ID A0A3Q3N1L3_9LABR Unreviewed; 871 AA.
AC A0A3Q3N1L3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Brevican {ECO:0008006|Google:ProtNLM};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000027730.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000027730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3N1L3; -.
DR Ensembl; ENSLBET00000029055.1; ENSLBEP00000027730.1; ENSLBEG00000020959.1.
DR GeneTree; ENSGT00940000157343; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; IPR000742; EGF-like_dom.
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:SF41; BREVICAN 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; SM00409; IG; 1.
DR SMART; SM00406; IGv; 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; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 14..134
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 136..231
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 237..321
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT DOMAIN 597..632
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 644..758
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 762..822
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 321..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..584
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 182..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00323"
FT DISULFID 622..631
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 764..807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 793..820
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 871 AA; 97438 MW; 6294FA95E4C3AC17 CRC64;
MHADVSKLLQ VTIPAAPPVL AVLGSSLTLP CLVSLAHPPP SPSTNGRHHV LTLPRVKWSV
LTQGRETEIL VARGDRVRVN EAYKERASLL NYASSPADLT LRLESLRHND SGFYRCEVQQ
GLEDADDVAQ VKVKGVVFHY RDASSRYAFT FERAREACQE IRADIATPEQ LLAAYHSGYE
QCDAGWLSDH SVRYPIQMPR EGCFGDMAGL PGVRNYGLLE PDELYDVYCY VENINGEVFH
GSAPQHFTFW EAKAYCLSHR AELASTAQLY AAWHDGLNLC NPGWLADGSV RGEPGVRTVY
RYSNQTGFPE EHTRHDVYCF RETNQPSPDD NPVTNQTSPE DNPETNQPSP EDNPETNHPS
PEDNPETNQP SPEDNPETNQ TSPEDNPETN QTSPEDNPET NQPSPEDNTE TNQTSPDDNP
ETNQPEDNPE TNQTSPEDNP ETNQTSPEDN PETNQTSPDD NPETNQPSPD DNPETNQTSP
DDNPETNQTS PDDNPETNQT SPEDNLGTVP EESHQIPTAS PNADGGPTDE EGTTHTHTHT
HTHTHTHTHT HTHTHTHTHT HTHTHTHTHT HTHTHTHTHT HTHTHTHTPN GVNVLSAADS
CLENPCLNGG TCVDGETASC VCLSGYAGDV CQTGSVCEPG WEKFHGFCYR HFTTRQSWEA
AEQHCRMCGG HLLSVMTPEE QDYINDRYRE YQWIGLNDKT IEGDFRWSDG NPLLYQNWFR
GQPDSYFLSG EDCAVMVWHD GGRWSDVPCN YHLSYTCKKG VSSCGEPPTV PNAKVFGKKR
SRYETNTKVR YYCEDGFVQK LKPVINCMPG GLWEEPLITC MPIYTRSLHP QSTPVVYTCS
PHLPVVHTCL LYTPVLYNTY LYFSPACSLH L
//
