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Protein
Submitted name:

Plasminogen activator inhibitor 1

Gene

Serpine1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: Ensembl

GO - Biological processi

  1. angiogenesis Source: Ensembl
  2. cellular response to lipopolysaccharide Source: Ensembl
  3. chronological cell aging Source: Ensembl
  4. defense response to Gram-negative bacterium Source: Ensembl
  5. negative regulation of cell adhesion mediated by integrin Source: Ensembl
  6. negative regulation of endothelial cell apoptotic process Source: Ensembl
  7. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  8. negative regulation of fibrinolysis Source: Ensembl
  9. negative regulation of plasminogen activation Source: Ensembl
  10. negative regulation of smooth muscle cell-matrix adhesion Source: Ensembl
  11. negative regulation of smooth muscle cell migration Source: Ensembl
  12. negative regulation of vascular wound healing Source: Ensembl
  13. positive regulation of angiogenesis Source: Ensembl
  14. positive regulation of interleukin-8 production Source: Ensembl
  15. positive regulation of leukotriene production involved in inflammatory response Source: Ensembl
  16. positive regulation of monocyte chemotaxis Source: Ensembl
  17. positive regulation of receptor-mediated endocytosis Source: Ensembl
  18. regulation of cell proliferation Source: Ensembl
  19. regulation of receptor activity Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_198757. ECM proteoglycans.
REACT_261099. Dissolution of Fibrin Clot.

Names & Taxonomyi

Protein namesi
Submitted name:
Plasminogen activator inhibitor 1Imported
Gene namesi
Name:Serpine1Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 12

Organism-specific databases

RGDi3249. Serpine1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: Ensembl
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000118839.
OMAiRMAPTEM.
OrthoDBiEOG7327PB.
TreeFamiTF352620.

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.

F1LM16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQMSSALTCL TLGLVLVFGK GFASPLPESH TAQQATNFGV KVFQHVVQAS
60 70 80 90 100
KDRNVVFSPY GVSSVLAMLQ LTTAGKTRQQ IQDAMGFNIS ERGTAPALRK
110 120 130 140 150
LSKELMGSWN KNEISTADAI FVQRDLELVQ GFMPHFFKLF RTTVKQVDFS
160 170 180 190 200
EMERARFIIN DWVERHTKGM ISDLLAKGAV NELTRLVLVN ALYFNGQWKT
210 220 230 240 250
PFLEASTHQR LFHKSDGSTI SVPMMAQNNK FNYTEFTTPD GHEYDILELP
260 270 280 290 300
YHGETLSMFI AAPFEKDVPL SAITNILDAE LIRQWKSNMT RLPRLLILPK
310 320 330 340 350
FSLETEVDLR GPLEKLGMTD IFSSTQADFT SLSDQEQLSV AQALQKVKIE
360 370 380 390 400
VNESGTVASS STAILVSARM APTEMVLDRS FLFVVRHNPT ETILFMGQLM

EP
Length:402
Mass (Da):45,042
Last modified:May 3, 2011 - v1
Checksum:i2B6397F7F475E403
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06071123 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000001916; ENSRNOP00000001916; ENSRNOG00000001414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06071123 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001916; ENSRNOP00000001916; ENSRNOG00000001414.

Organism-specific databases

RGDi3249. Serpine1.

Phylogenomic databases

GeneTreeiENSGT00760000118839.
OMAiRMAPTEM.
OrthoDBiEOG7327PB.
TreeFamiTF352620.

Enzyme and pathway databases

ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_198757. ECM proteoglycans.
REACT_261099. Dissolution of Fibrin Clot.

Miscellaneous databases

NextBioi35575367.
PROiF1LM16.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiF1LM16_RAT
AccessioniPrimary (citable) accession number: F1LM16
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: March 4, 2015
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.