ID A0A091DVM4_FUKDA Unreviewed; 550 AA.
AC A0A091DVM4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Plasma kallikrein {ECO:0000313|EMBL:KFO35137.1};
GN ORFNames=H920_03467 {ECO:0000313|EMBL:KFO35137.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO35137.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO35137.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO35137.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KN121883; KFO35137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091DVM4; -.
DR STRING; 885580.ENSFDAP00000017437; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01100; APPLE_Factor_XI_like; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.50.4.10; Hepatocyte Growth Factor; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR000177; Apple.
DR InterPro; IPR003609; Pan_app.
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; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00024; PAN_1; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00005; APPLEDOMAIN.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00223; APPLE; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57414; Hairpin loop containing domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00495; APPLE; 1.
DR PROSITE; PS50948; PAN; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..550
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001873481"
FT DOMAIN 21..104
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 204..287
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 303..538
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 550 AA; 61225 MW; 0987F74A716766EC CRC64;
MFTFKKAAYF ICLFGTVSCA CHRDIYEGID MRGANFNVSK VKSVEECQTL CTNNIHCQFF
TFATQTFHNA EYRNCCLLKH SPSGTPTGIK TLNNVVSGFS LKPCALSEFG CRMDLFQHLA
FADMNVARVI TPDAFVCRTI CTYHPSCLFF TFYTNAWTTE SQRQVNACFL KTSKSGTPSS
FTPQENTISG HSLSTCKTTL PEPCLSKIYS GVAFGGEELN VTFVKGASVC QESCTKTIRC
QFFTYSLLPE DCKGEKCKCS LRLSLDGSPT RITYGTQRSS GYSLRLCKTG ESSVCTTKTN
ARIVGGTNSS WGEWPWQVSL QVKVTSSSHL CGGSLIAPQW VLTAAHCFDG IPFPDVWRIY
GGILNLSEIT KETSFSQIKE LIIHEKYKLS ETGHDIALIK LQAPLNYTEF QKPICLPSKD
DGNIIYTNCW VTGWGYNKEK GEIQNILQKT RIPLVTNEEC QKRYKDYVIT KQMICAGYKE
GGKDACKGDS GGPLVCKHNG MWRLVGITSW GEGCARKEQP GVYTKVAEYV DWILEKTQKD
DRSALMVSPA
//
