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Database: UniProt
Entry: A0A1V9XTM1_9ACAR
LinkDB: A0A1V9XTM1_9ACAR
Original site: A0A1V9XTM1_9ACAR 
ID   A0A1V9XTM1_9ACAR        Unreviewed;       558 AA.
AC   A0A1V9XTM1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-JUN-2023, entry version 22.
DE   SubName: Full=Neuropilin and tolloid protein 2-like {ECO:0000313|EMBL:OQR76854.1};
GN   ORFNames=BIW11_07510 {ECO:0000313|EMBL:OQR76854.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR76854.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR76854.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR76854.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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:OQR76854.1}.
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DR   EMBL; MNPL01004290; OQR76854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9XTM1; -.
DR   STRING; 418985.A0A1V9XTM1; -.
DR   InParanoid; A0A1V9XTM1; -.
DR   OrthoDB; 3024898at2759; -.
DR   Proteomes; UP000192247; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR24251:SF28; NEUROPILIN AND TOLLOID-LIKE, ISOFORM B; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 2.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        337..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..142
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          154..276
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   REGION          455..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..511
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        293..311
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   558 AA;  61972 MW;  42FBCB7381FA00CD CRC64;
     MTTAKEQKGY KFGDMDEEEK ARICFNFTVG DPERREFYSP LFNLSGGTYP NNTECIKRIT
     APLNHMVRLE FRDQFHLEES PSCEFDKLEV HNGGHGYSPL AGTFCGREFP KPIQSEGREL
     YLKFTSDASI EYVGFKAVYS FIPAPRTEVD PPECKFNRDG ENGRISYSDI SNGTIVHANE
     TLSPIDCTWT IRVQNGSKIY ITFLHYELAQ PNNCQTNFLD IISGGAKQDR LSHFCGTIAE
     PTTSVTNEVQ IRFFAQGALL KQNNKPPKLE VLYTAFREVN DPKDCNALTE FSCDDGWCIS
     NKLTCDGDYN CKYRYDEDAS RCAVSSGIFL VLTSDHMIII LVVFTALVMG MCASITITCY
     NKIQERRERE REYKIRRSKE VSMEIGLAPP AAPSSELEAA LAAEIRLRKQ HQTGQLAGQL
     APMGGQLVDD VEDGRYLPDH PNGVLIMAGS GPVCGGGGTD GDRQSLGDRQ SVKSVPLCPQ
     HGHGTYRDNA LDRDSLTPPI PPPPPPPLQA YYRMRDSPAN EMSGRWSPLE DSTMASSPQG
     PSQNNGGETG RPDLVAHR
//
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