ID   A0A0V0XLI4_TRIPS        Unreviewed;       984 AA.
AC   A0A0V0XLI4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Chondroitin proteoglycan-2 {ECO:0000313|EMBL:KRX88808.1};
DE   Flags: Fragment;
GN   Name=cpg-2 {ECO:0000313|EMBL:KRX88808.1};
GN   ORFNames=T4E_7302 {ECO:0000313|EMBL:KRX88808.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88808.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX88808.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX88808.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRX88808.1}.
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; JYDU01000221; KRX88808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XLI4; -.
DR   STRING; 6337.A0A0V0XLI4; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 5.
DR   InterPro; IPR002557; Chitin-bd_dom.
DR   InterPro; IPR036508; Chitin-bd_dom_sf.
DR   PANTHER; PTHR23301; CHITIN BINDING PERITROPHIN-A; 1.
DR   PANTHER; PTHR23301:SF109; PROTEIN CBG16847; 1.
DR   Pfam; PF01607; CBM_14; 8.
DR   SMART; SM00494; ChtBD2; 9.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 8.
DR   PROSITE; PS50940; CHIT_BIND_II; 9.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..984
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006872584"
FT   DOMAIN          20..79
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          86..146
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          150..213
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          235..295
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          311..375
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          394..453
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          466..525
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          553..610
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   DOMAIN          662..722
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          728..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX88808.1"
SQ   SEQUENCE   984 AA;  109719 MW;  8F6C55F317FD6C6A CRC64;
     LLLSLLASLR CCCCSANQTE FNCSYVSDGK YSHPDQPCSP VFYHCFQQVT TKMKCPDSLY
     FDVFQEICLP RKEVQACFNE PIPESALDCK ILADGQYPDI SANCSRKYYK CLAGVTTFFA
     CPGEYLYYDA EKKQCVPYTE VEECSSLSIS VDCTTLLSSG AQRQSIADNA CSEFFINCEN
     NSFGKISKCK DGLFFNPIKR SCDLNSNIEV CNISLLNSKT DYEHSTAASN SFNSYSTCSN
     MAEGMNPIAL NVCSQFYIYC QQNSTPILMK CSYELYFDSD QNRCVHKKVS KICNIRSGYK
     NETEQSFINF PVRCSDQMVV GKHAISDDSC SQFYIECEND SDFPIATFKK CKDTLLFDPK
     NKNCAREEKI TSCQLEHHSS TAEQSIYNKN RTNEFDCHGI GDGNYSISGK GCFNFYYQCI
     DEVAFKLFCL SELYFDPVLR ICSPYENIAY CNQESKLPPK MSMKEANFCS PSVNENYPDP
     LQNCSSKYYT CFNGYLIQRH CELGKYYDVQ SDKCDLFRMV PACSRFGRSN NLRTLSTEAA
     PTTASLSSLT TLSFNCENLP DGNWAASACK PYYFACVGGF SFMQPCPSGT YYDPDTDQCN
     YKSAIPLCGE IVEWISISPL STTDQPAATA TPAPAIVTAT TSTAAAAAAA TTTTNYIYST
     LSVDCKNLPN GYYADPRNSC SKIYFLCDNG NDFMFYCVGA RLFYDPDNGM CDDKAHVVAC
     GGSARGTAAS ASPLHQGSST METTQQPTRP PVSTLKTTHF PNIIRTRKLT NRIIKPTQST
     TGERRRTSSS STVTTKGINI PTRAMMRTTQ SPPVVRTRKT VHPWRRITTI KPTHLSSVDA
     LSIKRTTPSP LITASASATN TSPRGVVKPF VVSLPEIGRV TKAPLGSNQQ AKETHSVQSQ
     HSFSFQTKTS FQNRAFTGYN NTVISTGNNW ISIFQRELSA DGSIENSRYF LRTRQRAKPA
     RLGTRKPVMR EKEDYKRVYG MKLC
//