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Database: UniProt
Entry: A0A3S0Z6N9_ELYCH
LinkDB: A0A3S0Z6N9_ELYCH
Original site: A0A3S0Z6N9_ELYCH 
ID   A0A3S0Z6N9_ELYCH        Unreviewed;      1397 AA.
AC   A0A3S0Z6N9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=C-type lectin domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=EGW08_020386 {ECO:0000313|EMBL:RUS71852.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS71852.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS71852.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS71852.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS71852.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) 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:RUS71852.1}.
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DR   EMBL; RQTK01001150; RUS71852.1; -; Genomic_DNA.
DR   STRING; 188477.A0A3S0Z6N9; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   CDD; cd00037; CLECT; 2.
DR   CDD; cd19941; TIL; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1.
DR   PANTHER; PTHR11339:SF373; HEMOLECTIN, ISOFORM A; 1.
DR   Pfam; PF01826; TIL; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00034; CLECT; 2.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 3.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1397
FT                   /note="C-type lectin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018626004"
FT   DOMAIN          593..776
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   DOMAIN          1242..1358
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          20..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1397
FT                   /evidence="ECO:0000313|EMBL:RUS71852.1"
SQ   SEQUENCE   1397 AA;  158129 MW;  F2C60B8B4E0D1673 CRC64;
     MKLSWLGLLA VTLVAGLLSP HPAQADPKRG SSQQQSQQQA QQEAQHRIQQ AQEEAQRRIQ
     QAQEEAQRRV QQAQEEAQKA QQEAQRRAQQ AQEEAQKAQQ EAQRRAQQAQ EKAQRRAQQA
     QQEAQKAQEE AHRRAQQAQE EAQKAQEEAH RRAQQAQEED QRRAQQAQQE AQRRAQQAQE
     EAQKAQEEAH RRAQKAQEEA QKAQEEAHRR AQKAQEEAQK AQEEAHRRAQ QAQEEAQRRA
     QQAQEEAQKA QEEAHRRAQQ AQEEAQREAQ QAQRNQRQGH CNNGFSRVAR RCIKLEKTQL
     SHAAAKEVCS GQGGRLINLD KLMFSYRYIG QHMSDVRGGQ FFIGGVQSFN NGLPSDRWDL
     GFIREIADEF KITNRGQLVS ALKRFRVNPS AQELNEDSEL RGQCLALDYT THKKPIMVDC
     DQKMNFICEQ VSSEDEEEGV WTDWFDEHPV NARGEYESFT RIVRAIAQRK LTGTVCRNPL
     AMECRDKDTK ELFSSADSHG YRMVKACEHN QILCYHAMNG GKKCPDFEVR FKCAELPDDC
     SSEEVRERCE RRNLQCHNGP RGAVCVRQRA QKSGNEKIGV GSCTLDSVTY SLHQCAAWGD
     PHYITLDNSA FDMQGACHYN LMTTCNNFKD TPAFPRLKVV VFNERRDEKD QVTRTKAFTF
     EVNGVKYMFT RGEFYREGMK RNYVSYQDDD ISITAIPKGS RHFLVVKTGH CIEMTWDNIH
     TVKIKIPDIY KNHICGLCGN YDGIRENDLT IDGKPVSEVE YGTYHYEPGS NSAECKDGGV
     IPTVSCSDAD KAKFSVPDFC GVLNPAGDSP LAQTIIQTST SAEAKQANSD VLKQKFDSCV
     YDHCLQANFG DGRCRYLENI VEDMLEDLNI DDENLDRAWR QFSGCLDSDE EKCGDKPNME
     FHQSFKPHCQ DTCAEPDRSV ECEDHRTTSG CACKEGFVMD ANMNCVEEEE CSTSCNYMTD
     NGERISIKDG ETEVIQHCTQ FAKCENGEVK ITDQPPCSEF ADCVADGFQC ACRQGFKGDG
     RTCQVDRQCK PGYVAGGNKC RKLVRERLPW HDAALACGAE GAQLARYDVE EDSPLENFVA
     RVPDMFLMAV SQPRLLMCRS QSRACAIPHG KVAIDARLKF ARDSAQCEGK FELSANKRML
     IVSTGCTAEF IVRCVEPSIL TRPSNIPVWV GGSLDVLGFD KRNDEAPFQV DPQRLADKGA
     FAGQSGCFQA VTTNDKFSLS LKDCETPQPY ICEYDNTGEV PYDPLDFIAV RDKGDKQRAI
     ELCQARGRPV ASILNRAQQD KATEIVKTLG GEPVWISLEW NEQHSGFYWQ DGTDLAFSNW
     RGEPQPNVRD LQYYCVVITP IGFWYLKRCA ERRMVLCGPP LSETPMEFTP HITVDGFNSL
     PSLYNKLKNH GKEKDIC
//
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