ID G1KCT2_ANOCA Unreviewed; 396 AA.
AC G1KCT2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Serpin family E member 2 {ECO:0000313|Ensembl:ENSACAP00000004313.3};
GN Name=SERPINE2 {ECO:0000313|Ensembl:ENSACAP00000004313.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000004313.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000004313.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000004313.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000004313.3}
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 RefSeq; XP_003218312.1; XM_003218264.3.
DR AlphaFoldDB; G1KCT2; -.
DR STRING; 28377.ENSACAP00000004313; -.
DR MEROPS; I04.021; -.
DR Ensembl; ENSACAT00000004413.4; ENSACAP00000004313.3; ENSACAG00000004328.4.
DR GeneID; 100559583; -.
DR KEGG; acs:100559583; -.
DR CTD; 5270; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000158424; -.
DR HOGENOM; CLU_023330_0_4_1; -.
DR InParanoid; G1KCT2; -.
DR OMA; PNNTKMR; -.
DR OrthoDB; 3218836at2759; -.
DR TreeFam; TF352620; -.
DR Proteomes; UP000001646; Chromosome 3.
DR Bgee; ENSACAG00000004328; Expressed in testis and 13 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; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..396
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003412713"
FT DOMAIN 35..396
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 396 AA; 44047 MW; 9A4EA536513DEC78 CRC64;
MDWQFALLFV ALTSTCMCFP PNPMSLEELG SDIGIQVFNQ LVKSRPKDNV VVSPHGIASV
LGMLQLGADG KTKKQLTTVM RYSVNGVGKV LKKINKAIVA KRNKDLVTIA NAVFAKSGLK
MEVPFVSRNN DVFQCSVKSI DFEDKDSACD TVNHWVRNKT KGMIDSILSP DDIDSALTRL
ILVNAIYFKG LWKSRFQPEN TKKRTFTAAD GKTYQVPMLA QLSVFRCGTT STPNDLWYNI
IELPYHGETI SMLIALPTES TTPLSAIIPH ISTKTIQSWM TTMVQKRVQV ILPKFTVEAE
TDLKEPLQEL GIRDMFEQSK ANFLKITRTA SIHVSQILQK AKIEVSEDGT KASAATTAIL
IARSSPPWFV VDRAFVFFIR HNPTGAVLFM GQVNKP
//
