ID V5GUT5_IXORI Unreviewed; 651 AA.
AC V5GUT5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative fat-spondin {ECO:0000313|EMBL:JAB74170.1};
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB74170.1};
RN [1] {ECO:0000313|EMBL:JAB74170.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB74170.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR EMBL; GANP01010298; JAB74170.1; -; mRNA.
DR AlphaFoldDB; V5GUT5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR CDD; cd00109; Kunitz-type; 1.
DR Gene3D; 2.60.40.2130; F-spondin domain; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR009465; Spondin_N.
DR InterPro; IPR038678; Spondin_N_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR NCBIfam; NF038123; NF038123_dom; 1.
DR PANTHER; PTHR11311; SPONDIN; 1.
DR PANTHER; PTHR11311:SF16; SPONDIN-1; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 3.
DR Pfam; PF00090; TSP_1; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 24..215
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT DOMAIN 454..504
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 73658 MW; FC13487EBD70D731 CRC64;
MDEGELTKEL CQEEQENDDE QPEVLDECCA CDEAKYEMTF EGLWSRYTHP KGFPDNEWLT
HFSDIIGASH AADFKMWEYE GFASEGVKSV AEHGATKKLE SELKAKSGKI RTIIKARGLW
YPNVNGKTFA VFRLDKKHHV MSVLSMLGPS PDWIVGVSSL ELCLKNCSWI TEKTMNLYPW
DAGTSEGVTY VIGQREATSP QQRIQKITSS NPHHTDSPFY DPTGAPMKPV ARLTVTRQRI
YEKSCDEEVE PNTPPPLETP VPVDQRPECA VTEWSKFGSC SVTCGQGVRT RTRSFLMRDK
AFMFNCKTQL VDRDVCEIDC SGGVSCETTP WSEWGDCSVT CGKGVRIRQR KYKQHMARKR
CTLELMEKEM CVAPVMTCKD APEVIDPNCA VTQWAEWSPC TATCGKGIKV RTRAYLNAMT
AAMAMCNVEQ IQKAPCMAEN ADCKVDSQEA HEICLLPKDI GPCRGYFPRW YYDSTKRMCL
QFVYGGCRGN RNRFERYSEC NKMCEVTISP PLSTLTSLPP HNGLPTTSDE PTSPVIDCVL
TPWSQWGPCS KTCGNGRRER RRMIKLNPQN GGKPCPKKLV QRRRCKENPP CPVDCMLTPW
SEWRPCSKTC GVGAVQERHR TIKRHPKNGG STCDATFERR YCTLPPCDYH R
//
