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Database: UniProt
Entry: A0A9P0FQ16_CHRIL
LinkDB: A0A9P0FQ16_CHRIL
Original site: A0A9P0FQ16_CHRIL 
ID   A0A9P0FQ16_CHRIL        Unreviewed;      1206 AA.
AC   A0A9P0FQ16;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN   ORFNames=CINC_LOCUS2366 {ECO:0000313|EMBL:CAH0584119.1};
OS   Chrysodeixis includens (Soybean looper) (Pseudoplusia includens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Plusiinae; Chrysodeixis.
OX   NCBI_TaxID=689277 {ECO:0000313|EMBL:CAH0584119.1, ECO:0000313|Proteomes:UP001154114};
RN   [1] {ECO:0000313|EMBL:CAH0584119.1}
RP   NUCLEOTIDE SEQUENCE.
RA   King R.;
RL   Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LR824016; CAH0584119.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P0FQ16; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP001154114; Chromosome 13.
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   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:UP001154114};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          59..250
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          281..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          870..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..460
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..470
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        634..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..796
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..822
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1206 AA;  125932 MW;  06D14189E0AB0022 CRC64;
     MIVKYCLVPF LPAMECFRLN KTQRSRTYLY QWFLVLLLSS LCTANDGLFG SKFQTDIPEY
     DLLHAIGVPF SNPKTQYFDE GLDGFPAYGL MPGSDIKSPY RLFMPEKLYA EYSITATVRP
     ANKDGGFLFS VVNPLETVVQ LGVQLIPSGP GLTNISLLYT DANIYALSQT IASFVVPSFA
     KKWSRFALRV TTDNVTLFLN CHEFDTVVVK RNPLELVFDS ASTLYVGQAG PLIRGAFHGA
     FQELKLYGSP TQAEVQCVNT FEESGDGDEI DIDNYLVDQE EGDAEGSGRY GTIPPFPPPP
     PGLDGTGYML RLKGEKGERG PRGAPGESIR GPPGPPGPPG PSGPSGTPGV VAEISGSGDD
     QQIFGENYAS LGQCGCNSST ILALLQTAPE LKGPPGPPGI TGADGRTGSP GLPGQPGTPG
     ERGPVGPRGD KGDRGDVGPR GAEGPAGPKG EAGVDGRAGA PGPPGPPGTP GPSDYSNFDE
     SLIGSYGGAI GRPGAPGPKG DVGQPGPIGP QGERGFPGQK GERGQAGIGG HKGDRGYLGP
     QGERGYKGDR GSPGLDGRPG IPGASGRPAD KGEKGERGEP GPPGPPIAGV YNPDDAEFLV
     TGQRQAVAGL KGDKGEKGEK GAGGNDGPPG FPGKDGKSGE RGDIGPSGMP GISGPPGPPG
     LKGERGERGP PGPISVTMAG SDIVTIKGDK GDAGVRGRRG RPGPPGPKGS LGGQGPPGLP
     GRPGDKGDVG LPGWIGRPGT LGPPGAHGPP GPKGEKGDPG VNVLDVSMFK GEKGDRGFDG
     LPGLPGVPGP AGPPGPSGTL SEAVQYLPGP PGPPGPPGPP GTPGVSIVGP KGEPGITHFE
     EHPVHGSTKF YGRPIIKSPL DELKALKEIK DRERDRHGPV HTPPSMSHTA QNTEDSKTSV
     PGAAVFQTTE EMLKLASASP VGALAYVVEE QALFVKVNSG WQYVLLGSLV TQSAPAHQKP
     TPAPASPPMP AASLVHVPSI SNFVESSPAV GPSLHLAALN EPLSGNMHGI RRADYACYRQ
     GRRAGFRGTF RALLTSKIQN LNSIVRYSDR HLPVVNTQGE VLFKSFSDMF DGNGAMAAGS
     RIYSFNGRNI LTDSHWPQKV IWHGSRANGE RAIDSFCEEW QNGDPVNRGL ASSLYTHKLL
     AQERYPCNNH FVVLCIEVAS ELNSRRKRET PRFNATGLLD DDDYLYNSEE YQQLLNEIFA
     QPFREN
//
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