ID A0A482X2P5_LAOST Unreviewed; 1076 AA.
AC A0A482X2P5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=LSTR_LSTR001042 {ECO:0000313|EMBL:RZF39521.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF39521.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF39521.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF39521.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RZF39521.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QKKF02019844; RZF39521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482X2P5; -.
DR SMR; A0A482X2P5; -.
DR FunCoup; A0A482X2P5; 15.
DR InParanoid; A0A482X2P5; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
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 GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; 3.
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:UP000291343};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 23..215
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 263..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..355
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..525
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 114023 MW; 87037D4A0AC1C89E CRC64;
MVLKETLGFR KSHSKRVPYI NSDIDLLSAI KIPFEDPRRV YFDTSLEISP AFGLRAGADI
KLPLSLLFPD RLFAEFAITA HVKLESSEGG FLFSVVNSLE NVIQLGVSVT SVDHTSTNVS
LIHTDASKHY SSQTLASFAV PSILGKWTKL ALEVTVSEVK LFFNCEYYDS VKVSRRQSEE
LLFDSASTLY LGKAGSVIKG AFEGSIQELK ISADPRNAET FCDHSPKINE NEGANEQRTE
NYNYGENEYN QDTYHISPVV EQDGDSYRPL SLKGEKGERG PPGPPGEGIE GPPGPPGPPG
FPISGNENFN HNLRGPPGPP GSCSCNLTQM LLNFALPDMI PGPQGLPGLD GKPGLPGAPG
LPGPAGDIGI PGPSGPKGSK GDSGLRGFEG LQGPKGERGL DGAPGPPGPP GPPGSVNLAQ
LEDLWSSHSM FTSSKESSPT IEKLLKTGLP GPKGEAGTIG TNGLKGDQGF IGLRGDRGEP
GEKGVKGDKG QQGPSGDNGS KGERGPPGID GVPGYPGESG SSGPKGQKGE TGMVGPPGPP
GPSVTHSSNL EYIESITDQT IMSIKGDRGA TGEKGEKGEK GDAGAPGIPG SPGRQGLTGS
KGETGRQGES GLPGEVGPQG LPGLKGETGP PGPVSGDSLR MKGEKGDSGR RGRRGKPGLP
GPPGRPGPIG EIGLPGIPGR AVYTNIGVKG FTIKPVLIKG EKGEPGSSIT IKEENGIKYV
SIPGPPGPPG PPGPVGPPGR SGTSERSNGD DFMKHSNQMP QSGYSEHTSR SVHHDKLATE
ILEQTKIVPG AVTFQTLVAL SKMTLVSPVG TLAYVIDEEA LLLRVKNGWQ YIALGSLIPM
PTEPSFTPST DDNGSPLEVS NLINNQPLTS KDGPVLRMAA LNEPYSGDVK GLRGADYACY
RQARRAGLHG TFRAFLSSRV QNLDSIIKNS DQDLPVVNIK GDVLFNSWKD IFSGDGAFFQ
QQPRVYSFNG KNVLTDFSWP QKYIWHGAFP SGERAIDLYC DAWDSNSMDR FGLASSLLNN
RLLEQEKFSC NNRFAVLCIE VTGHLLTNKK RRRRESELLG EQEYHKFLEE LLNERD
//
