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Database: UniProt
Entry: A0A2K6NTM2_RHIRO
LinkDB: A0A2K6NTM2_RHIRO
Original site: A0A2K6NTM2_RHIRO 
ID   A0A2K6NTM2_RHIRO        Unreviewed;       382 AA.
AC   A0A2K6NTM2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Coagulation factor VII {ECO:0000313|Ensembl:ENSRROP00000007621.1};
GN   Name=F7 {ECO:0000313|Ensembl:ENSRROP00000007621.1};
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:ENSRROP00000007621.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000007621.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A2K6NTM2; -.
DR   Ensembl; ENSRROT00000031244.1; ENSRROP00000007621.1; ENSRROG00000027792.1.
DR   GeneTree; ENSGT00940000154474; -.
DR   OMA; QGRNCET; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF26; COAGULATION FACTOR VII; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..382
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014414683"
FT   DOMAIN          22..58
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          129..368
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        320
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   DISULFID        48..57
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   382 AA;  41743 MW;  FE247F0C16080F2F CRC64;
     MVSQALGLLC LLLGLQGCLA ADGDQCASNP CQNGGSCKDQ LQSYICFCLP SFEGRNCEKN
     KDDQLICVNE NGGCEQYCSD HTGAKRSCWC HEGYSLLADG VSCMPTVEHP CGKIPILEKR
     NTSKPQGRIV GGTVCPKGEC PWQVLLLVNG AQLCGGTLIN TLWVVSAAHC FDKIKSWRNL
     TAVLGEHDLS EHEGDEQSRR VAQVIIPSTY VPGTTNHDIA LLRLQRPVVL TDHVVPLCLP
     ERTFSERTLA FVRFSLVSGW GQLLDRGATA LELMALSVPR LMTQDCLQQS RKVDASPNIT
     EYMFCAGYSD GSKDSCKGDS GGPHATRYRG TWYLTGVVSW GQGCAAVGHF GVYTRVSQYI
     EWLQKLMRSE PHPGVLLRAP FP
//
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