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P17475

- A1AT_RAT

UniProt

P17475 - A1AT_RAT

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Protein

Alpha-1-antiproteinase

Gene

Serpina1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei376 – 3772Reactive bond

GO - Molecular functioni

  1. endopeptidase inhibitor activity Source: RGD
  2. serine-type endopeptidase inhibitor activity Source: RGD

GO - Biological processi

  1. acute-phase response Source: UniProtKB-KW
  2. inflammatory response Source: RGD
  3. negative regulation of endopeptidase activity Source: RefGenome
  4. negative regulation of serine-type endopeptidase activity Source: RGD
  5. regulation of proteolysis Source: RefGenome
  6. response to chromate Source: RGD
  7. response to cytokine Source: RGD
  8. response to estradiol Source: RGD
  9. response to hypoxia Source: RGD
  10. response to inorganic substance Source: RGD
  11. response to lead ion Source: RGD
  12. response to lipopolysaccharide Source: RGD
  13. response to methanol Source: RGD
  14. response to organic cyclic compound Source: RGD
  15. response to triglyceride Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Acute phase

Protein family/group databases

MEROPSiI04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1-antiproteinase
Alternative name(s):
Alpha-1-antitrypsin
Alpha-1-proteinase inhibitor
Serpin A1
Gene namesi
Name:Serpina1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi3326. Serpina1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 411387Alpha-1-antiproteinasePRO_0000032398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP17475.
PRIDEiP17475.

PTM databases

PhosphoSiteiP17475.

Expressioni

Tissue specificityi

Plasma.1 Publication

Gene expression databases

GenevestigatoriP17475.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012577.

Structurei

3D structure databases

ProteinModelPortaliP17475.
SMRiP17475. Positions 39-411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 38620RCLAdd
BLAST

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP17475.
KOiK03984.
OrthoDBiEOG7QC7W9.
PhylomeDBiP17475.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17475-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPSISRGLL LLAALCCLAP SFLAEDAQET DTSQQDQSPT YRKISSNLAD
60 70 80 90 100
FAFSLYRELV HQSNTSNIFF SPMSITTAFA MLSLGSKGDT RKQILEGLEF
110 120 130 140 150
NLTQIPEADI HKAFHHLLQT LNRPDSELQL NTGNGLFVNK NLKLVEKFLE
160 170 180 190 200
EVKNNYHSEA FSVNFADSEE AKKVINDYVE KGTQGKIVDL MKQLDEDTVF
210 220 230 240 250
ALVNYIFFKG KWKRPFNPEH TRDADFHVDK STTVKVPMMN RLGMFDMHYC
260 270 280 290 300
STLSSWVLMM DYLGNATAIF LLPDDGKMQH LEQTLTKDLI SRFLLNRQTR
310 320 330 340 350
SAILYFPKLS ISGTYNLKTL LSSLGITRVF NNDADLSGIT EDAPLKLSQA
360 370 380 390 400
VHKAVLTLDE RGTEAAGATV VEAVPMSLPP QVKFDHPFIF MIVESETQSP
410
LFVGKVIDPT R
Length:411
Mass (Da):46,136
Last modified:February 1, 1991 - v2
Checksum:iB4245CFE21C5C761
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141A → G in BAA00579. (PubMed:2229024)Curated
Sequence conflicti14 – 141A → G in AAH78824. (PubMed:15489334)Curated
Sequence conflicti84 – 841L → V in BAA00579. (PubMed:2229024)Curated
Sequence conflicti247 – 2471M → I in CAA34349. 1 PublicationCurated
Sequence conflicti248 – 2481H → Y in BAA00579. (PubMed:2229024)Curated
Sequence conflicti318 – 3181K → N in BAA00579. (PubMed:2229024)Curated
Sequence conflicti322 – 3221S → D in CAA34349. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00675 mRNA. Translation: BAA00579.1.
BC078824 mRNA. Translation: AAH78824.1.
M32247 mRNA. Translation: AAA40788.1.
X16273 mRNA. Translation: CAA34349.1.
PIRiA33892. ITRT.
RefSeqiNP_071964.2. NM_022519.2.
XP_006240518.1. XM_006240456.1.
UniGeneiRn.1419.

Genome annotation databases

EnsembliENSRNOT00000012577; ENSRNOP00000012577; ENSRNOG00000032669.
GeneIDi24648.
KEGGirno:24648.
UCSCiRGD:3326. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00675 mRNA. Translation: BAA00579.1 .
BC078824 mRNA. Translation: AAH78824.1 .
M32247 mRNA. Translation: AAA40788.1 .
X16273 mRNA. Translation: CAA34349.1 .
PIRi A33892. ITRT.
RefSeqi NP_071964.2. NM_022519.2.
XP_006240518.1. XM_006240456.1.
UniGenei Rn.1419.

3D structure databases

ProteinModelPortali P17475.
SMRi P17475. Positions 39-411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000012577.

Protein family/group databases

MEROPSi I04.001.

PTM databases

PhosphoSitei P17475.

Proteomic databases

PaxDbi P17475.
PRIDEi P17475.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000012577 ; ENSRNOP00000012577 ; ENSRNOG00000032669 .
GeneIDi 24648.
KEGGi rno:24648.
UCSCi RGD:3326. rat.

Organism-specific databases

CTDi 5265.
RGDi 3326. Serpina1.

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P17475.
KOi K03984.
OrthoDBi EOG7QC7W9.
PhylomeDBi P17475.
TreeFami TF343201.

Miscellaneous databases

NextBioi 603964.

Gene expression databases

Genevestigatori P17475.

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

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of the cDNA of rat alpha 1-protease inhibitor and its expression in COS-1 cells."
    Misumi Y., Sohda M., Ohkubo K., Takami N., Oda K., Ikehara Y.
    J. Biochem. 108:230-234(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "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].
    Tissue: Testis.
  3. "Molecular cloning and primary structure of rat alpha 1-antitrypsin."
    Chao S., Chai K.X., Chao L., Chao J.
    Biochemistry 29:323-329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-411, PROTEIN SEQUENCE OF 25-57, TISSUE SPECIFICITY.
    Tissue: Liver.
  4. Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-57; 148-172; 174-181; 187-192; 278-287 AND 301-328, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  5. Flink I.L., Bailey T., Morkin E.
    Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-389.
    Tissue: Liver.

Entry informationi

Entry nameiA1AT_RAT
AccessioniPrimary (citable) accession number: P17475
Secondary accession number(s): Q6AYZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3