ID A0A6I8TY14_AEDAE Unreviewed; 1169 AA.
AC A0A6I8TY14;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=5574086 {ECO:0000313|EnsemblMetazoa:AAEL019726-PD};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL019726-PD, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL019726-PD, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL019726-PD,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL019726-PD}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL019726-PD};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR AlphaFoldDB; A0A6I8TY14; -.
DR EnsemblMetazoa; AAEL019726-RD; AAEL019726-PD; AAEL019726.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1169
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5043938417"
FT DOMAIN 48..236
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 275..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..575
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..787
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 123092 MW; EA4D96504F82F940 CRC64;
MKYLPTFERW FERIPFLCLL LTYVQSSSVA ASELALFGGQ GIRDVFAEFD LLLAIKIPPE
DGITFVDGSD GFPAFGVAPH ADIKSPYRTI LPEKLTEFTI IATVRPGSRS GGYVFSVVNP
LDTVVQLGLL LEPILATDQW NITLIYTDAN VERVSQPLVS FQIPYTKSWI KLIFKVLNNQ
VVFYNNCVET ETVVVKKEPR SLTFDGASTL YIAQAGQILK RNFEGTLLFL KLYGNPEIVK
THCNRTATEL DDSSNVIYEE DDFLGDGDAL GGELFSDGIS ASSGDDDDSF DLPMISPPPP
EYGYRSKGEK GERGPKGPPG DAIRGPPGPP GPHGPPGPPG PPGAAGPRGP GLLDEGSGDD
AKRLSQLFDI QNNNLLNKCY CNVTEVIEDL KRDITLREYL RGPEGPQGRE GKTGSPGLTG
ATGPPGERGV AGLKGDKGDR GEPGLPGVEG IQGSKGEPGL DGIPGPAGLP GSPGPPGIPE
NFDMSWNPSR MFKESMLGAP GIQGLRSASP GSKGEPGDKG DVGLPGPKGE HGSKGERGDP
GLIGAKGERG HTSIGAPGPK GSVGPPGVPG IPGQTGSTGT KGDKGNSGDV GPAGPPGPPG
MVVYADVKNS TGTTDCHCQP GPPGPAGPRG PSGFDGAPGL PGETGLPGHP GLPGDKGERG
SPGPKGEKGP EFIINENAAF NSSRSNKGEK GERGPRGRRG KPGPIGPPGR PAGPSDMGTN
SWSGRPGPKG DQGPKGDVGP RGEKGDRGRD GMDGRPGPPG LPAASGDNIQ YIPMPGPPGP
PGPPGSPGIP GVSIAGPKGE PGMDSRSPYY GDPNYGGRQG SRSSFDELKQ LRELKHHREL
EDSTAGPPGP PGPPGAPGRG YHHDSSDEIP SSYGSNVRIV PGAVTFQSTE AMSKMSSTSP
VGTLAYIIDE EALLVRVNKG WQYIALGTLV PIATPAPPTT TVIPPPHRPD LQASNLINNI
PQPIEGPSLR MGALNEPYSG DIQGIRGADY ACYRQARRAG LLGTFRAFLS SRITNLDTIV
RIADRELPVV NTRGDVLFNS WNSIFNGQGG YFPQTPRIYS FSGKNVLTDI SWPQKLVWHG
ASALGERAMD TYCDAWHTAS PDKVGMASSL LGNKLLDQDR YSCDNRFIVL CVEALPHDQR
RKRDTYSHTY EFTNEHDYSR HLAEVMKQA
//
