GenomeNet

Database: UniProt
Entry: G3URX3_MELGA
LinkDB: G3URX3_MELGA
Original site: G3URX3_MELGA 
ID   G3URX3_MELGA            Unreviewed;       456 AA.
AC   G3URX3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Serpin family E member 2 {ECO:0000313|Ensembl:ENSMGAP00000018441.2};
GN   Name=SERPINE2 {ECO:0000313|Ensembl:ENSMGAP00000018441.2};
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000018441.2, ECO:0000313|Proteomes:UP000001645};
RN   [1] {ECO:0000313|Ensembl:ENSMGAP00000018441.2, ECO:0000313|Proteomes:UP000001645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA   Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA   Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA   Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA   Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA   Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA   Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA   Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA   Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA   Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA   Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA   Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA   Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA   Zhang Y., Reed K.M.;
RT   "Multi-platform next-generation sequencing of the domestic turkey
RT   (Meleagris gallopavo): genome assembly and analysis.";
RL   PLoS Biol. 8:E1000475-E1000475(2010).
RN   [2] {ECO:0000313|Ensembl:ENSMGAP00000018441.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   AlphaFoldDB; G3URX3; -.
DR   MEROPS; I04.021; -.
DR   Ensembl; ENSMGAT00000018687.2; ENSMGAP00000018441.2; ENSMGAG00000004930.3.
DR   GeneTree; ENSGT00940000158424; -.
DR   InParanoid; G3URX3; -.
DR   OrthoDB; 3218836at2759; -.
DR   TreeFam; TF352620; -.
DR   Proteomes; UP000001645; Chromosome 11.
DR   Bgee; ENSMGAG00000004930; Expressed in testis and 17 other cell types or tissues.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0021683; P:cerebellar granular layer morphogenesis; IEA:Ensembl.
DR   GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IEA:Ensembl.
DR   GO; GO:0060384; P:innervation; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0042628; P:mating plug formation; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0010757; P:negative regulation of plasminogen activation; IEA:Ensembl.
DR   GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl.
DR   GO; GO:0010766; P:negative regulation of sodium ion transport; IEA:Ensembl.
DR   GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
DR   GO; GO:0032940; P:secretion by cell; IEA:Ensembl.
DR   GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
DR   GO; GO:0061108; P:seminal vesicle epithelium development; IEA:Ensembl.
DR   CDD; cd19573; serpinE2_GDN; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   Gene3D; 1.10.287.580; Helix hairpin bin; 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:SF48; GLIA-DERIVED NEXIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5032943256"
FT   DOMAIN          49..456
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          99..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50861 MW;  4C0F20170718FA82 CRC64;
     MRSRCGLGDF QPEIMNWHFS LLFLLGTLTS VCSQFNFYPL EELSSDVGIQ VFNQIVKAKP
     QDNVVVSPHG IASVLGVLQL GADGKTKKQL TTMMRYSVNG AENPPRAAGS KEESQHHETS
     QLSPDHQQVL RGPPVVHRIQ FENLCYGVGK ALKKINRLIV SKKNKDIVTI ANAVFAKSGF
     KMEVPFVTRN KEVFQCSVKS VDFEDPNTAC DSINQWVKNE TRGMIDQVVA PDDIDSLTRL
     VLVNAVYFKG LWKSRFRPEN TKKRPFHGAD GKVYQVPMLS QLSIFRCGTT STPNELWYNI
     IELPYHGEMI SMLIALPTEN ATPLSAIIPH ISTKTIGSWM TTMVAKRVQV ILPKFTAVAE
     TDLKDPLKAL GITDMFDESK SNFAKITRTE GLHVSHVLQK TKIEVSEDGT KASAATTAIL
     IARSSPPWFI VDRPFVFFIR HNPTGTILFM GQINKP
//
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