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Database: UniProt
Entry: A0A556TS46_BAGYA
LinkDB: A0A556TS46_BAGYA
Original site: A0A556TS46_BAGYA 
ID   A0A556TS46_BAGYA        Unreviewed;      1361 AA.
AC   A0A556TS46;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Neurocan core protein {ECO:0000313|EMBL:TSK53689.1};
GN   ORFNames=Baya_3249 {ECO:0000313|EMBL:TSK53689.1};
OS   Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Sisoridae; Sisorinae; Bagarius.
OX   NCBI_TaxID=175774 {ECO:0000313|EMBL:TSK53689.1, ECO:0000313|Proteomes:UP000319801};
RN   [1] {ECO:0000313|EMBL:TSK53689.1, ECO:0000313|Proteomes:UP000319801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSK53689.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TSK53689.1};
RX   PubMed=31274158;
RA   Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA   You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA   Shi Q.;
RT   "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL   Genome Biol. Evol. 11:2071-2077(2019).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:TSK53689.1}.
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DR   EMBL; VCAZ01000015; TSK53689.1; -; Genomic_DNA.
DR   Proteomes; UP000319801; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd03517; Link_domain_CSPGs_modules_1_3; 1.
DR   CDD; cd03520; Link_domain_CSPGs_modules_2_4; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
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; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link_dom.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR   PANTHER; PTHR22804:SF24; NEUROCAN CORE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000319801};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1361
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5022085755"
FT   DOMAIN          53..153
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          160..255
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          261..357
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          1062..1098
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1144..1258
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1262..1322
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   REGION          444..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1324..1361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1351
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        206..227
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        304..325
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        1088..1097
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1264..1307
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        1293..1320
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1361 AA;  151467 MW;  A2F3017F449CFE81 CRC64;
     MLSVFHVSGL QSLLTVLLVV SLEHETVWGE TIVNMRKVTH QVEQIPLSGT ALLPCIFTLR
     PSPSHESHDI PRIKWTKIWG HRGLDGLQRE QSVLVAKGNV VKVKKAFQGR VTLPGYMENR
     YNASLALTGL RSSDSGMYRC EVVVGLNDEQ DIVPLQVTGV VFHYRAPYDR YALSFADAKQ
     ACVENSGVIA TPGQLQATFD DGYDNCDAGW LSDQTVRYPI QSPRPGCFGD REDSPGVRNY
     GSRDTDELFD VYCFAESLKG EVFYVNVPEK LSLATASTHC HKLGAQLATV GQLYLAWQAG
     LDRCDPGWLA DGSVRYPINQ PRRNCGGDET GVRTLYHNPN RTGFPDTASL FDAYCYRESQ
     PIALALMQTS QTSSNSTDDW EQLQQNQSFA QPSNWTGLVD LDKEEFTSIA DKESSEISGE
     HVVIHLSPKE RPVSQVMHVS NYQSPPVLEL NGGSAREESD EREVTEDHRL APKPSMTTSS
     SSIETQTSNS MLFNFVNSIM KPWKYWKGNT DTDVPSSVPS IVKKTANEVQ TARMKPGGEL
     RGTKGDVENA IVEPGSIPTD PLTPYSEEGL LEQEKDMVLS IPIKELKAPS QLHMEPSVSL
     PTASKGLIAS GRIEVINPTA ATSPLGSGSS FVFMPEVASQ QEQASQSLGV YTTTSSNGIY
     TTPTSEPVET KREAMEMRTI PVLGDHENYS GEGKDHIEES YLLPKVSTLQ SSPQTGILEK
     ENDTDGSGGN EFFIISSPKK QGTPEALKEQ NVLIQTTVQW ELLQLPTRPP SHSPGVSKDI
     ADPEEARGEI LYMHHPTQKL ENNSFDKIAV EKSLSKHTPN VSEIPNPYMA TTPEHSPNNS
     STNYQMPSTS TITTLNSQIE NTDTTAAEDT VSTSDLAISV SWLPVVQKET QEPPTHVPNI
     VTDGRFETTS NTILLTTPYM EEATQHAETE PQTQAAPTTK TTSKDNTSKS TDDEQENSSA
     SSGNNGAFTY EATSKDRCEC LLYPGHHLIA PHHQPAHVGC HVAYVTSFWR SRKKGRLLCE
     CSWFKSINRS FGFLALQPES CLLAGQDSFS LAIAQETILV DDIDECQSNP CQNGGTCIDE
     INSFVCLCLP SYGGATCEKA LWLIALSSQP GPSAAEHANH SPYGPICTGQ FADTEGCDHN
     WRKFHGHCYR YFIHRLNWED AEKDCREHNG HLASIHTREE QNFINSMSHE NTWIGLNDRT
     VEEDFHWTDN MDLQYENWRE NQPDNFFAGG EDCVVMIAHE NGKWNDVPCN YKLPYICKKG
     TVLCGPPPLV DNAFLIGRKR SHYDIHSVVR YQCADGFLQR HVPTTKCRAS GKWDHPKILC
     TKSRRSHRYR RHHHKSHHER RKHKKHGSDS HRGRHDSRDH F
//
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