PGCB_BOVIN
ID PGCB_BOVIN Reviewed; 912 AA.
AC Q28062;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Brevican core protein;
DE Flags: Precursor;
GN Name=BCAN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8144512; DOI=10.1016/s0021-9258(17)36998-3;
RA Yamada H., Watanabe K., Shimonaka M., Yamaguchi Y.;
RT "Molecular cloning of brevican, a novel brain proteoglycan of the
RT aggrecan/versican family.";
RL J. Biol. Chem. 269:10119-10126(1994).
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: Brain; expressed in cerebellar astrocytes but not
CC in neurons.
CC -!- PTM: Contains mostly chondroitin sulfate.
CC -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC {ECO:0000305}.
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DR EMBL; X75887; CAA53481.1; -; mRNA.
DR PIR; A54423; A54423.
DR AlphaFoldDB; Q28062; -.
DR SMR; Q28062; -.
DR STRING; 9913.ENSBTAP00000020965; -.
DR PaxDb; Q28062; -.
DR PRIDE; Q28062; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q28062; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 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 Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Hyaluronic acid; Immunoglobulin domain;
KW Lectin; Phosphoprotein; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Signal; Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..912
FT /note="Brevican core protein"
FT /id="PRO_0000017509"
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 647..683
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 683..811
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 814..874
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 408..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..479
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Pro 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 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 651..662
FT /evidence="ECO:0000250"
FT DISULFID 656..671
FT /evidence="ECO:0000250"
FT DISULFID 673..682
FT /evidence="ECO:0000250"
FT DISULFID 689..700
FT /evidence="ECO:0000250"
FT DISULFID 717..809
FT /evidence="ECO:0000250"
FT DISULFID 785..801
FT /evidence="ECO:0000250"
FT DISULFID 816..859
FT /evidence="ECO:0000250"
FT DISULFID 845..872
FT /evidence="ECO:0000250"
SQ SEQUENCE 912 AA; 99554 MW; 677B3EB1C688C4D7 CRC64;
MAPLFLPLLA TLVLAWIPVA LADALEGDSS EDRAFRVRIA GDAPLQGVLG GALTIPCHVH
YLRPSPSRRA AQGSPRVKWT FLSGGREAEV LVARGLRVKV SEAYRFRVAL PAYPASLTDV
SLVLSELRPN DSGIYRCEVQ HGIDDSSDAV EVKVKGVVFL YREGSARYAF SFAGAQEACA
RIGARIATPE QLYAAYLGGY EQCDAGWLSD QTVRYPIQTP REACYGDMDG FPGVRNYGVV
DPDDLYDVYC YAEELNGELF LGAPPDKLTL EEARTYCQER GAKIATTGQL YAAWDGGLDR
CSSGWLSDGS VRYPIVTPSQ RCGGGLPGVK TLFLFPNQTG FPNKHSRFNV YCFRDSAQPS
AIPEAANPAS HLASDALEAI VTVTETLEEL KLPQEAVESE SRGAIYSIPI IEDGGGGSST
PEDPAEAPRT LLEFETQSIV PPLGSSEEEG KVLEQEEKYR GEEEKEEEEE EEEVEDEALW
AWPSELSSLD PEAPLPTEPV PEESLTQASP PVRAALQPGV SPPPYDEPEA PRPPRVLGPP
TKTLPTPREG NLASPPPSTL VGAREIEEET GGPELSGAPR GESEETGSSE DAPSLLPATR
APGDTRDLET PSEENSRRTV PAGTSVRAQP VLPTDSASRG GVAVAPSSGD CVPSPCHNGG
TCLEEEEGVR CLCLPGYGGD LCDVGLHFCS PGWDAFQGAC YKHFSARRSW EEAENKCRMY
GAHLASISTP EEQDFINNRY REYQWIGLND RTIEGDFLWS DGVPLLYENW NPGQPDSYFL
SGENCVVMVW HDQGQWSDVP CNYHLSYTCK MGLVSCGPPP ELPLAEVFGR PRLRYEVDTV
LRYRCREGLT QRNLPLIRCQ ENGRWGLPQI SCVPRRPARA LRPVEAQEGR PWRLVGHWKA
RLNPSPNPAP GP
