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P05545 (SPA3K_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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:
Serine protease inhibitor A3K

Short name=Serpin A3K
Alternative name(s):
CPI-21
Contrapsin-like protease inhibitor 1
GHR-P63
Growth hormone-regulated proteinase inhibitor
Kallikrein-binding protein
Short name=KBP
SPI-2.3
Serine protease inhibitor 2
Short name=SPI-2
Thyroid hormone-regulated protein
Gene names
Name:Serpina3k
Synonyms:Spin2b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

Binds to and inhibits kallikreins. Inhibits trypsin but not chymotrypsin or elastase. Ref.1 Ref.6

Subcellular location

Secreted By similarity.

Tissue specificity

Liver and plasma. Ref.1 Ref.6 Ref.9

Induction

By growth hormone, thyroid hormone and sex hormones. Its expression is reduced by inflammation. In male rats, its level is several fold higher than in female rats. Reduced during acute inflammation. Ref.1 Ref.3 Ref.4 Ref.9

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 serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable By similarity. Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity. Ref.11

Post-translational modification

N-glycosylated. Ref.1 Ref.4

Miscellaneous

The single human alpha1-antichymotrypsin gene (SERPINA3) is represented by a cluster of 6 individual rat paralogs.

Sequence similarities

Belongs to the serpin family.

Sequence caution

The sequence AAH62236.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAA34407.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA34409.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.9
Chain21 – 416396Serine protease inhibitor A3K
PRO_0000032421

Regions

Region365 – 39228RCL

Sites

Site379 – 3802Reactive bond By similarity

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential

Natural variations

Natural variant3261E → D. Ref.5

Experimental info

Sequence conflict301P → S AA sequence Ref.9
Sequence conflict471S → A AA sequence Ref.9
Sequence conflict981V → G in AAA42173. Ref.3
Sequence conflict981V → G in BAA00648. Ref.6
Sequence conflict981V → G in AAH62236. Ref.8
Sequence conflict1121H → HH in CAA34407. Ref.4
Sequence conflict1941E → D in BAA00648. Ref.6
Sequence conflict2501I → V in BAA00648. Ref.6
Sequence conflict3261E → D in CAA34409. Ref.5
Sequence conflict3851I → V in BAA00648. Ref.6
Sequence conflict3871L → P in CAA34407. Ref.4
Sequence conflict4011N → D in AAH62236. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P05545 [UniParc].

Last modified April 1, 1993. Version 3.
Checksum: 6072BAE56BFF91B1

FASTA41646,562
        10         20         30         40         50         60 
MAFIAALGLL MAGICPAVLC DGILGRDTLP HEDQGKGRQL HSLTLASINT DFTLSLYKKL 

        70         80         90        100        110        120 
ALRNPDKNVV FSPLSISAAL AILSLGAKDS TMEEILEVLK FNLTEITEEE IHQGFGHLLQ 

       130        140        150        160        170        180 
RLSQPEDQAE INTGSALFID KEQPILSEFQ EKTRALYQAE AFVADFKQCN EAKKFINDYV 

       190        200        210        220        230        240 
SNQTQGKIAE LFSELDERTS MVLVNYLLFK GKWKVPFNPN DTFESEFYLD EKRSVKVPMM 

       250        260        270        280        290        300 
KIKDLTTPYI RDEELSCSVL ELKYTGNASA LFILPDQGKM QQVESSLQPE TLKKWKDSLR 

       310        320        330        340        350        360 
PRIISELRMP KFSISTDYNL EEVLPELGIR KIFSQQADLS RITGTKNLHV SQVVHKAVLD 

       370        380        390        400        410 
VDETGTEGAA ATAVTAALKS LPQTIPLLNF NRPFMLVITD NNGQSVFFMG KVTNPM 

« Hide

References

« Hide 'large scale' references
[1]"Study of a growth hormone-regulated protein secreted by rat hepatocytes: cDNA cloning, anti-protease activity and regulation of its synthesis by various hormones."
le Cam A., Pages G., Auberger P., le Cam G., Leopold P., Benarous R., Glaichenhaus N.
EMBO J. 6:1225-1232(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION.
[2]le Cam A.
Submitted (OCT-1987) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Growth hormone induces two mRNA species of the serine protease inhibitor gene family in rat liver."
Yoon J.-B., Towle H.C., Seelig S.
J. Biol. Chem. 262:4284-4289(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Tissue: Liver.
[4]"Molecular characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning."
Pages G., Rouayrenc J.F., le Cam G., Mariller M., le Cam A.
Eur. J. Biochem. 190:385-391(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, GLYCOSYLATION.
Tissue: Liver.
[5]"Primary structure and assignment to chromosome 6 of three related rat genes encoding liver serine protease inhibitors."
Pages G., Rouayrenc J.F., Rossi V., Le Cam G., Mariller M., Szpirer J., Szpirer C., Levan G., Le Cam A.
Gene 94:273-282(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-326.
[6]"Molecular cloning and characterization of rat contrapsin-like protease inhibitor and related proteins."
Ohkubo K., Ogata S., Misumi Y., Takami N., Ikehara Y.
J. Biochem. 109:243-250(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY.
Tissue: Liver.
[7]"Molecular cloning and analysis of the rat kallikrein-binding protein gene."
Chai K.X., Ma J.-X., Murray S.R., Chao J., Chao L.
J. Biol. Chem. 266:16029-16036(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[8]"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: Pituitary.
[9]"Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats."
Chao J., Chai K.X., Chen L.-M., Xiong W., Chao S., Woodley-Miller C., Wang L., Lu H.S., Chao L.
J. Biol. Chem. 265:16394-16401(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-49, PROTEIN SEQUENCE OF 21-49, CHARACTERIZATION, TISSUE SPECIFICITY, INDUCTION.
[10]Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 155-167; 188-210 AND 312-330, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[11]"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] [Europe PMC] [Abstract]
Cited for: DOMAIN RCL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05348 mRNA. Translation: CAA28958.1.
M15916 mRNA. Translation: AAA42173.1.
X16358 mRNA. Translation: CAA34407.1. Different initiation.
X16362 Genomic DNA. Translation: CAA34409.1. Different initiation.
D00751 mRNA. Translation: BAA00648.1.
M67496 Genomic DNA. No translation available.
BC062236 mRNA. Translation: AAH62236.2. Different initiation.
PIRA29035.
B29131.
RefSeqNP_036789.2. NM_012657.2.
XP_006240520.1. XM_006240458.1.
UniGeneRn.91257.
Rn.97597.

3D structure databases

ProteinModelPortalP05545.
SMRP05545. Positions 45-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP05545. 1 interaction.

Protein family/group databases

MEROPSI04.051.

PTM databases

PhosphoSiteP05545.

Proteomic databases

PaxDbP05545.
PRIDEP05545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000013896; ENSRNOP00000013896; ENSRNOG00000010410.
GeneID24794.
KEGGrno:24794.
UCSCRGD:3746. rat.

Organism-specific databases

CTD16625.
RGD3746. Serpina3k.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00740000115120.
HOGENOMHOG000238521.
HOVERGENHBG005957.
InParanoidP05545.
KOK04525.
OrthoDBEOG78M027.
PhylomeDBP05545.
TreeFamTF343201.

Gene expression databases

GenevestigatorP05545.

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

NextBio604434.

Entry information

Entry nameSPA3K_RAT
AccessionPrimary (citable) accession number: P05545
Secondary accession number(s): P14281, Q64254, Q6P6G8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 115 of the entry and version 3 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