .
CCDSi CCDS32150.1. [P01011-1 ]
PIRi A90475. ITHUC.
S62374.
RefSeqi NP_001076.2. NM_001085.4. [P01011-1 ]
UniGenei Hs.534293.
Hs.710488.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AS4 X-ray 2.10 A 43-383 [» ]
B 387-423 [» ]
1QMN X-ray 2.27 A 26-423 [» ]
2ACH X-ray 2.70 A 24-383 [» ]
B 384-423 [» ]
3CAA X-ray 2.40 A 43-383 [» ]
B 387-423 [» ]
3DLW X-ray 2.70 A 25-423 [» ]
4CAA X-ray 2.90 A 43-383 [» ]
B 387-423 [» ]
ProteinModelPortali P01011.
SMRi P01011. Positions 48-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106530. 14 interactions.
IntActi P01011. 10 interactions.

Chemistry

ChEMBLi CHEMBL5960.

Protein family/group databases

MEROPSi I04.002.

PTM databases

PhosphoSitei P01011.
UniCarbKBi P01011.

Polymorphism databases

DMDMi 112874.

2D gel databases

DOSAC-COBS-2DPAGE P01011.
SWISS-2DPAGE P01011.

Proteomic databases

MaxQBi P01011.
PaxDbi P01011.
PRIDEi P01011.

Protocols and materials databases

DNASUi 12.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393080 ; ENSP00000376795 ; ENSG00000196136 . [P01011-1 ]
ENST00000467132 ; ENSP00000450540 ; ENSG00000196136 . [P01011-1 ]
ENST00000556968 ; ENSP00000452476 ; ENSG00000196136 . [P01011-2 ]
GeneIDi 12.
KEGGi hsa:12.
UCSCi uc001ydp.3. human. [P01011-1 ]
uc021sbb.2. human. [P01011-3 ]

Organism-specific databases

CTDi 12.
GeneCardsi GC14P095078.
H-InvDB HIX0079611.
HGNCi HGNC:16. SERPINA3.
HPAi CAB016647.
HPA000893.
HPA002560.
MIMi 107280. gene.
neXtProti NX_P01011.
Orphaneti 93594. Alpha-1-antichymotrypsin deficiency.
PharmGKBi PA35020.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOVERGENi HBG005957.
InParanoidi P01011.
KOi K04525.
PhylomeDBi P01011.
TreeFami TF343201.

Miscellaneous databases

ChiTaRSi SERPINA3. human.
EvolutionaryTracei P01011.
GeneWikii Alpha_1-antichymotrypsin.
GenomeRNAii 12.
NextBioi 23.
PMAP-CutDB P01011.
PROi P01011.
SOURCEi Search...

Gene expression databases

Bgeei P01011.
ExpressionAtlasi P01011. baseline.
Genevestigatori P01011.

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. "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.
    , 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.

Entry informationi

Entry nameiAACT_HUMAN
AccessioniPrimary (citable) accession number: P01011
Secondary accession number(s): B3KVQ7
, Q13703, Q2TU87, Q2TU88, Q59GP9, Q6LBY8, Q6LDT7, Q6NSC9, Q8N177, Q96DW8, Q9UC47, Q9UNU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 183 of the entry and version 2 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

Alpha-1-antichymotrypsin can bind DNA.

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