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P34955 (A1AT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1-antiproteinase
Alternative name(s):
Alpha-1-antitrypsin
Alpha-1-proteinase inhibitor
Serpin A1
Gene names
Name:SERPINA1
Synonyms:PI
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Inhibits trypsin, chymotrypsin and plasminogen activator By similarity.

Subcellular location

Secreted.

Tissue specificity

Plasma.

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 By similarity.

Sequence similarities

Belongs to the serpin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 By similarity
Chain25 – 416392Alpha-1-antiproteinase
PRO_0000032380

Regions

Region371 – 39020RCL

Sites

Site380 – 3812Reactive bond

Amino acid modifications

Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P34955 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 3280CDAF42DA35E2

FASTA41646,104
        10         20         30         40         50         60 
MALSITRGLL LLAALCCLAP ISLAGVLQGH AVQETDDTSH QEAACHKIAP NLANFAFSIY 

        70         80         90        100        110        120 
HHLAHQSNTS NIFFSPVSIA SAFAMLSLGA KGNTHTEILK GLGFNLTELA EAEIHKGFQH 

       130        140        150        160        170        180 
LLHTLNQPNH QLQLTTGNGL FINESAKLVD TFLEDVKNLY HSEAFSINFR DAEEAKKKIN 

       190        200        210        220        230        240 
DYVEKGSHGK IVELVKVLDP NTVFALVNYI SFKGKWEKPF EMKHTTERDF HVDEQTTVKV 

       250        260        270        280        290        300 
PMMNRLGMFD LHYCDKLASW VLLLDYVGNV TACFILPDLG KLQQLEDKLN NELLAKFLEK 

       310        320        330        340        350        360 
KYASSANLHL PKLSISETYD LKSVLGDVGI TEVFSDRADL SGITKEQPLK VSKALHKAAL 

       370        380        390        400        410 
TIDEKGTEAV GSTFLEAIPM SLPPDVEFNR PFLCILYDRN TKSPLFVGKV VNPTQA 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA sequence of bovine alpha 1-antitrypsin."
Sinha D., Bakhshi M.R., Kirby E.P.
Biochim. Biophys. Acta 1130:209-212(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.
[4]"Isolation and characterization of two protease inhibitors from bovine plasma."
Sinha D., Yang X., Emig F., Kirby E.P.
J. Biochem. 115:387-391(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63129 mRNA. Translation: CAA44840.1.
BT025459 mRNA. Translation: ABF57415.1.
BC102730 mRNA. Translation: AAI02731.1.
PIRS21097.
RefSeqNP_776307.1. NM_173882.2.
XP_005222164.1. XM_005222107.1.
UniGeneBt.982.

3D structure databases

ProteinModelPortalP34955.
SMRP34955. Positions 46-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000004927.

Protein family/group databases

MEROPSI04.001.

Proteomic databases

PaxDbP34955.
PRIDEP34955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000004927; ENSBTAP00000004927; ENSBTAG00000018843.
GeneID280699.
KEGGbta:280699.

Organism-specific databases

CTD5265.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00750000117448.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP34955.
KOK03984.
OMAVVNPTQK.
OrthoDBEOG7QC7W9.
TreeFamTF343201.

Family and domain databases

InterProIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804882.

Entry information

Entry nameA1AT_BOVIN
AccessionPrimary (citable) accession number: P34955
Secondary accession number(s): Q3SZS3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families