GenomeNet

Database: UniProt
Entry: A0A3B4YRB6_SERLL
LinkDB: A0A3B4YRB6_SERLL
Original site: A0A3B4YRB6_SERLL 
ID   A0A3B4YRB6_SERLL        Unreviewed;       843 AA.
AC   A0A3B4YRB6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Neurocan {ECO:0008006|Google:ProtNLM};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000030761.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000030761.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   AlphaFoldDB; A0A3B4YRB6; -.
DR   STRING; 1841481.ENSSLDP00000030761; -.
DR   Ensembl; ENSSLDT00000031647.1; ENSSLDP00000030761.1; ENSSLDG00000023679.1.
DR   GeneTree; ENSGT00940000158649; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd00054; EGF_CA; 2.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
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; IPR000538; Link_dom.
DR   PANTHER; PTHR22804; AGGRECAN/VERSICAN PROTEOGLYCAN; 1.
DR   PANTHER; PTHR22804:SF24; NEUROCAN CORE PROTEIN; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00193; Xlink; 1.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 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:ARBA00022974};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974}.
FT   DOMAIN          12..105
FT                   /note="Link"
FT                   /evidence="ECO:0000259|PROSITE:PS50963"
FT   DOMAIN          671..707
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          709..745
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          758..829
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          132..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        55..76
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT   DISULFID        697..706
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        735..744
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   843 AA;  89646 MW;  318BD6A1E4A24112 CRC64;
     QAPVSCLPPP GEVFHSSVPG RLSLSSASDR CVSLGGQLAT VGQLYLAWRA GLDSCAPGWL
     SDGSVRYPVT WPRPECGGSQ PGVCTVTPNS TADNTTALYD AYCYRGKVKN TGSISQIYTS
     LWKPWSYLTG SSDADSTGTD KPDLTTQQTF TTRGSSDASP SNWTGLVDLE EEAALHNADA
     STDPWSSESS GSYLTLQLIP GQSSLDWGEL LEPGPDSEEF LRPPVHPTPA EKKVISKIVK
     SIWKPWNYLV GTGDEEGTRA PNGQAGEEDT ATAKTEPSNT SSPGLLSWGS SWFSSTPEEN
     ASSASEDSPT RLASTLAASG IPTTTESTKS WESSETHTFT ASSSAPEITA SSGDTWVRVE
     AETTTQPGEK REETVTSRAS GRGGRGRGKK NRGEDRSRGE ERGRGEEKGK GEDEGSGEIT
     GAEAKGEIQV SRRPVGTSKP RERSRERSRE RGHRKGQSTT TTTTATTTAS PPEPTVMTTP
     GSESADFSTS KSPSALPAET PSPSISLDPY QTLSSSPSPS TSPSPSISAF MSFSQSSPSQ
     SPSLSFSSSP SPSTDAPLST SQTPSLSPSP ASPSSQSSTQ MVGSGDPSPS PLSENQDSAT
     NPLTSLHWVP VEKVSHNSSL DYPPLLSGPS DEEEPAWSHA VGSGALLPGN MDEESSRGSN
     ISTITLGQTM EVEPCVTNPC LHGGKCLPQG TGYSCYCPQG YTGENCEIDV DDCQSEPCEN
     GGTCIDKIDA FLCLCLPSYG GDTCEKDIEG CEHGWRKFHG HCYRYFTHRH TWEDAEKDCR
     EHSAHLSSVI SATEQEFING LGHDNAWIGL NDRTVEEDFQ WTDGNDLVSD RRSVVPPTAN
     HQL
//
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