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P07093 (GDN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glia-derived nexin

Short name=GDN
Alternative name(s):
Peptidase inhibitor 7
Short name=PI-7
Protease nexin 1
Short name=PN-1
Protease nexin I
Serpin E2
Gene names
Name:SERPINE2
Synonyms:PI7, PN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 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 with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.

Subcellular location

Secretedextracellular space.

Sequence similarities

Belongs to the serpin family.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandHeparin-binding
   Molecular functionDevelopmental protein
Protease inhibitor
Serine protease inhibitor
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from electronic annotation. Source: Ensembl

cerebellar granular layer morphogenesis

Inferred from electronic annotation. Source: Ensembl

detection of mechanical stimulus involved in sensory perception

Inferred from electronic annotation. Source: Ensembl

innervation

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

mating plug formation

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood coagulation

Inferred from direct assay PubMed 17379830. Source: BHF-UCL

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

negative regulation of plasminogen activation

Inferred from mutant phenotype PubMed 19855083. Source: BHF-UCL

negative regulation of platelet activation

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet aggregation

Inferred from sequence or structural similarity PubMed 19855083. Source: BHF-UCL

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein processing

Inferred by curator PubMed 19855083. Source: BHF-UCL

negative regulation of proteolysis

Inferred from direct assay PubMed 17379830Ref.8. Source: BHF-UCL

negative regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of astrocyte differentiation

Inferred from direct assay PubMed 1691280. Source: BHF-UCL

regulation of cell migration

Non-traceable author statement Ref.2. Source: UniProtKB

regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

regulation of timing of cell differentiation

Inferred from electronic annotation. Source: Ensembl

secretion by cell

Inferred from electronic annotation. Source: Ensembl

secretory granule organization

Inferred from electronic annotation. Source: Ensembl

seminal vesicle epithelium development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 19855083. Source: BHF-UCL

extracellular matrix

Inferred from direct assay PubMed 3279057. Source: BHF-UCL

extracellular region

Inferred from direct assay Ref.8. Source: BHF-UCL

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

extrinsic component of external side of plasma membrane

Inferred from direct assay PubMed 19855083. Source: BHF-UCL

neuromuscular junction

Inferred from sequence or structural similarity PubMed 2037625. Source: BHF-UCL

platelet alpha granule

Inferred from mutant phenotype PubMed 19855083. Source: BHF-UCL

   Molecular_functionglycosaminoglycan binding

Inferred from direct assay PubMed 19855083. Source: BHF-UCL

heparin binding

Inferred from direct assay PubMed 1939253Ref.8. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 19911255. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 17379830. Source: BHF-UCL

serine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 19249338Ref.8. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07093-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07093-2)

The sequence of this isoform differs from the canonical sequence as follows:
     329-330: TG → R
Isoform 3 (identifier: P07093-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSDCRSSLVEGTM
     329-330: TG → R
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.8 Ref.9
Chain20 – 398379Glia-derived nexin
PRO_0000032504

Sites

Site365 – 3662Reactive bond Potential

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence11M → MSDCRSSLVEGTM in isoform 3.
VSP_043668
Alternative sequence329 – 3302TG → R in isoform 2 and isoform 3.
VSP_038367
Natural variant511I → M.
Corresponds to variant rs3795875 [ dbSNP | Ensembl ].
VAR_051955
Natural variant2041K → N in a breast cancer sample; somatic mutation. Ref.10
VAR_036027

Experimental info

Sequence conflict1591N → D in BAG35401. Ref.4
Sequence conflict2611S → E Ref.2

Secondary structure

......................................................................... 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 2A165604E2CBE6B8

FASTA39844,002
        10         20         30         40         50         60 
MNWHLPLFLL ASVTLPSICS HFNPLSLEEL GSNTGIQVFN QIVKSRPHDN IVISPHGIAS 

        70         80         90        100        110        120 
VLGMLQLGAD GRTKKQLAMV MRYGVNGVGK ILKKINKAIV SKKNKDIVTV ANAVFVKNAS 

       130        140        150        160        170        180 
EIEVPFVTRN KDVFQCEVRN VNFEDPASAC DSINAWVKNE TRDMIDNLLS PDLIDGVLTR 

       190        200        210        220        230        240 
LVLVNAVYFK GLWKSRFQPE NTKKRTFVAA DGKSYQVPML AQLSVFRCGS TSAPNDLWYN 

       250        260        270        280        290        300 
FIELPYHGES ISMLIALPTE SSTPLSAIIP HISTKTIDSW MSIMVPKRVQ VILPKFTAVA 

       310        320        330        340        350        360 
QTDLKEPLKV LGITDMFDSS KANFAKITTG SENLHVSHIL QKAKIEVSED GTKASAATTA 

       370        380        390 
ILIARSSPPW FIVDRPFLFF IRHNPTGAVL FMGQINKP 

« Hide

Isoform 2 [UniParc].

Checksum: 45A9C934A800D7EB
Show »

FASTA39744,000
Isoform 3 [UniParc].

Checksum: 6315691891B53A7B
Show »

FASTA40945,267

References

« Hide 'large scale' references
[1]"cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily."
Sommer J., Gloor S.M., Rovelli G.F., Hofsteenge J., Nick H., Meier R., Monard D.
Biochemistry 26:6407-6410(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins."
Gloor S.M., Odink K., Guenther J., Nick H., Monard D.
Cell 47:687-693(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning and expression of two forms of human protease nexin I."
McGrogan M., Kennedy J., Li M.P., Hsu C., Scott R.W., Simonsen C.C., Baker J.B.
Biotechnology (N.Y.) 6:172-177(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Hippocampus and Thalamus.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1 AND 2).
Tissue: Skin and Testis.
[8]"Protease nexin. Properties and a modified purification procedure."
Scott R.W., Bergman B.L., Bajpai A., Hersh R.T., Rodriguez H., Jones B.N., Barreda C., Watts S., Baker J.B.
J. Biol. Chem. 260:7029-7034(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-47, CHARACTERIZATION.
[9]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-34.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-204.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17783 mRNA. Translation: AAA35883.1.
AK295564 mRNA. Translation: BAG58464.1.
AK312499 mRNA. Translation: BAG35401.1.
AC073641 Genomic DNA. Translation: AAY14926.1.
CH471063 Genomic DNA. Translation: EAW70821.1.
CH471063 Genomic DNA. Translation: EAW70823.1.
BC015663 mRNA. Translation: AAH15663.1.
BC042628 mRNA. Translation: AAH42628.1.
CCDSCCDS2460.1. [P07093-1]
CCDS46525.1. [P07093-3]
CCDS46526.1. [P07093-2]
PIRA37274.
RefSeqNP_001130000.1. NM_001136528.1. [P07093-2]
NP_001130002.1. NM_001136530.1. [P07093-3]
NP_006207.1. NM_006216.3. [P07093-1]
XP_005246699.1. XM_005246642.1. [P07093-1]
UniGeneHs.38449.
Hs.708453.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DY0X-ray2.35A/B20-398[»]
4DY7X-ray2.80C/F20-398[»]
ProteinModelPortalP07093.
SMRP07093. Positions 21-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111288. 10 interactions.
STRING9606.ENSP00000415786.

Protein family/group databases

MEROPSI04.021.

PTM databases

PhosphoSiteP07093.

Polymorphism databases

DMDM121110.

Proteomic databases

MaxQBP07093.
PaxDbP07093.
PeptideAtlasP07093.
PRIDEP07093.

Protocols and materials databases

DNASU5270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258405; ENSP00000258405; ENSG00000135919. [P07093-1]
ENST00000409304; ENSP00000386412; ENSG00000135919. [P07093-2]
ENST00000409840; ENSP00000386969; ENSG00000135919. [P07093-2]
ENST00000447280; ENSP00000415786; ENSG00000135919. [P07093-3]
GeneID5270.
KEGGhsa:5270.
UCSCuc002vnu.2. human. [P07093-1]
uc002vnv.2. human. [P07093-2]
uc010zlr.1. human. [P07093-3]

Organism-specific databases

CTD5270.
GeneCardsGC02M224839.
HGNCHGNC:8951. SERPINE2.
HPAHPA051263.
MIM177010. gene.
neXtProtNX_P07093.
PharmGKBPA269.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOGENOMHOG000238519.
HOVERGENHBG106493.
InParanoidP07093.
KOK16643.
OMAIQVFNQI.
OrthoDBEOG7327PB.
PhylomeDBP07093.
TreeFamTF352620.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP07093.
BgeeP07093.
CleanExHS_SERPINE2.
GenevestigatorP07093.

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

ChiTaRSSERPINE2. human.
GeneWikiSERPINE2.
GenomeRNAi5270.
NextBio20360.
PMAP-CutDBP07093.
PROP07093.
SOURCESearch...

Entry information

Entry nameGDN_HUMAN
AccessionPrimary (citable) accession number: P07093
Secondary accession number(s): B2R6A4 expand/collapse secondary AC list , B4DIF2, Q53S15, Q5D0C4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM