ID   PGCB_HUMAN              Reviewed;         911 AA.
AC   Q96GW7; D3DVC2; Q5SZ10; Q5T3I5; Q8TBB9; Q9HBK1; Q9HBK4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Brevican core protein;
DE   AltName: Full=Brain-enriched hyaluronan-binding protein;
DE            Short=BEHAB;
DE   AltName: Full=Chondroitin sulfate proteoglycan 7;
DE   Flags: Precursor;
GN   Name=BCAN; Synonyms=BEHAB, CSPG7; ORFNames=UNQ2525/PRO6018;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain cortex;
RX   PubMed=11054543; DOI=10.1016/s0378-1119(00)00362-0;
RA   Gary S.C., Zerillo C.A., Chiang V.L., Gaw J.U., Gray G., Hockfield S.;
RT   "cDNA cloning, chromosomal localization, and expression analysis of human
RT   BEHAB/brevican, a brain specific proteoglycan regulated during cortical
RT   development and in glioma.";
RL   Gene 256:139-147(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-504.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-906, AND STRUCTURE
RP   OF CARBOHYDRATES.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA   Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-418.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [8]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023;
RA   Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y.,
RA   Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C.,
RA   Lako M.;
RT   "Extracellular matrix component expression in human pluripotent stem cell-
RT   derived retinal organoids recapitulates retinogenesis in vivo and reveals
RT   an important role for IMPG1 and CD44 in the development of photoreceptors
RT   and interphotoreceptor matrix.";
RL   Acta Biomater. 74:207-221(2018).
RN   [9]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-418.
RX   PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA   Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT   "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT   Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL   Mol. Cell. Proteomics 22:100617-100617(2023).
CC   -!- FUNCTION: May play a role in the terminally differentiating and the
CC       adult nervous system during postnatal development. Could stabilize
CC       interactions between hyaluronan (HA) and brain proteoglycans.
CC   -!- SUBUNIT: Interacts with TNR. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96GW7; Q06481-5: APLP2; NbExp=3; IntAct=EBI-2690445, EBI-25646567;
CC       Q96GW7; P05067: APP; NbExp=3; IntAct=EBI-2690445, EBI-77613;
CC       Q96GW7; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-2690445, EBI-9087876;
CC       Q96GW7; P07948: LYN; NbExp=3; IntAct=EBI-2690445, EBI-79452;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:37453717}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space,
CC       extracellular matrix.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane; Lipid-anchor, GPI-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96GW7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96GW7-2; Sequence=VSP_011184, VSP_011185;
CC   -!- TISSUE SPECIFICITY: Expressed in the retina, specifically in the inner
CC       nuclear layer, inner plexiform layer and ganglion cell layer (at
CC       protein level) (PubMed:29777959). Detected in cerebrospinal fluid (at
CC       protein level) (PubMed:25326458). Detected in urine (at protein level)
CC       (PubMed:37453717). {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:37453717}.
CC   -!- DEVELOPMENTAL STAGE: Expressed between 6 and 19 weeks post-conception
CC       (WPC) in the outer neuroblastic zone, inner neuroblastic zone, and
CC       inner plexiform layer of the retina (at protein level)
CC       (PubMed:29777959). Expressed at the surface ectoderm at 6 WPC and the
CC       neural retinal at 6 to 8 WPC (at protein level) (PubMed:29777959).
CC       Expressed in the interphotoreceptor matrix and abundantly in developing
CC       photoreceptors between 12 and 19 WPC (at protein level)
CC       (PubMed:29777959). Isoform 1: Highly expressed from birth through 8
CC       years of age and is down-regulated by 20 years of age to low levels
CC       that are maintained in the normal adult cortex (PubMed:11054543).
CC       Isoform 2: Expressed at uniformly low levels throughout development
CC       (PubMed:11054543). {ECO:0000269|PubMed:11054543,
CC       ECO:0000269|PubMed:29777959}.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate (PubMed:25326458). O-
CC       glycosylated with a core 1 or possibly core 8 glycan (PubMed:19838169).
CC       {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:25326458}.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Brevican;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_212";
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DR   EMBL; AF228710; AAG23134.1; -; mRNA.
DR   EMBL; AF229053; AAG23135.1; -; mRNA.
DR   EMBL; AY358372; AAQ88738.1; -; mRNA.
DR   EMBL; AL365181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW52927.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW52928.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW52929.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW52930.1; -; Genomic_DNA.
DR   EMBL; BC009117; AAH09117.1; -; mRNA.
DR   EMBL; BC022938; AAH22938.1; -; mRNA.
DR   EMBL; BC027971; AAH27971.1; -; mRNA.
DR   CCDS; CCDS1149.1; -. [Q96GW7-1]
DR   CCDS; CCDS1150.1; -. [Q96GW7-2]
DR   RefSeq; NP_068767.3; NM_021948.4. [Q96GW7-1]
DR   RefSeq; NP_940819.1; NM_198427.1. [Q96GW7-2]
DR   RefSeq; XP_011508168.1; XM_011509866.1. [Q96GW7-1]
DR   AlphaFoldDB; Q96GW7; -.
DR   SMR; Q96GW7; -.
DR   BioGRID; 121964; 43.
DR   IntAct; Q96GW7; 10.
DR   STRING; 9606.ENSP00000331210; -.
DR   GlyCosmos; Q96GW7; 7 sites, 2 glycans.
DR   GlyGen; Q96GW7; 11 sites, 3 O-linked glycans (6 sites).
DR   iPTMnet; Q96GW7; -.
DR   PhosphoSitePlus; Q96GW7; -.
DR   BioMuta; BCAN; -.
DR   DMDM; 68067899; -.
DR   jPOST; Q96GW7; -.
DR   MassIVE; Q96GW7; -.
DR   PaxDb; 9606-ENSP00000331210; -.
DR   PeptideAtlas; Q96GW7; -.
DR   ProteomicsDB; 76671; -. [Q96GW7-1]
DR   ProteomicsDB; 76672; -. [Q96GW7-2]
DR   TopDownProteomics; Q96GW7-2; -. [Q96GW7-2]
DR   ABCD; Q96GW7; 4 sequenced antibodies.
DR   Antibodypedia; 2188; 218 antibodies from 29 providers.
DR   DNASU; 63827; -.
DR   Ensembl; ENST00000329117.10; ENSP00000331210.4; ENSG00000132692.19. [Q96GW7-1]
DR   Ensembl; ENST00000361588.5; ENSP00000354925.5; ENSG00000132692.19. [Q96GW7-2]
DR   GeneID; 63827; -.
DR   KEGG; hsa:63827; -.
DR   MANE-Select; ENST00000329117.10; ENSP00000331210.4; NM_021948.5; NP_068767.3.
DR   UCSC; uc001fpo.4; human. [Q96GW7-1]
DR   AGR; HGNC:23059; -.
DR   CTD; 63827; -.
DR   DisGeNET; 63827; -.
DR   GeneCards; BCAN; -.
DR   HGNC; HGNC:23059; BCAN.
DR   HPA; ENSG00000132692; Tissue enriched (brain).
DR   MIM; 600347; gene.
DR   neXtProt; NX_Q96GW7; -.
DR   OpenTargets; ENSG00000132692; -.
DR   PharmGKB; PA134868393; -.
DR   VEuPathDB; HostDB:ENSG00000132692; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000157343; -.
DR   HOGENOM; CLU_000303_0_0_1; -.
DR   InParanoid; Q96GW7; -.
DR   OMA; APQISCV; -.
DR   OrthoDB; 5402504at2759; -.
DR   PhylomeDB; Q96GW7; -.
DR   TreeFam; TF332134; -.
DR   PathwayCommons; Q96GW7; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR   Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-HSA-2022923; Dermatan sulfate biosynthesis.
DR   Reactome; R-HSA-2024101; CS/DS degradation.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR   Reactome; R-HSA-3560801; Defective B3GAT3 causes JDSSDHD.
DR   Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR   Reactome; R-HSA-3595174; Defective CHST14 causes EDS, musculocontractural type.
DR   Reactome; R-HSA-3595177; Defective CHSY1 causes TPBS.
DR   Reactome; R-HSA-4420332; Defective B3GALT6 causes EDSP2 and SEMDJL1.
DR   SignaLink; Q96GW7; -.
DR   BioGRID-ORCS; 63827; 62 hits in 1157 CRISPR screens.
DR   ChiTaRS; BCAN; human.
DR   GeneWiki; Brevican; -.
DR   GenomeRNAi; 63827; -.
DR   Pharos; Q96GW7; Tbio.
DR   PRO; PR:Q96GW7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96GW7; Protein.
DR   Bgee; ENSG00000132692; Expressed in ventricular zone and 160 other cell types or tissues.
DR   ExpressionAtlas; Q96GW7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR   GO; GO:0072534; C:perineuronal net; IBA:GO_Central.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0010001; P:glial cell differentiation; IBA:GO_Central.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   GO; GO:0060074; P:synapse maturation; IEA:Ensembl.
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; 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; IPR003006; Ig/MHC_CS.
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; 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; PS00290; IG_MHC; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
DR   Genevisible; Q96GW7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; GPI-anchor; Hyaluronic acid;
KW   Immunoglobulin domain; Lectin; Lipoprotein; Membrane; Phosphoprotein;
KW   Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..911
FT                   /note="Brevican core protein"
FT                   /id="PRO_0000017511"
FT   DOMAIN          36..155
FT                   /note="Ig-like V-type"
FT   DOMAIN          157..252
FT                   /note="Link 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DOMAIN          257..354
FT                   /note="Link 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT   DOMAIN          646..682
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          695..809
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DOMAIN          813..873
FT                   /note="Sushi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          391..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..530
FT                   /note="O-glycosylated at two sites"
FT   REGION          540..545
FT                   /note="O-glycosylated at two sites"
FT   REGION          569..575
FT                   /note="O-glycosylated at one site"
FT   COMPBIAS        453..479
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55068"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:37453717"
FT   CARBOHYD        905
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000305|PubMed:19838169"
FT   CARBOHYD        906
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000305|PubMed:19838169"
FT   DISULFID        57..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..250
FT                   /evidence="ECO:0000250"
FT   DISULFID        203..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        277..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        650..661
FT                   /evidence="ECO:0000250"
FT   DISULFID        655..670
FT                   /evidence="ECO:0000250"
FT   DISULFID        672..681
FT                   /evidence="ECO:0000250"
FT   DISULFID        688..699
FT                   /evidence="ECO:0000250"
FT   DISULFID        716..808
FT                   /evidence="ECO:0000250"
FT   DISULFID        784..800
FT                   /evidence="ECO:0000250"
FT   DISULFID        815..858
FT                   /evidence="ECO:0000250"
FT   DISULFID        844..871
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         649..671
FT                   /note="DCVPSPCHNGGTCLEEEEGVRCL -> NSAQGSTALSILLLFFPLQLWVT
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11054543"
FT                   /id="VSP_011184"
FT   VAR_SEQ         672..911
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11054543"
FT                   /id="VSP_011185"
FT   VARIANT         356
FT                   /note="S -> L (in dbSNP:rs12065791)"
FT                   /id="VAR_050123"
FT   VARIANT         504
FT                   /note="E -> K (in dbSNP:rs1056695)"
FT                   /evidence="ECO:0000269|PubMed:12975309"
FT                   /id="VAR_019551"
FT   CONFLICT        175
FT                   /note="A -> T (in Ref. 5; AAH22938)"
FT                   /evidence="ECO:0000305"
FT   LIPID           Q96GW7-2:646
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   911 AA;  99118 MW;  5268E796FA3938D2 CRC64;
     MAQLFLPLLA ALVLAQAPAA LADVLEGDSS EDRAFRVRIA GDAPLQGVLG GALTIPCHVH
     YLRPPPSRRA VLGSPRVKWT FLSRGREAEV LVARGVRVKV NEAYRFRVAL PAYPASLTDV
     SLALSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFSGAQEACA
     RIGAHIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV
     DPDDLYDVYC YAEDLNGELF LGDPPEKLTL EEARAYCQER GAEIATTGQL YAAWDGGLDH
     CSPGWLADGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS
     AIPEASNPAS NPASDGLEAI VTVTETLEEL QLPQEATESE SRGAIYSIPI MEDGGGGSST
     PEDPAEAPRT LLEFETQSMV PPTGFSEEEG KALEEEEKYE DEEEKEEEEE EEEVEDEALW
     AWPSELSSPG PEASLPTEPA AQEESLSQAP ARAVLQPGAS PLPDGESEAS RPPRVHGPPT
     ETLPTPRERN LASPSPSTLV EAREVGEATG GPELSGVPRG ESEETGSSEG APSLLPATRA
     PEGTRELEAP SEDNSGRTAP AGTSVQAQPV LPTDSASRGG VAVVPASGDC VPSPCHNGGT
     CLEEEEGVRC LCLPGYGGDL CDVGLRFCNP GWDAFQGACY KHFSTRRSWE EAETQCRMYG
     AHLASISTPE EQDFINNRYR EYQWIGLNDR TIEGDFLWSD GVPLLYENWN PGQPDSYFLS
     GENCVVMVWH DQGQWSDVPC NYHLSYTCKM GLVSCGPPPE LPLAQVFGRP RLRYEVDTVL
     RYRCREGLAQ RNLPLIRCQE NGRWEAPQIS CVPRRPARAL HPEEDPEGRQ GRLLGRWKAL
     LIPPSSPMPG P
//