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P01011

- AACT_HUMAN

UniProt

P01011 - AACT_HUMAN

Protein

Alpha-1-antichymotrypsin

Gene

SERPINA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 2 (01 Aug 1991)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. 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

    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: UniProt
    5. intracellular Source: UniProtKB
    6. nucleus Source: UniProtKB

    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...)2 Publications
    Glycosylationi93 – 931N-linked (GlcNAc...)5 Publications
    Glycosylationi106 – 1061N-linked (GlcNAc...)4 Publications
    Glycosylationi127 – 1271N-linked (GlcNAc...)3 Publications
    Glycosylationi186 – 1861N-linked (GlcNAc...)2 Publications
    Glycosylationi271 – 2711N-linked (GlcNAc...)3 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

    ArrayExpressiP01011.
    BgeeiP01011.
    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. 11 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.
    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

    MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA    50
    SANVDFAFSL YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL 100
    KGLKFNLTET SEAEIHQSFQ HLLRTLNQSS DELQLSMGNA MFVKEQLSLL 150
    DRFTEDAKRL YGSEAFATDF QDSAAAKKLI NDYVKNGTRG KITDLIKDLD 200
    SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM VPMMSLHHLT 250
    IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR 300
    DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR 350
    NLAVSQVVHK AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL 400
    MIIVPTDTQN IFFMSKVTNP KQA 423
    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. 11 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.
    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

    ArrayExpressi P01011.
    Bgeei P01011.
    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

    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 1, 2014
    This is version 182 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