GenomeNet

Database: UniProt
Entry: P55068
LinkDB: P55068
Original site: P55068 
ID   PGCB_RAT                Reviewed;         883 AA.
AC   P55068; Q62860; Q63040; Q63513;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   13-FEB-2019, entry version 158.
DE   RecName: Full=Brevican core protein;
DE   AltName: Full=Brain-enriched hyaluronan-binding protein;
DE            Short=BEHAB;
DE   Flags: Precursor;
GN   Name=Bcan; Synonyms=Behab;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GPI-ANCHOR AT SER-622 (ISOFORM 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=7592978; DOI=10.1074/jbc.270.45.27206;
RA   Seidenbecher C.I., Richter K., Rauch U., Faessler R., Garner C.C.,
RA   Gundelfinger E.D.;
RT   "Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs as
RT   secreted and cell surface glycosylphosphatidylinositol-anchored
RT   isoforms.";
RL   J. Biol. Chem. 270:27206-27212(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 396-407.
RC   TISSUE=Brain;
RX   PubMed=7488217; DOI=10.1006/bbrc.1995.2713;
RA   Yamada H., Watanabe K., Shimonaka M., Yamasaki M., Yamaguchi Y.;
RT   "cDNA cloning and the identification of an aggrecanase-like cleavage
RT   site in rat brevican.";
RL   Biochem. Biophys. Res. Commun. 216:957-963(1995).
RN   [3]
RP   INTERACTION WITH TNR.
RX   PubMed=9294172; DOI=10.1073/pnas.94.19.10116;
RA   Aspberg A., Miura R., Bourdoulous S., Shimonaka M., Heinegard D.,
RA   Schachner M., Ruoslahti E., Yamaguchi Y.;
RT   "The C-type lectin domains of lecticans, a family of aggregating
RT   chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein
RT   interactions independent of carbohydrate moiety.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:10116-10121(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-423.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=7512973; DOI=10.1083/jcb.125.2.495;
RA   Jaworski D.M., Kelly G.M., Hockfield S.;
RT   "BEHAB, a new member of the proteoglycan tandem repeat family of
RT   hyaluronan-binding proteins that is restricted to the brain.";
RL   J. Cell Biol. 125:495-509(1994).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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. Isoform 2 may function as a chondroitin sulfate-
CC       bearing cell surface receptor.
CC   -!- SUBUNIT: Interacts with TNR. {ECO:0000269|PubMed:9294172}.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Secreted, extracellular space,
CC       extracellular matrix.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Membrane; Lipid-anchor, GPI-
CC       anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P55068-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55068-2; Sequence=VSP_003076, VSP_003077;
CC         Note=Contains a GPI-anchor amidated serine at position 622.
CC         {ECO:0000305|PubMed:7592978};
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 increases from day P4 to P64.
CC       Isoform 2 increases after day P8.
CC   -!- PTM: Contains mostly chondroitin sulfate.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA82215.1; Type=Frameshift; Positions=364; Evidence={ECO:0000305};
DR   EMBL; X79881; CAA56255.1; -; mRNA.
DR   EMBL; X86406; CAA60160.1; -; mRNA.
DR   EMBL; U37142; AAA87847.1; -; mRNA.
DR   EMBL; Z28366; CAA82215.1; ALT_FRAME; mRNA.
DR   PIR; A53908; A53908.
DR   PIR; S49126; S49126.
DR   RefSeq; NP_001028837.1; NM_001033665.1.
DR   RefSeq; NP_037048.2; NM_012916.2.
DR   UniGene; Rn.10315; -.
DR   UniGene; Rn.168035; -.
DR   ProteinModelPortal; P55068; -.
DR   SMR; P55068; -.
DR   BioGrid; 247431; 2.
DR   STRING; 10116.ENSRNOP00000025496; -.
DR   iPTMnet; P55068; -.
DR   PhosphoSitePlus; P55068; -.
DR   SwissPalm; P55068; -.
DR   PaxDb; P55068; -.
DR   PRIDE; P55068; -.
DR   GeneID; 25393; -.
DR   KEGG; rno:25393; -.
DR   UCSC; RGD:2194; rat. [P55068-1]
DR   CTD; 63827; -.
DR   RGD; 2194; Bcan.
DR   eggNOG; ENOG410IG1W; Eukaryota.
DR   eggNOG; ENOG410XW3U; LUCA.
DR   HOGENOM; HOG000115520; -.
DR   HOVERGEN; HBG008175; -.
DR   InParanoid; P55068; -.
DR   KO; K06795; -.
DR   OrthoDB; 174823at2759; -.
DR   PhylomeDB; P55068; -.
DR   PMAP-CutDB; P55068; -.
DR   PRO; PR:P55068; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098966; C:perisynaptic extracellular matrix; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IDA:RGD.
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:0048168; P:regulation of neuronal synaptic plasticity; IEP:RGD.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
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; 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; 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   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   GPI-anchor; Hyaluronic acid; Immunoglobulin domain; Lectin;
KW   Lipoprotein; Membrane; 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_0000017513.
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     413    413       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
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    692    784       {ECO:0000250}.
FT   DISULFID    760    776       {ECO:0000250}.
FT   DISULFID    791    834       {ECO:0000250}.
FT   DISULFID    820    847       {ECO:0000250}.
FT   VAR_SEQ     625    645       DCIPSPCHNGGTCLEEKEGFR -> NSAEGSMPAFLLFLLL
FT                                QLWDT (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_003076.
FT   VAR_SEQ     646    883       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_003077.
FT   CONFLICT     51     52       AL -> WV (in Ref. 4; CAA82215).
FT                                {ECO:0000305}.
FT   CONFLICT    503    503       V -> L (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    518    519       TV -> PA (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    526    526       G -> R (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    541    541       G -> A (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    556    556       R -> S (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    573    573       E -> A (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    583    583       V -> L (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    649    649       V -> L (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    670    670       P -> A (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    738    738       P -> A (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
FT   CONFLICT    809    809       R -> A (in Ref. 2; AAA87847).
FT                                {ECO:0000305}.
SQ   SEQUENCE   883 AA;  96057 MW;  AC7ACC40CB53ED37 CRC64;
     MIPLLLSLLA ALVLTQAPAA LADDLKEDSS EDRAFRVRIG AAQLRGVLGG ALAIPCHVHH
     LRPPPSRRAA PGFPRVKWTF LSGDREVEVL VARGLRVKVN EAYRFRVALP AYPASLTDVS
     LVLSELRPND SGVYRCEVQH GIDDSSDAVE VKVKGVVFLY REGSARYAFS FAGAQEACAR
     IGARIATPEQ LYAAYLGGYE QCDAGWLSDQ TVRYPIQNPR EACYGDMDGY PGVRNYGVVG
     PDDLYDVYCY AEDLNGELFL GAPPGKLTWE EARDYCLERG AQIASTGQLY AAWNGGLDRC
     SPGWLADGSV RYPIITPSQR CGGGLPGVKT LFLFPNQTGF PSKQNRFNVY CFRDSAHPSA
     FSEASSPASD GLEAIVTVTE KLEELQLPQE AVESESRGAI YSIPITEDGG GGSSTPEDPA
     EAPRTPLESE TQSVAPPTGS SEEEGEALEE EERFKDTETP KEEKEQENLW VWPTELSSPL
     PTGLETEHSL SQVSPPAQAV LQVGASPSPR PPRVHGPTVE TLQPPGEGSL TSTPDGAREV
     GGETGSPELS GVPREREEAG SSSLEDGPSL LPETWAPVGT REVETPSEEK SGRTVLTGTS
     VQAQPVLPTD SASRGGVAVA PSSGDCIPSP CHNGGTCLEE KEGFRCLCVP GYGGDLCDVG
     LHFCSPGWEP FQGACYKHFS TRRSWEEAES QCRALGAHLT SICTPEEQDF VNDRYREYQW
     IGLNDRTIEG DFLWSDGPPL LYENWNPGQP DSYFLSGENC VVMVWHDQGQ WSDVPCNYHL
     SYTCKMGLVS CGPPPQLPLA QIFGRPRLRY AVDTVLRYRC RDGLAQRNLP LIRCQENGLW
     EAPQISCVPR RPARALRSMT APEGPRGQLP RQRKALLTPP SSL
//
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