Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O35684 (NEUS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Neuroserpin
Alternative name(s):
Peptidase inhibitor 12
Short name=PI-12
Serine protease inhibitor 17
Serpin I1
Gene names
Name:Serpini1
Synonyms:Pi12, Spi17
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator.

Subcellular location

Secreted.

Tissue specificity

During embryonic development mostly expressed in CNS. In adult expressed in brain and much less in spinal cord, heart, kidney and testis.

Sequence similarities

Belongs to the serpin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 410394Neuroserpin
PRO_0000032522

Sites

Site362 – 3632Reactive bond By similarity

Amino acid modifications

Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict51E → G in AAH06776. Ref.3

Secondary structure

......................................................... 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35684 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DA3AF6F5195EBB7C

FASTA41046,348
        10         20         30         40         50         60 
MTYLELLALL ALQSVVTGAT FPDETITEWS VNMYNHLRGT GEDENILFSP LSIALAMGMM 

        70         80         90        100        110        120 
ELGAQGSTRK EIRHSMGYEG LKGGEEFSFL RDFSNMASAE ENQYVMKLAN SLFVQNGFHV 

       130        140        150        160        170        180 
NEEFLQMLKM YFNAEVNHVD FSQNVAVANS INKWVENYTN SLLKDLVSPE DFDGVTNLAL 

       190        200        210        220        230        240 
INAVYFKGNW KSQFRPENTR TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ 

       250        260        270        280        290        300 
VLEIPYEGDE ISMMLALSRQ EVPLATLEPL LKAQLIEEWA NSVKKQKVEV YLPRFTVEQE 

       310        320        330        340        350        360 
IDLKDILKAL GVTEIFIKDA NLTAMSDKKE LFLSKAVHKS CIEVNEEGSE AAAASGMIAI 

       370        380        390        400        410 
SRMAVLYPQV IVDHPFLYLI RNRKSGIILF MGRVMNPETM NTSGHDFEEL 

« Hide

References

« Hide 'large scale' references
[1]"Expression of neuroserpin, an inhibitor of tissue plasminogen activator, in the developing and adult nervous system of the mouse."
Krueger S.R., Ghisu G.-P., Cinelli P., Gschwend T.P., Osterwalder T., Wolfer D.P., Sonderegger P.
J. Neurosci. 17:8984-8996(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Olfactory bulb and Spinal ganglion.
[3]"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].
[4]"Structure of the mouse gene for the serine protease inhibitor neuroserpin (PI12)."
Berger P., Kozlov S.V., Krueger S.R., Sonderegger P.
Gene 214:25-33(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE.
[5]"The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin."
Osterwalder T., Cinelli P., Baici A., Pennella A., Krueger S.R., Schrimpf S.P., Meins M., Sonderegger P.
J. Biol. Chem. 273:2312-2321(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Crystal structure of neuroserpin: a neuronal serpin involved in a conformational disease."
Briand C., Kozlov S.V., Sonderegger P., Gruetter M.G.
FEBS Lett. 505:18-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.06 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001700 mRNA. Translation: CAA04939.1.
AK032152 mRNA. Translation: BAC27727.1.
AK051756 mRNA. Translation: BAC34756.1.
BC006776 mRNA. Translation: AAH06776.1.
RefSeqNP_033276.1. NM_009250.2.
UniGeneMm.41560.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JJOX-ray3.06A/B25-64[»]
C/D101-361[»]
E/F367-397[»]
ProteinModelPortalO35684.
SMRO35684. Positions 22-400.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI04.025.

PTM databases

PhosphoSiteO35684.

Proteomic databases

PaxDbO35684.
PRIDEO35684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029423; ENSMUSP00000029423; ENSMUSG00000027834.
GeneID20713.
KEGGmmu:20713.
UCSCuc008pne.2. mouse.

Organism-specific databases

CTD5274.
MGIMGI:1194506. Serpini1.

Phylogenomic databases

eggNOGCOG4826.
GeneTreeENSGT00740000115014.
HOGENOMHOG000238519.
HOVERGENHBG005957.
InParanoidO35684.
OMAINEWANS.
PhylomeDBO35684.
TreeFamTF352620.

Gene expression databases

ArrayExpressO35684.
BgeeO35684.
GenevestigatorO35684.

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

EvolutionaryTraceO35684.
NextBio299293.
PROO35684.
SOURCESearch...

Entry information

Entry nameNEUS_MOUSE
AccessionPrimary (citable) accession number: O35684
Secondary accession number(s): Q543F7, Q922U6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 117 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot