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Database: UniProt
Entry: A0A2K6QYQ7_RHIRO
LinkDB: A0A2K6QYQ7_RHIRO
Original site: A0A2K6QYQ7_RHIRO 
ID   A0A2K6QYQ7_RHIRO        Unreviewed;       413 AA.
AC   A0A2K6QYQ7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Serpin family E member 2 {ECO:0000313|Ensembl:ENSRROP00000033908.1};
GN   Name=SERPINE2 {ECO:0000313|Ensembl:ENSRROP00000033908.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000033908.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000033908.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   AlphaFoldDB; A0A2K6QYQ7; -.
DR   STRING; 61622.ENSRROP00000033908; -.
DR   Ensembl; ENSRROT00000058350.1; ENSRROP00000033908.1; ENSRROG00000040515.1.
DR   GeneTree; ENSGT00940000158424; -.
DR   Proteomes; UP000233200; Unplaced.
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; 2.10.310.10; Serpins superfamily; 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:UP000233200}.
FT   DOMAIN          52..413
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   413 AA;  45678 MW;  BAAB86A71C487AB2 CRC64;
     VSDCLFGHES SLAEGTMNWH LPLFLLASVT LPSICSHFNP LSLEELGSNT GIQVFNQIVK
     SRPHDNIVIS PHGIASVLGM LQLGADGRTK KQLAMVMRYS VNGVGKILKK INKAIVSKKN
     KDIVTVANAV FVKNASEIEV PFITRNKDVF QCEVRNVNFE DPASACDSIN AWVKNETRDM
     IDNLLSPDLI DGVLTRLVLV NAVYFKGLWK SRFQPENTKK RTFVAADGKS YQVPMLAQLS
     VFRCGSTSAP NDLWYNFIEL PYHGESISML IALPTESSTP LSAIIPHIST KTIDSWMSIM
     VPKRVQVILP KFTAVAQTDL KEPLKVLGIT DMFDSSKANF AKITRSENLH VSHILQKAKI
     EVSEDGTKAS AATTAILIAR SSPPWFIVDR PFLFFIRHNP TGAVLFMGQI NKP
//
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