ID B7PC21_IXOSC Unreviewed; 595 AA.
AC B7PC21;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Secreted salivary gland peptide, putative {ECO:0000313|EMBL:EEC04143.1, ECO:0000313|EnsemblMetazoa:ISCW002695-PA};
DE EC=3.4.21.4 {ECO:0000313|EMBL:EEC04143.1};
GN Name=8027684 {ECO:0000313|EnsemblMetazoa:ISCW002695-PA};
GN ORFNames=IscW_ISCW002695 {ECO:0000313|EMBL:EEC04143.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC04143.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC04143.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW002695-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW002695-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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DR EMBL; ABJB010109540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010183180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010299178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010319969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010720069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB011052515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS680999; EEC04143.1; -; Genomic_DNA.
DR RefSeq; XP_002409227.1; XM_002409183.1.
DR AlphaFoldDB; B7PC21; -.
DR STRING; 6945.B7PC21; -.
DR PaxDb; 6945-B7PC21; -.
DR EnsemblMetazoa; ISCW002695-RA; ISCW002695-PA; ISCW002695.
DR GeneID; 8027684; -.
DR KEGG; isc:IscW_ISCW002695; -.
DR VEuPathDB; VectorBase:ISCI002695; -.
DR VEuPathDB; VectorBase:ISCP_035170; -.
DR VEuPathDB; VectorBase:ISCW002695; -.
DR HOGENOM; CLU_458766_0_0_1; -.
DR InParanoid; B7PC21; -.
DR OMA; VWNNTEC; -.
DR OrthoDB; 3680575at2759; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR022700; CLIP.
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; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:EEC04143.1};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..595
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010825977"
FT DOMAIN 360..594
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 21..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..237
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65282 MW; 1DAEFD0A39D5D68A CRC64;
MRIGLLSAAV LVCLVNTTSV GGSHPTSLVR SKREGKPPSQ FGPQGNQNQG PQAPHLIHGS
PIKDQGTINS FIRNVQNSGH DFNLPRSRSS FFGPLISTLR QFQICTTPTQ GPGKCRYVKD
CVLPAFLENF DIFLSYSCRI SNRHLGVCCP DEFFGGGGQK KPLFPILSGI LGINQNQAPP
PSRAPDYDDY DPPQPQGPPQ GPHQQGPGPH GPQPHYPPPE QFPGGNGGPP NGPQRPPFYE
DVEPHGGVPP VQPPVQPPVQ PKPVQPPPVQ QPPPVQQPPP VQQPPPVQQL PQVQKPPSKS
PSVNAPIHFP DDEEEAPVQQ PPPSRQAPRP PRDPSKPPPP IPNGLSQLLT SCGLNFKTRI
VGGTIAKPND WTWMAALLRR FDDDQFCGGA LISERYVLTA AHCTQGLRPQ NITVRLGEYD
FKQNSTSRQT RDFNVSRIRQ HREFKKDTYQ NDIALLRLSR RVRFTEHIRP ICLPKRHETF
IGKLATVVGW GTLSFGGPSS SILRQVTLPV WNNTECKTKF TQAIPDIFLC AGTREGGQDA
CQGDSGGPLM LEAESSQWTL IGVVSWGIKC AEKGLPGVYT RITEFLDWIY ENAVD
//
