Reviewed, UniProtKB/Swiss-Prot P01011 (AACT_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-1-antichymotrypsin
      Short name=ACT
Alternative name(s):
    Cell growth-inhibiting gene 24/25 protein
Cleaved into the following chain:
    1- Recommended name:
            Alpha-1-antichymotrypsin His-Pro-less

Gene names

Name:	SERPINA3
Synonyms:	AACT
ORF Names:	GIG24, GIG25

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 myloid plaques from the hippocampus of Alzheimer's 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.
Involvement in disease	Defects in SERPINA3 may be a cause of chronic obstructive pulmonary disease (COPD) [MIM:107280]. Ref.2
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.

Ontologies

Keywords
Biological process	Acute phase
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW regulation of lipid metabolic process Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Ref.8 Non-traceable author statement. Source: UniProtKB nucleus Ref.18 Traceable author statement. Source: UniProtKB
Molecular function	DNA binding Ref.18 Traceable author statement. Source: UniProtKB protein binding Ref.18 Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase inhibitor activity Ref.14 Traceable author statement. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.10

Chain

24 – 423

400

Alpha-1-antichymotrypsin

PRO_0000032411

Chain

26 – 423

398

Alpha-1-antichymotrypsin His-Pro-less

PRO_0000032412

Regions

DNA binding

235 – 237

3

Region

369 – 394

26

RCL

Sites

Site

383 – 384

2

Reactive bond

Amino acid modifications

Glycosylation

33

1

N-linked (GlcNAc...) Ref.21

Glycosylation

93

1

N-linked (GlcNAc...) Ref.21 Ref.17 Ref.20

Glycosylation

106

1

N-linked (GlcNAc...) Ref.21 Ref.17

Glycosylation

127

1

N-linked (GlcNAc...) Ref.21

Glycosylation

186

1

N-linked (GlcNAc...) Ref.21

Glycosylation

271

1

N-linked (GlcNAc...) Ref.21

Natural variations

Alternative sequence

64 – 95

32

LVLKA…AHNTT → SPRWSIRLCLMYLRRAQKHL LPQQSKSPSFLH in isoform 3.

VSP_014225

Alternative sequence

96 – 423

328

Missing in isoform 3.

VSP_014226

Alternative sequence

215 – 216

2

AK → ER in isoform 2.

VSP_014227

Alternative sequence

217 – 423

207

Missing in isoform 2.

VSP_014228

Natural variant

9

1

A → T: dbSNP rs4934. Ref.3 Ref.4 Ref.5 Ref.6

VAR_006973

Natural variant

78

1

L → P in COPD; Bochum-1. dbSNP rs1800463.

VAR_006974

Natural variant

167

1

A → G

VAR_006975

Natural variant

252

1

P → A in COPD; Bonn-1. dbSNP rs17473.

VAR_006976

Natural variant

267

1

K → R: dbSNP rs17853314. Ref.6

VAR_037902

Natural variant

401

1

M → V Associated with occlusive-cerebrovascular disease; Isehara-1. Ref.27 Ref.29

VAR_006977

Natural variant

407

1

D → G: dbSNP rs10956.

VAR_011742

Experimental info

Sequence conflict

55

1

D → S AA sequence Ref.12

Sequence conflict

69

1

P → L in AAA51543. Ref.1

Sequence conflict

101

1

K → R in BAD92297. Ref.5

Sequence conflict

106

1

N → Y in AAT08028. Ref.3

Sequence conflict

198

1

D → N in AAT08029. Ref.3

Sequence conflict

199

1

L → P in AAA51543. Ref.1

Sequence conflict

234

1

S → N in AAT08029. Ref.3

Sequence conflict

339

1

S → G in AAT08028. Ref.3

Sequence conflict

346

1

I → S in AAT08028. Ref.3

Sequence conflict

361 – 363

3

AVL → VVS in AAA51543. Ref.1

Secondary structure

1

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423

Helix Strand Turn

Details...

Helix

49 – 67

19

Beta strand

73 – 75

3

Helix

77 – 88

12

Helix

93 – 102

10

Turn

107 – 109

3

Helix

112 – 126

15

Beta strand

134 – 144

11

Helix

151 – 161

11

Beta strand

164 – 168

5

Helix

173 – 187

15

Turn

188 – 190

3

Beta strand

203 – 219

17

Helix

223 – 225

3

Beta strand

227 – 234

8

Beta strand

237 – 256

20

Turn

257 – 260

4

Beta strand

261 – 279

19

Helix

284 – 289

6

Helix

293 – 302

10

Beta strand

304 – 314

11

Beta strand

316 – 323

8

Helix

325 – 330

6

Helix

335 – 337

3

Helix

344 – 347

4

Beta strand

348 – 350

3

Beta strand

352 – 365

14

Beta strand

367 – 382

16

Beta strand

391 – 394

4

Beta strand

399 – 405

7

Beta strand

412 – 418

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: B002F946C86A8951	FASTA	423	47,651
	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
	Isoform 2. Checksum: 49312EDF91439D4D	FASTA	216	24,034
	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 NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKER
	Isoform 3. Checksum: 15B1759843F9809B	FASTA	95	10,717
	10 20 30 40 50 60 MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL 70 80 90 YKQSPRWSIR LCLMYLRRAQ KHLLPQQSKS PSFLH

References

	« Hide 'large scale' referencesShow '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: 6606438] [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: 8244391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, 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: 14702039] [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: 15489334] [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: 3257719] [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: 9880565] [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: 2787670] [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: 7521171] [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: 6687683] [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: 8647626] [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: 2404007] [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: 6547997] [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: 6556193] [Abstract] Cited for: ACTIVE 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: 12754519] [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: 14668352] [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: 15638460] [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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, MASS SPECTROMETRY. 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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; ASN-127; ASN-186 AND ASN-271, MASS SPECTROMETRY. 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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-106; ASN-127 AND ASN-271, MASS SPECTROMETRY. Tissue: Liver.
[23]	"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: 2016749] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423.
[24]	"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: 8836107] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 AND ARG-372.
[25]	"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: 9521649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; ARG-372 AND ARG-374.
[26]	"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: 10618372] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423.
[27]	"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: 1618300] [Abstract] Cited for: VARIANT ISEHARA-1 VAL-401.
[28]	"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: 1351206] [Abstract] Cited for: VARIANT BONN-1 ALA-252.
[29]	"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: 11289720] [Abstract] Cited for: VARIANT VAL-401.
+	Additional computationally mapped references.

Web resources

Wikipedia

Alpha-1 antichymotrypsin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00550991.
IPI00607870.
IPI00847635.

PIR

ITHUC. A90475.
S62374.

RefSeq

NP_001076.2.

UniGene

Hs.534293
Hs.710488

3D structure databases

PDBPDBe

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	[»]
4CAA	X-ray	2.90	A	43-383	[»]
			B	387-423	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P01011. 1 interaction.

Protein family/group databases

MEROPS

I04.002.

PTM databases

GlycoSuiteDB

P01011.

PhosphoSite

P01011.

2-D gel databases

SWISS-2DPAGE

P01011.

DOSAC-COBS-2DPAGE

P01011.

Siena-2DPAGE

P01011.

Proteomic databases

PRIDE

P01011.

Genome annotation databases

Ensembl

ENSG00000196136. Homo sapiens. [Contig view]

GeneID

12.

KEGG

hsa:12.

Organism-specific databases

GeneCards

GC14P094148.

H-InvDB

HIX0011931.
HIX0079611.

HGNC

HGNC:16. SERPINA3.

HPA

CAB016647.
HPA002560.

MIM

107280. gene.

PharmGKB

PA35020.

GenAtlas

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Phylogenomic databases

HOVERGEN

P01011.

Gene expression databases

ArrayExpress

P01011.

Bgee

P01011.

GermOnline

ENSG00000196136. Homo sapiens.

Family and domain databases

InterPro

IPR000215. Protease_inhib_I4_serpin.
[Graphical view]

PANTHER

PTHR11461. Prot_inh_serpin. 1 hit.

Pfam

PF00079. Serpin. 1 hit.
[Graphical view]

SMART

SM00093. SERPIN. 1 hit.
[Graphical view]

PROSITE

PS00284. SERPIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

23.

PMAP-CutDB

P01011.

SOURCE

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Entry information

Entry name

AACT_HUMAN

Accession

Primary (citable) accession number: P01011
Secondary accession number(s): B3KVQ7 , 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:	June 16, 2009
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)