PGCB_RAT
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 03-AUG-2022, entry version 175.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 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 site
RT 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 BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Isoform 2
CC may function as a chondroitin sulfate-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-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 -!- TISSUE SPECIFICITY: Brain.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 increases from day P4 to P64. Isoform 2
CC 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; Evidence={ECO:0000305};
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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 AlphaFoldDB; P55068; -.
DR SMR; P55068; -.
DR BioGRID; 247431; 2.
DR IntAct; P55068; 1.
DR MINT; P55068; -.
DR STRING; 10116.ENSRNOP00000025496; -.
DR GlyGen; P55068; 2 sites.
DR iPTMnet; P55068; -.
DR PhosphoSitePlus; P55068; -.
DR SwissPalm; P55068; -.
DR PaxDb; P55068; -.
DR PRIDE; P55068; -.
DR ABCD; P55068; 2 sequenced antibodies.
DR GeneID; 25393; -.
DR KEGG; rno:25393; -.
DR UCSC; RGD:2194; rat. [P55068-1]
DR CTD; 63827; -.
DR RGD; 2194; Bcan.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P55068; -.
DR PhylomeDB; P55068; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-RNO-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR PRO; PR:P55068; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043194; C:axon initial segment; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
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:0033268; C:node of Ranvier; IDA:RGD.
DR GO; GO:0072534; C:perineuronal net; IDA:RGD.
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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:RGD.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0042063; P:gliogenesis; IEP:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:1990138; P:neuron projection extension; IDA:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEP:RGD.
DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; ISO:RGD.
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; 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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; GPI-anchor;
KW Hyaluronic acid; Immunoglobulin domain; Lectin; Lipoprotein; Membrane;
KW Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted; Signal;
KW Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..883
FT /note="Brevican core protein"
FT /id="PRO_0000017513"
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 389..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 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 VAR_SEQ 625..645
FT /note="DCIPSPCHNGGTCLEEKEGFR -> NSAEGSMPAFLLFLLLQLWDT (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003076"
FT VAR_SEQ 646..883
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003077"
FT CONFLICT 51..52
FT /note="AL -> WV (in Ref. 4; CAA82215)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="V -> L (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 518..519
FT /note="TV -> PA (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="G -> R (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="G -> A (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="R -> S (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="E -> A (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="V -> L (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="V -> L (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="P -> A (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="P -> A (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="R -> A (in Ref. 2; AAA87847)"
FT /evidence="ECO:0000305"
FT LIPID P55068-2:622
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000305|PubMed:7592978"
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
