GDN_RAT
ID GDN_RAT Reviewed; 397 AA.
AC P07092;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=Serpin E2;
DE Flags: Precursor;
GN Name=Serpine2; Synonyms=Pi7, Pn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3427015; DOI=10.1021/bi00394a016;
RA Sommer J., Gloor S.M., Rovelli G.F., Hofsteenge J., Nick H., Meier R.,
RA Monard D.;
RT "cDNA sequence coding for a rat glia-derived nexin and its homology to
RT members of the serpin superfamily.";
RL Biochemistry 26:6407-6410(1987).
RN [2]
RP PROTEIN SEQUENCE OF 82-96; 165-178 AND 317-333, AND HEPARIN-BINDING.
RX PubMed=1554734; DOI=10.1021/bi00128a031;
RA Rovelli G., Stone S.R., Guidolin A., Sommer J., Monard D.;
RT "Characterization of the heparin-binding site of glia-derived
RT nexin/protease nexin-1.";
RL Biochemistry 31:3542-3549(1992).
RN [3]
RP PROTEIN SEQUENCE OF 133-153 AND 347-397, AND FUNCTION.
RX PubMed=2337608; DOI=10.1021/bi00461a027;
RA Nick H., Hofsteenge J., Shaw E., Rovelli G., Monard D.;
RT "Functional sites of glia-derived nexin (GDN): importance of the site
RT reacting with the protease.";
RL Biochemistry 29:2417-2421(1990).
CC -!- FUNCTION: Serine protease inhibitor with activity toward thrombin,
CC trypsin, and urokinase. Promotes neurite extension by inhibiting
CC thrombin. Binds heparin. {ECO:0000269|PubMed:2337608}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; M17784; AAA41209.1; -; mRNA.
DR PIR; B27496; B27496.
DR RefSeq; NP_062070.1; NM_019197.1.
DR AlphaFoldDB; P07092; -.
DR SMR; P07092; -.
DR BioGRID; 248020; 2.
DR IntAct; P07092; 1.
DR STRING; 10116.ENSRNOP00000020919; -.
DR MEROPS; I04.021; -.
DR GlyGen; P07092; 1 site.
DR PhosphoSitePlus; P07092; -.
DR jPOST; P07092; -.
DR PaxDb; P07092; -.
DR PRIDE; P07092; -.
DR GeneID; 29366; -.
DR KEGG; rno:29366; -.
DR UCSC; RGD:3748; rat.
DR CTD; 5270; -.
DR RGD; 3748; Serpine2.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P07092; -.
DR PhylomeDB; P07092; -.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-75205; Dissolution of Fibrin Clot.
DR PRO; PR:P07092; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021683; P:cerebellar granular layer morphogenesis; ISO:RGD.
DR GO; GO:0061110; P:dense core granule biogenesis; IDA:RGD.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR GO; GO:0060384; P:innervation; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0042628; P:mating plug formation; ISO:RGD.
DR GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010466; P:negative regulation of peptidase activity; ISO:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0010757; P:negative regulation of plasminogen activation; ISO:RGD.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISO:RGD.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0048711; P:positive regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; ISO:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; ISO:RGD.
DR GO; GO:0032940; P:secretion by cell; ISO:RGD.
DR GO; GO:0033363; P:secretory granule organization; IDA:RGD.
DR GO; GO:0061108; P:seminal vesicle epithelium development; ISO:RGD.
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; Direct protein sequencing;
KW Glycoprotein; Heparin-binding; Neurogenesis; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..397
FT /note="Glia-derived nexin"
FT /id="PRO_0000032506"
FT SITE 364..365
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 397 AA; 44063 MW; 11EF0790C7297646 CRC64;
MNWHFPFFIL TTVTLSSVYS QLNSLSLEEL GSDTGIQVFN QIIKSQPHEN VVISPHGIAS
ILGMLQLGAD GRTKKQLSTV MRYNVNGVGK VLKKINKAIV SKKNKDIVTV ANAVFVRNGF
KVEVPFAARN KEVFQCEVQS VNFQDPASAC DAINFWVKNE TRGMIDNLLS PNLIDSALTK
LVLVNAVYFK GLWKSRFQPE NTKKRTFVAG DGKSYQVPML AQLSVFRSGS TKTPNGLWYN
FIELPYHGES ISMLIALPTE SSTPLSAIIP HISTKTINSW MNTMVPKRMQ LVLPKFTALA
QTDLKEPLKA LGITEMFEPS KANFAKITRS ESLHVSHILQ KAKIEVSEDG TKAAVVTTAI
LIARSSPPWF IVDRPFLFCI RHNPTGAILF LGQVNKP
