ID A0A087RDX1_APTFO Unreviewed; 561 AA.
AC A0A087RDX1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Hepatocyte growth factor activator {ECO:0000313|EMBL:KFM11675.1};
DE Flags: Fragment;
GN ORFNames=AS27_15294 {ECO:0000313|EMBL:KFM11675.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM11675.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM11675.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM11675.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00479}.
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DR EMBL; KL226318; KFM11675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087RDX1; -.
DR STRING; 9233.A0A087RDX1; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
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; PTHR24264:SF43; HEPATOCYTE GROWTH FACTOR ACTIVATOR; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57603; FnI-like domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 22..69
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 74..112
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 114..154
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 155..193
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 199..281
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 318..556
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 83..100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 102..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 164..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 183..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM11675.1"
FT NON_TER 561
FT /evidence="ECO:0000313|EMBL:KFM11675.1"
SQ SEQUENCE 561 AA; 63182 MW; EC274A76EF6D16F4 CRC64;
HYKSEAGRGS KHEFTLPQVF TEDGNLCKFP FRYGGRFYHS CLSNLFSRKK WCSTTHNHDR
DRRWGHCASL PKDHSDHCAN NPCQNGGTCS LTHGHRMYHC TCPEEFTGEN CQMKKCFDNS
LYEFFDVGMS WSRVQQGAVE QCVCVNGQIE CESVKHKSCV RDPCMNGGEC KMVIFSGKIV
CDCKGNYAGK YCNIVPSHRC YVGNGTEYRG MAKTTVSGHS CLPWDSDLLY QELHVDSVEQ
AVQLGLGSFS YCRNPDDDEK PWCYIMKDDS LSWEYCDIPS CASRERRPPL PDNVDSSAVT
RRPCGRRHKK RSFVRPRIVG GSSSLPGSHP WTAAIYIGES FCGGSLIQTC WVVSAAHCFA
NSPLKSTITV VLGQHIFNRT TDVTQTFEIE KYILHPQYSV FNPTEHDIAL IKLKKNGQRC
AVKSQFVQPI CLPESNTVFP DQFKCQISGW GHRHENISGY SNVLQETLIP IIPEEKCRSP
EIYGTEITEN MFCAGYFDSK SDACQGDSGG PLACEKNDIS YLYGVISWGD GCGRVNKPGV
YTRMTNYVNW INEKIAPRKT S
//
