Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05545

- SPA3K_RAT

UniProt

P05545 - SPA3K_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Serine protease inhibitor A3K

Gene

Serpina3k

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

Functioni

Binds to and inhibits kallikreins. Inhibits trypsin but not chymotrypsin or elastase.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei379 – 3802Reactive bondBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of angiogenesis Source: RGD
  2. negative regulation of endothelial cell proliferation Source: RGD
  3. positive regulation of apoptotic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI04.051.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Serpina3k
Synonyms:Spin2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi3746. Serpina3k.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 416396Serine protease inhibitor A3KPRO_0000032421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP05545.
PRIDEiP05545.

PTM databases

PhosphoSiteiP05545.

Expressioni

Tissue specificityi

Liver and plasma.3 Publications

Inductioni

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.4 Publications

Gene expression databases

GenevestigatoriP05545.

Interactioni

Protein-protein interaction databases

IntActiP05545. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP05545.
SMRiP05545. Positions 45-415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni365 – 39228RCLAdd
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 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.By similarity1 Publication

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP05545.
KOiK04525.
OrthoDBiEOG78M027.
PhylomeDBiP05545.
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.

P05545-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFIAALGLL MAGICPAVLC DGILGRDTLP HEDQGKGRQL HSLTLASINT
60 70 80 90 100
DFTLSLYKKL ALRNPDKNVV FSPLSISAAL AILSLGAKDS TMEEILEVLK
110 120 130 140 150
FNLTEITEEE IHQGFGHLLQ RLSQPEDQAE INTGSALFID KEQPILSEFQ
160 170 180 190 200
EKTRALYQAE AFVADFKQCN EAKKFINDYV SNQTQGKIAE LFSELDERTS
210 220 230 240 250
MVLVNYLLFK GKWKVPFNPN DTFESEFYLD EKRSVKVPMM KIKDLTTPYI
260 270 280 290 300
RDEELSCSVL ELKYTGNASA LFILPDQGKM QQVESSLQPE TLKKWKDSLR
310 320 330 340 350
PRIISELRMP KFSISTDYNL EEVLPELGIR KIFSQQADLS RITGTKNLHV
360 370 380 390 400
SQVVHKAVLD VDETGTEGAA ATAVTAALKS LPQTIPLLNF NRPFMLVITD
410
NNGQSVFFMG KVTNPM
Length:416
Mass (Da):46,562
Last modified:April 1, 1993 - v3
Checksum:i6072BAE56BFF91B1
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301P → S AA sequence (PubMed:2398056)Curated
Sequence conflicti47 – 471S → A AA sequence (PubMed:2398056)Curated
Sequence conflicti98 – 981V → G in AAA42173. (PubMed:3494016)Curated
Sequence conflicti98 – 981V → G in BAA00648. (PubMed:1864837)Curated
Sequence conflicti98 – 981V → G in AAH62236. (PubMed:15489334)Curated
Sequence conflicti112 – 1121H → HH in CAA34407. (PubMed:1694763)Curated
Sequence conflicti194 – 1941E → D in BAA00648. (PubMed:1864837)Curated
Sequence conflicti250 – 2501I → V in BAA00648. (PubMed:1864837)Curated
Sequence conflicti326 – 3261E → D in CAA34409. (PubMed:2258058)Curated
Sequence conflicti385 – 3851I → V in BAA00648. (PubMed:1864837)Curated
Sequence conflicti387 – 3871L → P in CAA34407. (PubMed:1694763)Curated
Sequence conflicti401 – 4011N → D in AAH62236. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261E → D.1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA29035.
B29131.
RefSeqiNP_036789.2. NM_012657.2.
XP_006240520.1. XM_006240458.2.
UniGeneiRn.91257.
Rn.97597.

Genome annotation databases

EnsembliENSRNOT00000013896; ENSRNOP00000013896; ENSRNOG00000010410.
GeneIDi24794.
KEGGirno:24794.
UCSCiRGD:3746. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi A29035.
B29131.
RefSeqi NP_036789.2. NM_012657.2.
XP_006240520.1. XM_006240458.2.
UniGenei Rn.91257.
Rn.97597.

3D structure databases

ProteinModelPortali P05545.
SMRi P05545. Positions 45-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P05545. 1 interaction.

Protein family/group databases

MEROPSi I04.051.

PTM databases

PhosphoSitei P05545.

Proteomic databases

PaxDbi P05545.
PRIDEi P05545.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000013896 ; ENSRNOP00000013896 ; ENSRNOG00000010410 .
GeneIDi 24794.
KEGGi rno:24794.
UCSCi RGD:3746. rat.

Organism-specific databases

CTDi 16625.
RGDi 3746. Serpina3k.

Phylogenomic databases

eggNOGi COG4826.
GeneTreei ENSGT00760000118839.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P05545.
KOi K04525.
OrthoDBi EOG78M027.
PhylomeDBi P05545.
TreeFami TF343201.

Miscellaneous databases

NextBioi 604434.

Gene expression databases

Genevestigatori P05545.

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. "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.

Entry informationi

Entry nameiSPA3K_RAT
AccessioniPrimary (citable) accession number: P05545
Secondary accession number(s): P14281, Q64254, Q6P6G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3