GDN_MOUSE
ID GDN_MOUSE Reviewed; 397 AA.
AC Q07235; Q921T7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glia-derived nexin;
DE Short=GDN;
DE AltName: Full=Peptidase inhibitor 7;
DE Short=PI-7;
DE AltName: Full=Protease nexin 1;
DE Short=PN-1;
DE AltName: Full=Protease nexin I;
DE AltName: Full=Serine protease-inhibitor 4;
DE AltName: Full=Serpin E2;
DE Flags: Precursor;
GN Name=Serpine2; Synonyms=Pi7, Pn1, Spi4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Belin D.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-366.
RC STRAIN=BALB/cJ;
RX PubMed=8491179; DOI=10.1002/j.1460-2075.1993.tb05835.x;
RA Vassalli J.-D., Huarte J., Bosco D., Sappino A.P., Sappino N., Velardi A.,
RA Wohlwend A., Erno H., Monard D., Belin D.;
RT "Protease-nexin I as an androgen-dependent secretory product of the murine
RT seminal vesicle.";
RL EMBO J. 12:1871-1878(1993).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine protease inhibitor with activity toward thrombin,
CC trypsin, and urokinase. Promotes neurite extension by inhibiting
CC thrombin. Binds heparin.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Most abundant in seminal vesicles.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; X70296; CAA49777.1; -; mRNA.
DR EMBL; BC010675; AAH10675.1; -; mRNA.
DR EMBL; X70946; CAA50285.1; -; Genomic_DNA.
DR CCDS; CCDS15092.1; -.
DR PIR; I48717; I48717.
DR RefSeq; NP_033281.1; NM_009255.4.
DR RefSeq; XP_006496522.1; XM_006496459.3.
DR AlphaFoldDB; Q07235; -.
DR SMR; Q07235; -.
DR BioGRID; 203445; 6.
DR IntAct; Q07235; 1.
DR MINT; Q07235; -.
DR STRING; 10090.ENSMUSP00000027467; -.
DR MEROPS; I04.021; -.
DR GlyConnect; 2336; 1 N-Linked glycan (1 site).
DR GlyGen; Q07235; 2 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q07235; -.
DR CPTAC; non-CPTAC-3982; -.
DR EPD; Q07235; -.
DR PaxDb; Q07235; -.
DR PeptideAtlas; Q07235; -.
DR PRIDE; Q07235; -.
DR ProteomicsDB; 273043; -.
DR ABCD; Q07235; 4 sequenced antibodies.
DR Antibodypedia; 34366; 391 antibodies from 31 providers.
DR DNASU; 20720; -.
DR Ensembl; ENSMUST00000027467; ENSMUSP00000027467; ENSMUSG00000026249.
DR GeneID; 20720; -.
DR KEGG; mmu:20720; -.
DR UCSC; uc007bqz.2; mouse.
DR CTD; 5270; -.
DR MGI; MGI:101780; Serpine2.
DR VEuPathDB; HostDB:ENSMUSG00000026249; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158424; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; Q07235; -.
DR OMA; DSINMWV; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q07235; -.
DR TreeFam; TF352620; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-75205; Dissolution of Fibrin Clot.
DR BioGRID-ORCS; 20720; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Serpine2; mouse.
DR PRO; PR:Q07235; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q07235; protein.
DR Bgee; ENSMUSG00000026249; Expressed in seminal vesicle and 323 other tissues.
DR ExpressionAtlas; Q07235; baseline and differential.
DR Genevisible; Q07235; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IGI:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021683; P:cerebellar granular layer morphogenesis; IMP:MGI.
DR GO; GO:0061110; P:dense core granule biogenesis; ISO:MGI.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:MGI.
DR GO; GO:0060384; P:innervation; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0042628; P:mating plug formation; IMP:MGI.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IMP:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IGI:MGI.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; IMP:BHF-UCL.
DR GO; GO:0010544; P:negative regulation of platelet activation; IMP:BHF-UCL.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:BHF-UCL.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; IC:BHF-UCL.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; IMP:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0032940; P:secretion by cell; IMP:MGI.
DR GO; GO:0033363; P:secretory granule organization; IMP:MGI.
DR GO; GO:0061108; P:seminal vesicle epithelium development; IMP:MGI.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Glycoprotein; Heparin-binding;
KW Neurogenesis; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..397
FT /note="Glia-derived nexin"
FT /id="PRO_0000032505"
FT SITE 364..365
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 313
FT /note="I -> V (in Ref. 2; AAH10675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44207 MW; B8EBAE3CA899D4A5 CRC64;
MNWHFPFFIL TTVTLYSVHS QFNSLSLEEL GSNTGIQVFN QIIKSRPHEN VVVSPHGIAS
ILGMLQLGAD GKTKKQLSTV MRYNVNGVGK VLKKINKAIV SKKNKDIVTV ANAVFLRNGF
KMEVPFAVRN KDVFQCEVQN VNFQDPASAS ESINFWVKNE TRGMIDNLLS PNLIDGALTR
LVLVNAVYFK GLWKSRFQPE STKKRTFVAG DGKSYQVPML AQLSVFRSGS TRTPNGLWYN
FIELPYHGES ISMLIALPTE SSTPLSAIIP HITTKTIDSW MNTMVPKRMQ LVLPKFTAVA
QTDLKEPLKA LGITEMFEPS KANFTKITRS ESLHVSHILQ KAKIEVSEDG TKASAATTAI
LIARSSPPWF IVDRPFLFSI RHNPTGAILF LGQVNKP
