CPLM-001859

CPLM 1.0 - Compendium of Protein Lysine Modification

Tag

Content

CPLM ID

CPLM-001859

UniProt Accession

AACT_HUMAN; P01011; B3KVQ7; Q13703; Q2TU87; Q2TU88; Q59GP9; Q6LBY8; Q6LDT7; Q6NSC9; Q8N177; Q96DW8; Q9UC47; Q9UNU9

Genbank Protein ID

K01500; X68733; X68734; X68735; X68736; X68737; AY513275; AY513276; AK123091; AB209060; BC003559; BC010530; BC013189; BC034554; BC070265; M18906; AF089747; J05176; X00947

Genbank Nucleotide ID

AAA51543.1; CAA48671.1; CAA48671.1; CAA48671.1; CAA48671.1; CAA48671.1; AAT08028.1; AAT08029.1; BAG53869.1; BAD92297.1; AAH03559.3; AAH10530.1; AAH13189.1; AAH34554.1; AAH70265.1; AAA51559.1; AAD08810.1; AAA51560.1; CAA25459.1

Protein Name

Alpha-1-antichymotrypsin

Protein Synonyms/Alias

ACT; Cell growth-inhibiting gene 24/25 protein; Serpin A3; Alpha-1-antichymotrypsin His-Pro-less

Gene Name

SERPINA3

Gene Synonyms/Alias

AACT; GIG24; GIG25

Created Date

July 27, 2013

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Lysine Modification

Position	Peptide	Type	References
416	QNIFFMSKVTNPKQA	acetylation	[1]
421	MSKVTNPKQA*****	acetylation	[1]

Reference

[1] Identification of lysines within alpha 1-antichymotrypsin important for DNA binding. An unusual combination of DNA-binding elements.
Naidoo N, Cooperman BS, Wang ZM, Liu XZ, Rubin H.
J Biol Chem. 1995 Jun 16;270(24):14548-55. [PMID: 7782318]

Functional Description

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.

Sequence Annotation

DNA_BIND 235 237
REGION 369 394 RCL.
REGION 381 389 O-glycosylated at one site.
CARBOHYD 33 33 N-linked (GlcNAc...).
CARBOHYD 93 93 N-linked (GlcNAc...).
CARBOHYD 106 106 N-linked (GlcNAc...).
CARBOHYD 127 127 N-linked (GlcNAc...).
CARBOHYD 186 186 N-linked (GlcNAc...).
CARBOHYD 271 271 N-linked (GlcNAc...).

Keyword

3D-structure; Acute phase; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Glycoprotein; Polymorphism; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal.

Sequence Source

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

Protein Length

423 AA

Protein Sequence

MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL 60
YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ 120
HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI 180
NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM 240
VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR 300
DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK 360
AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP 420
KQA 423

Gene Ontology

GO:0005576; C:extracellular region; NAS:UniProtKB.
GO:0005634; C:nucleus; TAS:UniProtKB.
GO:0003677; F:DNA binding; TAS:UniProtKB.
GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB.
GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO:0030277; P:maintenance of gastrointestinal epithelium; NAS:UniProtKB.
GO:0019216; P:regulation of lipid metabolic process; NAS:UniProtKB.
GO:0030162; P:regulation of proteolysis; IBA:RefGenome.

Interpro

IPR023795; Protease_inhib_I4_serpin_CS.
IPR023796; Serpin_dom.
IPR000215; Serpin_fam.

Pfam

PF00079; Serpin

SMART

SM00093; SERPIN

PROSITE

PS00284; SERPIN

PRINTS