PGCB_MOUSE
ID PGCB_MOUSE Reviewed; 883 AA.
AC Q61361; Q80WT7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Brevican core protein;
DE Flags: Precursor;
GN Name=Bcan;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9286696; DOI=10.1006/geno.1997.4853;
RA Rauch U., Meyer H., Brakebusch C., Seidenbecher C., Gundelfinger E.D.,
RA Beier D.R., Fassler R.;
RT "Sequence and chromosomal localization of the mouse brevican gene.";
RL Genomics 44:15-21(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=14550776; DOI=10.1016/s1044-7431(03)00133-7;
RA Bekku Y., Su W.-D., Hirakawa S., Faessler R., Ohtsuka A., Kang J.S.,
RA Sanders J., Murakami T., Ninomiya Y., Oohashi T.;
RT "Molecular cloning of Bral2, a novel brain-specific link protein, and
RT immunohistochemical colocalization with brevican in perineuronal nets.";
RL Mol. Cell. Neurosci. 24:148-159(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22121037; DOI=10.1002/cne.23009;
RA Bekku Y., Saito M., Moser M., Fuchigami M., Maehara A., Nakayama M.,
RA Kusachi S., Ninomiya Y., Oohashi T.;
RT "Bral2 is indispensable for the proper localization of brevican and the
RT structural integrity of the perineuronal net in the brainstem and
RT cerebellum.";
RL J. Comp. Neurol. 520:1721-1736(2012).
RN [8]
RP TISSUE SPECIFICITY.
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).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina, specifically around the
CC inner and outer segments of photoreceptors, retinal pigment epithelium,
CC outer plexiform layer, and the ganglion cell layer (at protein level)
CC (PubMed:29777959). Brain (PubMed:9286696, PubMed:14550776,
CC PubMed:22121037). Expressed in the brainstem and cerebellum in a
CC perineuronal net pattern (PubMed:14550776, PubMed:22121037).
CC {ECO:0000269|PubMed:14550776, ECO:0000269|PubMed:22121037,
CC ECO:0000269|PubMed:29777959, ECO:0000269|PubMed:9286696}.
CC -!- PTM: Contains mostly chondroitin sulfate. {ECO:0000250}.
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_mou_Ctlect_155";
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; X87096; CAA60575.1; -; mRNA.
DR EMBL; CH466547; EDL15323.1; -; Genomic_DNA.
DR EMBL; BC052032; AAH52032.1; -; mRNA.
DR CCDS; CCDS17462.1; -.
DR PIR; S57653; S57653.
DR RefSeq; NP_001103228.1; NM_001109758.1.
DR RefSeq; NP_031555.2; NM_007529.2.
DR RefSeq; XP_006500999.1; XM_006500936.3.
DR RefSeq; XP_006501000.1; XM_006500937.3.
DR AlphaFoldDB; Q61361; -.
DR SMR; Q61361; -.
DR BioGRID; 198308; 2.
DR IntAct; Q61361; 2.
DR MINT; Q61361; -.
DR STRING; 10090.ENSMUSP00000088491; -.
DR GlyConnect; 2161; 9 N-Linked glycans (2 sites).
DR GlyGen; Q61361; 2 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; Q61361; -.
DR PhosphoSitePlus; Q61361; -.
DR jPOST; Q61361; -.
DR MaxQB; Q61361; -.
DR PaxDb; Q61361; -.
DR PeptideAtlas; Q61361; -.
DR PRIDE; Q61361; -.
DR ProteomicsDB; 288130; -.
DR ABCD; Q61361; 2 sequenced antibodies.
DR Antibodypedia; 2188; 198 antibodies from 29 providers.
DR DNASU; 12032; -.
DR Ensembl; ENSMUST00000090971; ENSMUSP00000088491; ENSMUSG00000004892.
DR GeneID; 12032; -.
DR KEGG; mmu:12032; -.
DR UCSC; uc008pto.2; mouse.
DR CTD; 63827; -.
DR MGI; MGI:1096385; Bcan.
DR VEuPathDB; HostDB:ENSMUSG00000004892; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000157343; -.
DR HOGENOM; CLU_000303_0_0_1; -.
DR InParanoid; Q61361; -.
DR OMA; APQISCV; -.
DR OrthoDB; 174823at2759; -.
DR PhylomeDB; Q61361; -.
DR TreeFam; TF332134; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR BioGRID-ORCS; 12032; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Bcan; mouse.
DR PRO; PR:Q61361; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q61361; protein.
DR Bgee; ENSMUSG00000004892; Expressed in superior frontal gyrus and 112 other tissues.
DR ExpressionAtlas; Q61361; baseline and differential.
DR Genevisible; Q61361; MM.
DR GO; GO:0031225; C:anchored component of membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043194; C:axon initial segment; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0033268; C:node of Ranvier; ISO:MGI.
DR GO; GO:0072534; C:perineuronal net; IDA:UniProtKB.
DR GO; GO:0098966; C:perisynaptic extracellular matrix; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
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:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IDA:SynGO.
DR CDD; cd00033; CCP; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.100.10; -; 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; 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 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; SM00406; IGv; 1.
DR SMART; SM00445; LINK; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56436; SSF56436; 3.
DR SUPFAM; SSF57535; SSF57535; 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.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Hyaluronic acid; Immunoglobulin domain; Lectin; Phosphoprotein;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..883
FT /note="Brevican core protein"
FT /id="PRO_0000017512"
FT DOMAIN 35..154
FT /note="Ig-like V-type"
FT DOMAIN 156..251
FT /note="Link 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 256..353
FT /note="Link 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DOMAIN 622..658
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 658..786
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 789..849
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 402..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55068"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..136
FT /evidence="ECO:0000250"
FT DISULFID 178..249
FT /evidence="ECO:0000250"
FT DISULFID 202..223
FT /evidence="ECO:0000250"
FT DISULFID 276..351
FT /evidence="ECO:0000250"
FT DISULFID 300..321
FT /evidence="ECO:0000250"
FT DISULFID 626..637
FT /evidence="ECO:0000250"
FT DISULFID 631..646
FT /evidence="ECO:0000250"
FT DISULFID 648..657
FT /evidence="ECO:0000250"
FT DISULFID 664..675
FT /evidence="ECO:0000250"
FT DISULFID 692..784
FT /evidence="ECO:0000250"
FT DISULFID 760..776
FT /evidence="ECO:0000250"
FT DISULFID 791..834
FT /evidence="ECO:0000250"
FT DISULFID 820..847
FT /evidence="ECO:0000250"
FT CONFLICT 42
FT /note="T -> A (in Ref. 1; CAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="H -> R (in Ref. 1; CAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="G -> D (in Ref. 1; CAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="V -> F (in Ref. 1; CAA60575)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..530
FT /note="GSP -> WSA (in Ref. 1; CAA60575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 95815 MW; 64DDE4D951D2042A CRC64;
MIPLLLSLLA ALVLTQAPAA LADDLKEDSS EDRAFRVRIG ATQLRGVLGG ALAIPCHVHH
LRPPHSRRAA PGFPRVKWTF LSGDREVEVL VARGLRVKVN EAYRFRVALP AYPASLTDVS
LVLSELRPND SGVYRCEVQH GIDDSSDAVE VKVKGVVFLY REGSARYAFS FAGAQEACAR
IGARIATPEQ LYAAYLGGYE QCDAGWLSDQ TVRYPIQNPR EACSGDMDGY PGVRNYGVVG
PDDLYDVYCY AEDLNGELFL GAPPSKLTWE EARDYCLERG AQIASTGQLY AAWNGGLDRC
SPGWLADGSV RYPIITPSQR CGGGLPGVKT LFLFPNQTGF PSKQNRFNVY CFRDSAHPSA
SSEASSPASD GLEAIVTVTE KLEELQLPQE AMESESRGAI YSIPISEDGG GGSSTPEDPA
EAPRTPLESE TQSIAPPTES SEEEGVALEE EERFKDLEAL EEEKEQEDLW VWPRELSSPL
PTGSETEHSL SQVSPPAQAV LQLGASPSPG PPRVRGPPAE TLLPPREGSP TSTPGGAREV
GGETGSPELS GVPRESEEAG SSSLEDGPSL LPATWAPVGP RELETPSEEK SGRTVLAGTS
VQAQPVLPTD SASHGGVAVA PSSGDCIPSP CHNGGTCLEE KEGFRCLCLP GYGGDLCDVG
LHFCSPGWEA FQGACYKHFS TRRSWEEAES QCRALGAHLT SICTPEEQDF VNDRYREYQW
IGLNDRTIEG DFLWSDGAPL LYENWNPGQP DSYFLSGENC VVMVWHDQGQ WSDVPCNYHL
SYTCKMGLVS CGPPPQLPLA QIFGRPRLRY AVDTVLRYRC RDGLAQRNLP LIRCQENGLW
EAPQISCVPR RPGRALRSMD APEGPRGQLS RHRKAPLTPP SSL
