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Database: UniProt
Entry: G3S7C3_GORGO
LinkDB: G3S7C3_GORGO
Original site: G3S7C3_GORGO 
ID   G3S7C3_GORGO            Unreviewed;       491 AA.
AC   G3S7C3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Serpin family F member 2 {ECO:0000313|Ensembl:ENSGGOP00000023981.1};
GN   Name=SERPINF2 {ECO:0000313|Ensembl:ENSGGOP00000023981.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000023981.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000023981.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000023981.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000023981.1}
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   EMBL; CABD030103027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004058283.1; XM_004058235.2.
DR   AlphaFoldDB; G3S7C3; -.
DR   STRING; 9593.ENSGGOP00000023981; -.
DR   MEROPS; I04.023; -.
DR   Ensembl; ENSGGOT00000034363.2; ENSGGOP00000023981.1; ENSGGOG00000026220.2.
DR   GeneID; 101127494; -.
DR   KEGG; ggo:101127494; -.
DR   CTD; 5345; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000158386; -.
DR   HOGENOM; CLU_023330_3_2_1; -.
DR   InParanoid; G3S7C3; -.
DR   OMA; HAYPLRW; -.
DR   OrthoDB; 3218836at2759; -.
DR   TreeFam; TF317350; -.
DR   Proteomes; UP000001519; Chromosome 17.
DR   Bgee; ENSGGOG00000026220; Expressed in liver and 6 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; IEA:Ensembl.
DR   GO; GO:0051918; P:negative regulation of fibrinolysis; IEA:Ensembl.
DR   GO; GO:0010757; P:negative regulation of plasminogen activation; IEA:Ensembl.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IEA:Ensembl.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl.
DR   CDD; cd02053; serpinF2_A2AP; 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; IPR033833; Alpha2AP_serpin_dom.
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:SF20; ALPHA-2-ANTIPLASMIN; 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:UP000001519};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..491
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003453328"
FT   DOMAIN          91..436
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          55..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  54623 MW;  1C78D7C835AE1795 CRC64;
     MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVPPLTLL KLGNQEPGGQ
     TALKSPPGIC SRDPTPEQTR RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL
     ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE
     QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF
     WRNKFDPSLT QRESFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV
     LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF
     QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF
     EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM
     EEDYPQFGSP K
//
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