Q9JLD2 (NEUS_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the serpin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of cell adhesion Inferred from direct assay PubMed 12438159. Source: RGD regulation of proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from direct assay PubMed 12438159. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 410	394	Neuroserpin		PRO_0000032523
Sites
	Site	362 – 363	2	Reactive bond By similarity
Amino acid modifications
	Glycosylation	157	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	12	1	L → M in AAF70387. Ref.1
	Sequence conflict	177	1	H → Q in AAF70387. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9JLD2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 99008624B3A366D8	FASTA	410	46,278
	10 20 30 40 50 60 MAYLGLLSLV ALQSLVTGAA FPDETIAEWS VNVYNHLRAT GEDENILFSP LSIALAMGVM 70 80 90 100 110 120 ELGAQGSTLK EIRHSMGYES LKSGEEFSFL RDFSSMVSAE EGQYVMKIAN SLFVQNGFHI 130 140 150 160 170 180 NEEFLQMMKM YFNAEVNHVD FSENVAVANY INKWVENYTN SLLKDLVSPG DFDAVTHLAL 190 200 210 220 230 240 INAVYFKGNW KSQFRPENTR TFSFTKDDES EVQIPMMYQQ GEFYYGEFSD GSNEAGGIYQ 250 260 270 280 290 300 VLEIPYEGDE ISMMLVLSRQ EVPLATLEPL LKPQLIEEWA NSVKKQKVEV YLPRFTVEQE 310 320 330 340 350 360 IDLKDILKAL GVTEIFIKDA NLTAMSDKKE LFLSKAVHKS FIEVNEEGSE AAVASGMIAI 370 380 390 400 410 SRMAVLFPQV IVDHPFLFLI KNRKTGTILF MGRVMHPETM NTSGHDFEEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Neuroserpin is expressed in the pituitary and adrenal glands and induces the extension of neurite-like processes in AtT-20 cells." Hill R.M., Parmar P.K., Coates L.C., Mezey E., Pearson J.F., Birch N.P. Biochem. J. 345:595-601(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Pituitary.
[2]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF193014 mRNA. Translation: AAF70386.1. AF193015 mRNA. Translation: AAF70387.1. BC061536 mRNA. Translation: AAH61536.1.
IPI	IPI00203519.
RefSeq	NP_446231.1. NM_053779.1.
UniGene	Rn.52632.
3D structure databases
ProteinModelPortal	Q9JLD2.
SMR	Q9JLD2. Positions 25-64, 101-361, 367-397.
ModBase	Search...
Protein family/group databases
MEROPS	I04.025.
Proteomic databases
PaxDb	Q9JLD2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013904; ENSRNOP00000013905; ENSRNOG00000010248.
GeneID	116459.
KEGG	rno:116459.
UCSC	RGD:619896. rat.
Organism-specific databases
CTD	5274.
RGD	619896. Serpini1.
Phylogenomic databases
eggNOG	COG4826.
GeneTree	ENSGT00560000076706.
HOGENOM	HOG000238519.
HOVERGEN	HBG005957.
InParanoid	Q9JLD2.
OMA	MGYEGLK.
OrthoDB	EOG4DV5M8.
Gene expression databases
Genevestigator	Q9JLD2.
GermOnline	ENSRNOG00000010248. 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	618974.

Entry information

Entry name

NEUS_RAT

Accession

Primary (citable) accession number: Q9JLD2
Secondary accession number(s): Q9JLD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program