ID AACT_HUMAN Reviewed; 423 AA. AC P01011; B3KVQ7; Q13703; Q2TU87; Q2TU88; Q59GP9; Q6LBY8; Q6LDT7; AC Q6NSC9; Q8N177; Q96DW8; Q9UC47; Q9UNU9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 2. DT 05-APR-2011, entry version 148. DE RecName: Full=Alpha-1-antichymotrypsin; DE Short=ACT; DE AltName: Full=Cell growth-inhibiting gene 24/25 protein; DE AltName: Full=Serpin A3; DE Contains: DE RecName: Full=Alpha-1-antichymotrypsin His-Pro-less; DE Flags: Precursor; GN Name=SERPINA3; Synonyms=AACT; ORFNames=GIG24, GIG25; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX MEDLINE=84080367; PubMed=6606438; DOI=10.1021/bi00291a001; RA Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.; RT "Sequence homology between human alpha 1-antichymotrypsin, alpha 1- RT antitrypsin, and antithrombin III."; RL Biochemistry 22:5055-5061(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, AND VARIANTS RP BOCHUM-1 PRO-78 AND BONN-1 ALA-252. RX MEDLINE=94063919; PubMed=8244391; DOI=10.1006/geno.1993.1396; RA Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M., RA Olek K., Kirchgesser M., Heidtmann H.-H.; RT "A leucine-to-proline substitution causes a defective alpha 1- RT antichymotrypsin allele associated with familial obstructive lung RT disease."; RL Genomics 17:740-743(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. RA Kim J.W.; RT "Identification of a human cell growth inhibiting gene."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. RC TISSUE=Urinary bladder; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND RP VARIANTS THR-9 AND ARG-267. RC TISSUE=Brain, Liver, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX MEDLINE=88135764; PubMed=3257719; DOI=10.1016/0092-8674(88)90462-X; RA Abraham C.R., Selkoe D.J., Potter H.; RT "Immunochemical identification of the serine protease inhibitor alpha RT 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's RT disease."; RL Cell 52:487-501(1988). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Hippocampus; RX MEDLINE=99098931; PubMed=9880565; DOI=10.1074/jbc.274.3.1821; RA Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.; RT "Molecular studies define the primary structure of alpha1- RT antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease RT brains. Comparison of act in hippocampus and liver."; RL J. Biol. Chem. 274:1821-1827(1999). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1). RA Rubin H.; RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases. RN [10] RP PROTEIN SEQUENCE OF 24-34. RX MEDLINE=89323223; PubMed=2787670; DOI=10.1016/0167-4838(89)90139-8; RA Lindmark B., Hilja H., Alan R., Eriksson S.; RT "The microheterogeneity of desialylated alpha 1-antichymotrypsin: the RT occurrence of two amino-terminal isoforms, one lacking a His-Pro RT dipeptide."; RL Biochim. Biophys. Acta 997:90-95(1989). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-45. RX MEDLINE=94354957; PubMed=7521171; RA Korzus E., Luisetti M., Travis J.; RT "Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase RT inhibitor, and alpha-2-macroglobulin with the fungal enzyme, RT seaprose."; RL Biol. Chem. Hoppe-Seyler 375:335-341(1994). RN [12] RP PROTEIN SEQUENCE OF 41-60. RX MEDLINE=83178256; PubMed=6687683; DOI=10.1016/0006-291X(83)90325-X; RA Morii M., Travis J.; RT "Structural alterations in alpha 1-antichymotrypsin from normal and RT acute phase human plasma."; RL Biochem. Biophys. Res. Commun. 111:438-443(1983). RN [13] RP PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2). RX MEDLINE=96216555; PubMed=8647626; RX DOI=10.1002/(SICI)1097-0215(19960529)66:5<636::AID-IJC10>3.0.CO;2-2; RA Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C., RA Preston B.N., Linnane A.W.; RT "Characterisation of the tumour-associated carbohydrate epitope RT recognised by monoclonal antibody 4D3."; RL Int. J. Cancer 66:636-644(1996). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION. RC TISSUE=Liver; RX MEDLINE=90110106; PubMed=2404007; RA Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N., RA Schoenberger O.L., Johnson J.L., Cooperman B.S.; RT "Cloning, expression, purification, and biological activity of RT recombinant native and variant human alpha 1-antichymotrypsins."; RL J. Biol. Chem. 265:1199-1207(1990). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423. RX MEDLINE=84295637; PubMed=6547997; DOI=10.1038/311175a0; RA Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.; RT "Plasma protease inhibitors in mouse and man: divergence within the RT reactive centre regions."; RL Nature 311:175-177(1984). RN [16] RP ACTIVE SITE. RX MEDLINE=84032476; PubMed=6556193; RA Morii M., Travis J.; RT "Amino acid sequence at the reactive site of human alpha 1- RT antichymotrypsin."; RL J. Biol. Chem. 258:12749-12752(1983). RN [17] RP GLYCOSYLATION AT ASN-93 AND ASN-106. RX MEDLINE=22660472; PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [18] RP INTERACTION WITH DNAJC1. RX PubMed=14668352; DOI=10.1074/jbc.M310903200; RA Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., RA Blond S.Y.; RT "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human RT homologue interacts with alpha1-antichymotrypsin and kinetically RT interferes with its serpin inhibitory activity."; RL J. Biol. Chem. 279:11432-11443(2004). RN [19] RP REGION RCL. RX PubMed=15638460; DOI=10.1007/s00239-004-2640-9; RA Horvath A.J., Forsyth S.L., Coughlin P.B.; RT "Expression patterns of murine antichymotrypsin-like genes reflect RT evolutionary divergence at the Serpina3 locus."; RL J. Mol. Evol. 59:488-497(2004). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; RP ASN-127; ASN-186 AND ASN-271, AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-106; ASN-127 AND RP ASN-271, AND MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423. RX MEDLINE=91202538; PubMed=2016749; DOI=10.1016/0022-2836(91)90704-A; RA Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.; RT "Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A RT resolution and its comparison with other serpins."; RL J. Mol. Biol. 218:595-606(1991). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 RP AND ARG-372. RX MEDLINE=96433079; PubMed=8836107; DOI=10.1038/nsb1096-888; RA Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S., RA Christianson D.W.; RT "Arginine substitutions in the hinge region of antichymotrypsin affect RT serpin beta-sheet rearrangement."; RL Nat. Struct. Biol. 3:888-893(1996). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; RP ARG-372 AND ARG-374. RX MEDLINE=98198038; PubMed=9521649; DOI=10.1021/bi972359e; RA Lukacs C.M., Rubin H., Christianson D.W.; RT "Engineering an anion-binding cavity in antichymotrypsin modulates the RT 'spring-loaded' serpin-protease interaction."; RL Biochemistry 37:3297-3304(1998). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423. RX MEDLINE=20087203; PubMed=10618372; DOI=10.1073/pnas.97.1.67; RA Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W., RA Read R.J., Lomas D.A.; RT "Inactive conformation of the serpin alpha(1)-antichymotrypsin RT indicates two-stage insertion of the reactive loop: implications for RT inhibitory function and conformational disease."; RL Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000). RN [27] RP VARIANT ISEHARA-1 VAL-401. RX MEDLINE=92316200; PubMed=1618300; DOI=10.1016/0014-5793(92)80590-D; RA Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.; RT "Detection of a new mutant alpha-1-antichymotrypsin in patients with RT occlusive-cerebrovascular disease."; RL FEBS Lett. 304:66-68(1992). RN [28] RP VARIANT BONN-1 ALA-252. RX MEDLINE=92292844; PubMed=1351206; DOI=10.1016/0140-6736(92)91301-N; RA Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K., RA Olek K., Eriksson S.; RT "Mis-sense mutation of alpha 1-antichymotrypsin gene associated with RT chronic lung disease."; RL Lancet 339:1538-1538(1992). RN [29] RP VARIANT VAL-401. RX PubMed=11289720; DOI=10.1007/s100380170125; RA Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.; RT "Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is RT associated with a lacunar type of ischemic cerebrovascular disease."; RL J. Hum. Genet. 46:45-47(2001). CC -!- FUNCTION: Although its physiological function is unclear, it can CC inhibit neutrophil cathepsin G and mast cell chymase, both of CC which can convert angiotensin-1 to the active angiotensin-2. CC -!- SUBUNIT: Interacts with DNAJC1. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P01011-1; Sequence=Displayed; CC Name=2; CC IsoId=P01011-2; Sequence=VSP_014227, VSP_014228; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P01011-3; Sequence=VSP_014225, VSP_014226; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the CC related alpha-1-antitrypsin, its concentration increases in the CC acute phase of inflammation or infection. Found in the amyloid CC plaques from the hippocampus of Alzheimer disease brains. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable. CC -!- DISEASE: Defects in SERPINA3 may be a cause of chronic obstructive CC pulmonary disease (COPD) [MIM:107280]. CC -!- MISCELLANEOUS: Alpha-1-antichymotrypsin can bind DNA. CC -!- SIMILARITY: Belongs to the serpin family. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC -!- SEQUENCE CAUTION: CC Sequence=AAA51543.1; Type=Frameshift; Positions=101, 106, 111, 117, 123, 129, 421; CC Sequence=AAT08029.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AAT08029.1; Type=Frameshift; Positions=4; CC Sequence=BAD92297.1; Type=Erroneous initiation; CC Sequence=CAA48671.1; Type=Erroneous initiation; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antichymotrypsin entry; CC URL="http://en.wikipedia.org/wiki/Alpha_1-antichymotrypsin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K01500; AAA51543.1; ALT_FRAME; mRNA. DR EMBL; X68733; CAA48671.1; ALT_INIT; Genomic_DNA. DR EMBL; X68734; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68735; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68736; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68737; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; AY513275; AAT08028.1; -; mRNA. DR EMBL; AY513276; AAT08029.1; ALT_SEQ; mRNA. DR EMBL; AK123091; BAG53869.1; -; mRNA. DR EMBL; AB209060; BAD92297.1; ALT_INIT; mRNA. DR EMBL; BC003559; AAH03559.3; -; mRNA. DR EMBL; BC010530; AAH10530.1; -; mRNA. DR EMBL; BC013189; AAH13189.1; -; mRNA. DR EMBL; BC034554; AAH34554.1; -; mRNA. DR EMBL; BC070265; AAH70265.1; -; mRNA. DR EMBL; M18906; AAA51559.1; -; mRNA. DR EMBL; AF089747; AAD08810.1; -; mRNA. DR EMBL; J05176; AAA51560.1; -; mRNA. DR EMBL; X00947; CAA25459.1; -; Genomic_DNA. DR IPI; IPI00550991; -. DR IPI; IPI00607870; -. DR IPI; IPI00847635; -. DR PIR; A90475; ITHUC. DR PIR; S62374; S62374. DR RefSeq; NP_001076.2; NM_001085.4. DR UniGene; Hs.534293; -. DR UniGene; Hs.710488; -. DR PDB; 1AS4; X-ray; 2.10 A; A=43-383, B=387-423. DR PDB; 1QMN; X-ray; 2.27 A; A=26-423. DR PDB; 2ACH; X-ray; 2.70 A; A=24-383, B=384-423. DR PDB; 3CAA; X-ray; 2.40 A; A=43-383, B=387-423. DR PDB; 3DLW; X-ray; 2.70 A; A=25-423. DR PDB; 4CAA; X-ray; 2.90 A; A=43-383, B=387-423. DR PDBsum; 1AS4; -. DR PDBsum; 1QMN; -. DR PDBsum; 2ACH; -. DR PDBsum; 3CAA; -. DR PDBsum; 3DLW; -. DR PDBsum; 4CAA; -. DR ProteinModelPortal; P01011; -. DR SMR; P01011; 48-422. DR IntAct; P01011; 3. DR STRING; P01011; -. DR MEROPS; I04.002; -. DR GlycoSuiteDB; P01011; -. DR PhosphoSite; P01011; -. DR SWISS-2DPAGE; P01011; -. DR DOSAC-COBS-2DPAGE; P01011; -. DR Siena-2DPAGE; P01011; -. DR PRIDE; P01011; -. DR Ensembl; ENST00000393078; ENSP00000376793; ENSG00000196136. DR Ensembl; ENST00000393080; ENSP00000376795; ENSG00000196136. DR GeneID; 12; -. DR KEGG; hsa:12; -. DR UCSC; uc001ydo.2; human. DR CTD; 12; -. DR GeneCards; GC14P075259; -. DR H-InvDB; HIX0011931; -. DR HGNC; HGNC:16; SERPINA3. DR HPA; CAB016647; -. DR HPA; HPA002560; -. DR MIM; 107280; gene. DR neXtProt; NX_P01011; -. DR PharmGKB; PA35020; -. DR eggNOG; prNOG14001; -. DR GeneTree; ENSGT00560000076583; -. DR HOVERGEN; HBG005957; -. DR InParanoid; P01011; -. DR OrthoDB; EOG4FFD1T; -. DR NextBio; 23; -. DR PMAP-CutDB; P01011; -. DR ArrayExpress; P01011; -. DR Bgee; P01011; -. DR Genevestigator; P01011; -. DR GermOnline; ENSG00000196136; Homo sapiens. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; NAS:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; NAS:UniProtKB. DR InterPro; IPR000215; Protease_inhib_I4_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Prot_inh_serpin; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Glycoprotein; KW Polymorphism; Protease inhibitor; Secreted; Serine protease inhibitor; KW Signal. FT SIGNAL 1 23 FT CHAIN 24 423 Alpha-1-antichymotrypsin. FT /FTId=PRO_0000032411. FT CHAIN 26 423 Alpha-1-antichymotrypsin His-Pro-less. FT /FTId=PRO_0000032412. FT DNA_BIND 235 237 FT REGION 369 394 RCL. FT SITE 383 384 Reactive bond. FT CARBOHYD 33 33 N-linked (GlcNAc...). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 106 106 N-linked (GlcNAc...). FT CARBOHYD 127 127 N-linked (GlcNAc...). FT CARBOHYD 186 186 N-linked (GlcNAc...). FT CARBOHYD 271 271 N-linked (GlcNAc...). FT VAR_SEQ 64 95 LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT -> SPRWS FT IRLCLMYLRRAQKHLLPQQSKSPSFLH (in isoform FT 3). FT /FTId=VSP_014225. FT VAR_SEQ 96 423 Missing (in isoform 3). FT /FTId=VSP_014226. FT VAR_SEQ 215 216 AK -> ER (in isoform 2). FT /FTId=VSP_014227. FT VAR_SEQ 217 423 Missing (in isoform 2). FT /FTId=VSP_014228. FT VARIANT 9 9 A -> T (in dbSNP:rs4934). FT /FTId=VAR_006973. FT VARIANT 78 78 L -> P (in COPD; Bochum-1; FT dbSNP:rs1800463). FT /FTId=VAR_006974. FT VARIANT 167 167 A -> G. FT /FTId=VAR_006975. FT VARIANT 252 252 P -> A (in COPD; Bonn-1; dbSNP:rs17473). FT /FTId=VAR_006976. FT VARIANT 267 267 K -> R (in dbSNP:rs17853314). FT /FTId=VAR_037902. FT VARIANT 401 401 M -> V (associated with occlusive- FT cerebrovascular disease; Isehara-1). FT /FTId=VAR_006977. FT VARIANT 407 407 D -> G (in dbSNP:rs10956). FT /FTId=VAR_011742. FT CONFLICT 55 55 D -> S (in Ref. 12; AA sequence). FT CONFLICT 69 69 P -> L (in Ref. 1; AAA51543). FT CONFLICT 101 101 K -> R (in Ref. 5; BAD92297). FT CONFLICT 106 106 N -> Y (in Ref. 3; AAT08028). FT CONFLICT 198 198 D -> N (in Ref. 3; AAT08029). FT CONFLICT 199 199 L -> P (in Ref. 1; AAA51543). FT CONFLICT 234 234 S -> N (in Ref. 3; AAT08029). FT CONFLICT 339 339 S -> G (in Ref. 3; AAT08028). FT CONFLICT 346 346 I -> S (in Ref. 3; AAT08028). FT CONFLICT 361 363 AVL -> VVS (in Ref. 1; AAA51543). FT HELIX 49 67 FT STRAND 73 75 FT HELIX 77 88 FT HELIX 93 102 FT TURN 107 109 FT HELIX 112 126 FT STRAND 134 144 FT HELIX 151 161 FT STRAND 164 168 FT HELIX 173 187 FT TURN 188 190 FT STRAND 203 219 FT HELIX 223 225 FT STRAND 227 234 FT STRAND 237 256 FT TURN 257 260 FT STRAND 261 279 FT HELIX 284 289 FT HELIX 293 302 FT STRAND 304 314 FT STRAND 316 323 FT HELIX 325 330 FT HELIX 335 337 FT HELIX 344 347 FT STRAND 348 350 FT STRAND 352 365 FT STRAND 367 382 FT STRAND 391 394 FT STRAND 399 405 FT STRAND 412 418 SQ SEQUENCE 423 AA; 47651 MW; B002F946C86A8951 CRC64; MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP KQA //