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Database: UniProt
Entry: F6YRB8_XENTR
LinkDB: F6YRB8_XENTR
Original site: F6YRB8_XENTR 
ID   F6YRB8_XENTR            Unreviewed;       629 AA.
AC   F6YRB8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Kallikrein B1 {ECO:0000313|Ensembl:ENSXETP00000012912};
DE   SubName: Full=Plasma kallikrein {ECO:0000313|RefSeq:XP_002934450.3, ECO:0000313|RefSeq:XP_004911242.2};
GN   Name=klkb1 {ECO:0000313|Ensembl:ENSXETP00000012912,
GN   ECO:0000313|RefSeq:XP_002934450.3, ECO:0000313|RefSeq:XP_004911242.2,
GN   ECO:0000313|Xenbase:XB-GENE-985051};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000012912};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000012912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000012912};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000012912}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_002934450.3, ECO:0000313|RefSeq:XP_004911242.2}
RP   IDENTIFICATION.
RC   STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002934450.3,
RC   ECO:0000313|RefSeq:XP_004911242.2};
RC   TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002934450.3,
RC   ECO:0000313|RefSeq:XP_004911242.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   RefSeq; XP_002934450.3; XM_002934404.5.
DR   RefSeq; XP_004911242.2; XM_004911185.4.
DR   STRING; 8364.ENSXETP00000012912; -.
DR   Ensembl; ENSXETT00000012912; ENSXETP00000012912; ENSXETG00000005867.
DR   KEGG; xtr:100486524; -.
DR   AGR; Xenbase:XB-GENE-985051; -.
DR   Xenbase; XB-GENE-985051; klkb1.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_031604_0_0_1; -.
DR   OMA; TTMNYTD; -.
DR   TreeFam; TF343687; -.
DR   Reactome; R-XTR-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-XTR-1592389; Activation of Matrix Metalloproteinases.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Bgee; ENSXETG00000005867; Expressed in liver and 2 other cell types or tissues.
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; 4.
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; 4.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00005; APPLEDOMAIN.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00223; APPLE; 4.
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; 4.
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:UP000008143};
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..629
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041157588"
FT   DOMAIN          21..103
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          110..193
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          200..283
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          290..373
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          391..628
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
SQ   SEQUENCE   629 AA;  70403 MW;  6E11952B8912A9A1 CRC64;
     MTCYYCLLVF LLFFTLGSGG CISELYQDSY WQGGDLRSVF APDVEYCQLV CTFSPRCLMF
     SYLPASWPKE NERFACYLKE SATNMLPKVT LTGAISGHSL KTCKSKINVC RDKNFHGIDM
     IGTNYNVTWA TNVQQCKEGC TNDIHCQYFT YVTEQFHSAP MRNRCYFKYS AKGMPTRIRL
     LDNVISGFSL KACGKSSLGC QNDLFQNMEL PGETLTRVFA PDVHTCQKIC TFYPNCLFFT
     FYKKESKEPL QRNVCYIRTS TKGIPDEGIN KEHTISGFSL LSCKFSPSVC PLTILSDAEF
     LGDELLVEEV SGEKECQQEC TNNIRCQFFT YRPMQSGCSE NKCKCHMKIS SNGLPTGIRH
     GNGEISGFSL RLCKIKSVKG CGEPIEHANR IVGGTDSVLG EWPWQVSMHL RLTASYKKHA
     CGGSIISNQW IVTAAHCFAM HPLPQMWIIY SGVVKLSNIT QSTPFSETEQ IIIHPHYTGA
     GNGTDIALLK LKTPISFNDH QKAICLPPRE PTFVLPNSCW ITGWGFTEES GSLANILQKA
     EVPQISTEEC QGNYEQTRID KKILCAGYKR GKIDSCKGDS GGPLACVVDE IWYLTGITSW
     GEGCARPGKP GVYTRVSEFT DWIIEHTRV
//
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