ID   A0A6V7X153_MELEN        Unreviewed;       803 AA.
AC   A0A6V7X153;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-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   ORFNames=MENT_LOCUS45628 {ECO:0000313|EMBL:CAD2192717.1};
OS   Meloidogyne enterolobii (Root-knot nematode worm) (Meloidogyne
OS   mayaguensis).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=390850 {ECO:0000313|EMBL:CAD2192717.1, ECO:0000313|Proteomes:UP000580250};
RN   [1] {ECO:0000313|EMBL:CAD2192717.1, ECO:0000313|Proteomes:UP000580250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Koutsovoulos G., Danchin GJ E.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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:CAD2192717.1}.
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DR   EMBL; CAJEWN010000971; CAD2192717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6V7X153; -.
DR   OrthoDB; 10060752at2759; -.
DR   Proteomes; UP000580250; Unassembled WGS sequence.
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   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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
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   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..803
FT                   /note="Thrombospondin-like N-terminal domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5027750266"
FT   DOMAIN          31..220
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          241..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..536
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   803 AA;  89388 MW;  F01D762AF44E24FF CRC64;
     MLYIFAFCCL HCAVISIGKS FEIPGDEETE ANLLIPVENL IDTDPRVFRT AGLDGLPAVG
     IKRGVEIVVP YRIYLPRKFY RNFAILASIR PSDNLGGFLF AVLNAFDTIV ELGPTQTNIS
     LFYTDSSSTD SSEQRSTSRV LASFLVPVFA GQWTQFALEV HEQTVGLYFR CMRYAVRQVY
     RHPTQLQMDD ASKLYIANAG PIIGGGFEGA IQELKLHDDP AEAANQCNEN WDSEKSGLVS
     SGFGSLEENG LRVDEGEEEE GKGRFPSTPP GSGPARFLPK NINLLTTTLT TTTKQQKEET
     KTTLFPTLHT PLIQQQMIPG PKGERGEPGI PGTCAATECR MPPPGPPGLQ GPPGVFPGLT
     EHDLRRIAAW PGVKGEKGDR GECCDKTTSK QTYREGYQDG GEEEVVLLNG QHSDQLPAYN
     RKVHGSSNSI KGEKGDRGEQ GPPGLPGKLI EKPQSPSFSG VRIFQTALEL LAATPNCPIG
     FLAFALSTQQ LFIRVNSGWK QIIVSLGGNL LTAQSGTKER NVDDYVSSPS ISNNNADDSD
     ELNRLSYWLA LDEPSSEEFR NDNEMINTLP SPEQRWQPRF PPKENRRLEE EKEEEKQKNR
     VPSVQQKRHK DRIIHLIALN EPLNGNFGGV RGADLECYKQ ARQFGFTTTF RAFLSSRVQD
     LNKVVHEDDR NYTPIVNIRG ERLFDSWNSV FDGERSVHAH VPIYSFNRRD VISDNNWPDR
     WLWHGSTAEG SRTSTAFCDG WYSDNSNSFG NASPLHSRHS LTGQSKEANC NNRFVVLCVE
     VMSKFNVDSK LGKRFMSDDV IRK
//