GenomeNet

Database: UniProt
Entry: Q61361
LinkDB: Q61361
Original site: Q61361 
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   13-FEB-2019, entry version 164.
DE   RecName: Full=Brevican core protein;
DE   Flags: Precursor;
GN   Name=Bcan;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
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.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May play a role in the terminally differentiating and
CC       the adult nervous system during postnatal development. Could
CC       stabilize interactions between hyaluronan (HA) and brain
CC       proteoglycans.
CC   -!- SUBUNIT: Interacts with TNR. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Brain.
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";
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   UniGene; Mm.4598; -.
DR   ProteinModelPortal; Q61361; -.
DR   SMR; Q61361; -.
DR   IntAct; Q61361; 2.
DR   MINT; Q61361; -.
DR   STRING; 10090.ENSMUSP00000088491; -.
DR   iPTMnet; Q61361; -.
DR   PhosphoSitePlus; Q61361; -.
DR   MaxQB; Q61361; -.
DR   PaxDb; Q61361; -.
DR   PeptideAtlas; Q61361; -.
DR   PRIDE; Q61361; -.
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   eggNOG; ENOG410IG1W; Eukaryota.
DR   eggNOG; ENOG410XW3U; LUCA.
DR   GeneTree; ENSGT00940000157343; -.
DR   HOGENOM; HOG000115520; -.
DR   HOVERGEN; HBG008175; -.
DR   InParanoid; Q61361; -.
DR   KO; K06795; -.
DR   OMA; NNRYREY; -.
DR   OrthoDB; 174823at2759; -.
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   ChiTaRS; Bcan; mouse.
DR   PRO; PR:Q61361; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000004892; Expressed in 136 organ(s), highest expression level in cerebellum.
DR   ExpressionAtlas; Q61361; baseline and differential.
DR   Genevisible; Q61361; MM.
DR   GO; GO:0031225; C:anchored component of membrane; 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: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:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0021766; P:hippocampus development; IMP: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; IPR013032; EGF-like_CS.
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   Complete proteome; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Hyaluronic acid;
KW   Immunoglobulin domain; Lectin; Phosphoprotein; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    883       Brevican core protein.
FT                                /FTId=PRO_0000017512.
FT   DOMAIN       35    154       Ig-like V-type.
FT   DOMAIN      156    251       Link 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      256    353       Link 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00323}.
FT   DOMAIN      622    658       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      658    786       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      789    849       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   MOD_RES     224    224       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     413    413       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P55068}.
FT   CARBOHYD    129    129       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    336    336       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     56    136       {ECO:0000250}.
FT   DISULFID    178    249       {ECO:0000250}.
FT   DISULFID    202    223       {ECO:0000250}.
FT   DISULFID    276    351       {ECO:0000250}.
FT   DISULFID    300    321       {ECO:0000250}.
FT   DISULFID    626    637       {ECO:0000250}.
FT   DISULFID    631    646       {ECO:0000250}.
FT   DISULFID    648    657       {ECO:0000250}.
FT   DISULFID    664    675       {ECO:0000250}.
FT   DISULFID    692    784       {ECO:0000250}.
FT   DISULFID    760    776       {ECO:0000250}.
FT   DISULFID    791    834       {ECO:0000250}.
FT   DISULFID    820    847       {ECO:0000250}.
FT   CONFLICT     42     42       T -> A (in Ref. 1; CAA60575).
FT                                {ECO:0000305}.
FT   CONFLICT     65     65       H -> R (in Ref. 1; CAA60575).
FT                                {ECO:0000305}.
FT   CONFLICT    504    504       G -> D (in Ref. 1; CAA60575).
FT                                {ECO:0000305}.
FT   CONFLICT    514    514       V -> F (in Ref. 1; CAA60575).
FT                                {ECO:0000305}.
FT   CONFLICT    528    530       GSP -> WSA (in Ref. 1; CAA60575).
FT                                {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
//
DBGET integrated database retrieval system