ID A0A182R5C7_ANOFN Unreviewed; 891 AA.
AC A0A182R5C7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Spondin-1 {ECO:0000256|ARBA:ARBA00019594};
DE AltName: Full=F-spondin {ECO:0000256|ARBA:ARBA00030964};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN001369-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN001369-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN001369-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A182R5C7; -.
DR STRING; 62324.A0A182R5C7; -.
DR EnsemblMetazoa; AFUN001369-RA; AFUN001369-PA; AFUN001369.
DR VEuPathDB; VectorBase:AFUN001369; -.
DR VEuPathDB; VectorBase:AFUN2_007956; -.
DR OrthoDB; 5404502at2759; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
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 CDD; cd00109; Kunitz-type; 1.
DR CDD; cd08544; Reeler; 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; 2.60.40.4060; Reeler 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; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
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; PF02014; Reeler; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 4.
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; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..891
FT /note="Spondin-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030024127"
FT DOMAIN 23..198
FT /note="Reelin"
FT /evidence="ECO:0000259|PROSITE:PS51019"
FT DOMAIN 199..389
FT /note="Spondin"
FT /evidence="ECO:0000259|PROSITE:PS51020"
FT DOMAIN 680..730
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 626..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 100750 MW; 3667A3D9FF95F727 CRC64;
MRSIRRRSPY RLFTSAFVLL PLLLLLLDAN HLVRGLRCDR SPEGSGANKS PADGRFRLRI
SGNPEKYVPG ESYTISLVGI RSMQVPHKFS GFFLAAEKDF SLVRGDGPPS GVHNVGTFQL
SGDALTKFSE RCPNAVTQTN SLPKSEIQVN WIAPPAGSGC IAIRATVVEH RDVWYMDDGP
LSKIFCEDEA DSVDTQPPVL KECCACDEAK YELTFEGLWS RHTHPKDFPS NGWLTRFSDV
IGASHTVDYR FWEYGQVASE GLKQVAEHGS TRMLESELKN QSDKIRTIIK ARGISYPNVT
GKTFAVFRVD SNHHLVSIVS MLDPSPDWIV GVSGLELCLT NCSWIENKIL NLYPWDAGTD
SGPTYISPDQ PTNPPEVIRR IKSNYPNDPR SPFYDPSGTE MKPLARIYLS RQRLYEKNCD
ADNEEENETK QACETEPWSD WTDCSARCGM GKHTRRRVYK HPMKARQAEC KVKLFDRRAC
VGTYRDCDYN NQDIEDAYLS DPECEVTEWG PWSECSSPCG KGNKTRSRKY KKKGARKKCE
RLPNPPMLQQ TVSCDEDCGG DISQPVLSSD INPKCKMTQW SEWSPCSVTC GLGRKMRTRM
PINKNMRVHH KRFVSYYMTR RRMTALNEEE DSEEGDGGED NDLHVTDQND PCYGVETVEE
VTCGHDLPPC VGLYGVPELC FLEPKPGNCR DSLTRWYFQS DKNDCSILFF TGCGGNNNNF
MSREDCLDTC SKDRKFTNIP IRDQISTNSA GASDDGTDLK QDCKTSHWKR GPCNATCGEG
SRVKSRTILV HPSNGGQRCP RKLRKVERCF VHCDSSRHDT NPSWGPSTRY EPEPIECEYS
AWSAWSPCSK TCGDYAVQQR TRYLLDPDNA RFCPHRLEER KCDIMPCLLG K
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