Serine protease inhibitor A3K precursor

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P05545 (SPA3K_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	416 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	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.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	extracellular region Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.9

Chain

21 – 416

396

Serine protease inhibitor A3K

PRO_0000032421

Regions

Region

365 – 392

RCL

Sites

Site

379 – 380

Reactive bond By similarity

Amino acid modifications

Glycosylation

102

N-linked (GlcNAc...) Potential

Glycosylation

182

N-linked (GlcNAc...) Potential

Glycosylation

220

N-linked (GlcNAc...) Potential

Glycosylation

267

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

326

E → D. Ref.5

Experimental info

Sequence conflict

P → S AA sequence Ref.9

Sequence conflict

S → A AA sequence Ref.9

Sequence conflict

V → G in AAA42173. Ref.3

Sequence conflict

V → G in BAA00648. Ref.6

Sequence conflict

V → G in AAH62236. Ref.8

Sequence conflict

112

H → HH in CAA34407. Ref.4

Sequence conflict

194

E → D in BAA00648. Ref.6

Sequence conflict

250

I → V in BAA00648. Ref.6

Sequence conflict

326

E → D in CAA34409. Ref.5

Sequence conflict

385

I → V in BAA00648. Ref.6

Sequence conflict

387

L → P in CAA34407. Ref.4

Sequence conflict

401

N → D in AAH62236. Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

P05545 [UniParc].

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

416

46,562

        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' referencesShow '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, 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.
IPI	IPI00200593.
PIR	A29035. B29131.
RefSeq	NP_036789.2. NM_012657.2.
UniGene	Rn.91257. Rn.97597.
3D structure databases
ProteinModelPortal	P05545.
SMR	P05545. Positions 45-415.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05545. 1 interaction.
Protein family/group databases
MEROPS	I04.051.
PTM databases
PhosphoSite	P05545.
Proteomic databases
PaxDb	P05545.
PRIDE	P05545.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013896; ENSRNOP00000013896; ENSRNOG00000010410.
GeneID	24794.
KEGG	rno:24794.
UCSC	RGD:3746. rat.
Organism-specific databases
CTD	20714.
RGD	3746. Serpina3k.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00700000104184.
HOGENOM	HOG000238521.
HOVERGEN	HBG005957.
InParanoid	P05545.
KO	K04525.
OrthoDB	EOG4FFD1T.
Gene expression databases
Genevestigator	P05545.
GermOnline	ENSRNOG00000010410. Rattus norvegicus.
Family and domain databases
InterPro	IPR023795. Protease_inhib_I4_serpin_CS. IPR023796. Serpin_dom. IPR000215. Serpin_fam. [Graphical view]
PANTHER	PTHR11461. PTHR11461. 1 hit.
Pfam	PF00079. Serpin. 1 hit. [Graphical view]
SMART	SM00093. SERPIN. 1 hit. [Graphical view]
SUPFAM	SSF56574. Prot_inh_serpin. 1 hit.
PROSITE	PS00284. SERPIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604434.

Entry information

Entry name

SPA3K_RAT

Accession

Primary (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 3, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents