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0PGCB_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBCAN
DescriptionBrevican core protein precursor (brain enriched hyaluronan binding protein) (behab protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Animal lectins display a wide variety of architectures.They are classified according to the carbohydrate-recognitiondomain (CRD) of which there are two main types.-type and C-type .C-type lectins display a wide range of specificities.They require Ca2+ for their activityThey are found predominantly but not exclusively in vertebrates.They can be classified into a number of subgroups based on their function and structure: Endocytic lectins - Membrane-bound receptors that mediate endocytosis of glycoproteins Collectins - Represented by the soluble mannose-binding proteins of mammalian serum and liver Selectins - Membrane-bound proteins involved in inflammation .D22 (also called BL-CAM or Lyb8) are adhesion and signaling molecules. Targeted disruption of CD22 in mice results in a reduced level of surface IgM on peripheral B cells.nhanced Ca2+ flux in response to Ig signaling.ariable proliferative responses to surface Ig crosslinking. Several studies observed a reduced response to thymus independent antigens. The CD22-knockout data support a role for CD22 in limiting antigen receptor signaling although a positive role in certain B cell response cannot be excluded. CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at http://www.ncbi.nlm.nih.gov/PROW/guide/45277084.htm
  IPR001304:C-type lectin
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . Ig-like domains can be classified according to the number of beta strands. The V-type is antibody variable domain-like.nd has two extra beta strands over the classical C1-type Ig-like domain. This subfamily includes Ig variable domains.yelin membrane adhesion molecules. cell surface glycoproteins.unction adhesion molecules (JAM).oxsackie virus and adenovirus Car receptors.nd viral haemagglutinin.
  IPR003596:Immunoglobulin V-set, subgroup
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Sushi domains are also known as Complement control protein (CCP) modules.r short consensus repeats (SCR).xist in a widevariety of complement and adhesion proteins. The structure is known for this domain.t is based on a beta-sandwich arrangement; oneface made up of three beta-strands hydrogen-bonded to form a triple-stranded region at itscentre and the other face formed from two separate beta-strands .CD21 (also called C3d receptor.R2.pstein Barr virus receptor or EBV-R) is the receptor for EBV and for C3d.3dg and iC3b. Complement components may activate B cells through CD21. CD21 is part of a large signal-transduction complex that also involves CD19.D81.nd Leu13. Some of the proteins in this group are responsible for the molecular basis of the blood group antigens.urface markers on the outside of the red blood cell membrane. Most of these markers are proteins.ut some are carbohydrates attached to lipids or proteins [Reid M.E..omas-Francis C. The Blood Group Antigen FactsBook Academic Press.ondon / San Diego.1997)]. Complement decay-accelerating factor (Antigen CD55) belongs to the Cromer blood group system and is associated with Cr(a).r(a).s(a).c(a/b/c).d(a).ES(a/b).FC and UMC antigens. Complement receptor type 1 (C3b/C4b receptor) (Antigen CD35) belongs to the Knops blood group system and is associated with Kn(a/b).cC(a).l(a) and Yk(a) antigens.CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at http://www.ncbi.nlm.nih.gov/PROW/guide/45277084.htm
  IPR000436:Sushi/SCR/CCP
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents the V-set domains.hich are Ig-like domains resembling the antibody variable domain. V-set domains are found in diverse protein families.ncluding immunoglobulin light and heavy chains; in several T-cell receptors such as CD2 (Cluster of Differentiation 2).D4.D80.nd CD86; in myelin membrane adhesion molecules; in junction adhesion molecules (JAM); in tyrosine-protein kinase receptors; and in the programmed cell death protein 1 (PD1).
  IPR013106:Immunoglobulin V-set
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
The link domain is a hyaluronan(HA)-binding region found in proteins of vertebrates that are involved in the assembly of extracellular matrix.ell adhesion.nd migration. The structure has been shown to consist of two alpha helices and two antiparallel beta sheets arranged around a large hydrophobic core similar to that of C-typelectin. This domain contains four conserved cysteines involved in two disulphide bonds. The link domain has also been termed HABM (HA binding module) and PTR (proteoglycan tandem repeat). Proteins with such a domain include the proteoglycans aggrecan.revican.eurocan and versican.hich are expressed in the CNS; the cartilage link protein (LP). proteoglycan that together with HA and aggrecan forms multimolecular aggregates; Tumor necrosis factor-inducible protein TSG-6.hich may be involved in cell-cell and cell-matrix interactions during inflammation and tumorgenesis; and CD44 antigen.he main cell surface receptor for HA.
  IPR000538:Link
Marine teleosts from polar oceans can be protected from freezing in icysea-water by serum antifreeze proteins (AFPs) or glycoproteins (AFGPs) .These function by binding to.nd preventing the growth of.ce crystalswithin the fish. Despite functional similarity.he proteins arestructurally diverse and include glycosylated and at least 3 non-glycosylated forms: the AFGP of nototheniids and cod are polymers of atripeptide repeat.la-Ala-Thr.ith a disaccharide attached to thethreonine residue; type I AFPs are Ala-rich.lpha-helical peptidesfound in flounder and sculpin; type II AFPs of sea-raven.melt andherring are Cys-rich proteins; and type III AFPs.ound in eel pouts.re rich in beta-structure. Although no direct structural information is available for type II AFPs.heir sequences are similar to the carbohydrate recognition domain (CRD)of Ca2+-dependent lectins. This domain is present in a superfamily ofproteins that bind sugars specifically through contact with a calciumion. The extent of similarity within the superfamily is confined to short motifs and single amino acids at intervals throughout the protein.
  IPR002353:Type II antifreeze protein
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
IPR000538:Xlink 
Evalue:-101.130767822266 
Location:257-353IPR000538:Xlink 
Evalue:-95.2757263183594 
Location:156-251IPR001304:CLECT 
Evalue:-35.301029995664 
Location:688-809IPR003596:IGv 
Evalue:-11.4948500216801 
Location:52-139IPR006209:EGF 
Evalue:-9.02227592468262 
Location:650-681IPR000436:Sushi 
Evalue:-8.52287864685059 
Location:815-871
SequencesProtein: PGCB_HUMAN (911 aa)
mRNA: NM_021948
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK06795
  Level 3 annotation:
    brevican
  Level 2 annotation:
    Proteoglycans
    Cell adhesion molecules (CAMs)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 110 residues, 154878363-154878691Exon2: 35 residues, 154882462-154882561Exon3: 127 residues, 154883216-154883591Exon4: 60 residues, 154883923-154884098Exon5: 44 residues, 154884398-154884526Exon6: 100 residues, 154884983-154885277Exon7: 80 residues, 154887871-154888105Exon8: 217 residues, 154888663-154889308Exon9: 38 residues, 154892697-154892805Exon10: 55 residues, 154893353-154893512Exon11: 29 residues, 154894090-154894173Exon12: 50 residues, 154894542-154894687Exon13: 65 residues, 154894958-154895149Exon14: 168 residues, 154895442-154895942Exon15: 2 residues, -Jump to PGCB_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3833 152220753-152225430 ~-5K 2681(RAB13)(-)Loci: 2551 152511662-152514973 ~-3K 2706(HAX1)(+)Loci: 2552 152806880-152815707 ~-9K 2720(CHRNB2)(+)Loci: 3834 152821158-152847306 ~-26K 2722(ADAR)(-)Loci: 3835 153201398-153209847 ~-8K 2739(SHC1)(-)Loci: 2553 153412983-153424069 ~-11K 2783(TRIM46)(+)Loci: 2554 153513997-153526262 ~-12K 2831(HCN3)(+)Loci: 3836 153526253-153537835 ~-12K 2833(PKLR)(-)Loci: 2555 153669594-153670676 ~-1K 2846(POU5FLC1)(+)Loci: 2556 154095923-154121459 ~-26K 2875(SYT11)(+)Loci: 3837 154183269-154214942 ~-32K 2882(ARHGEF2)(-)Loci: 2557 154297589-154306917 ~-9K 2890(RAB25)(+)Loci: 2558 154362603-154374280 ~-12K 2897(+)Loci: 2559 154855709-154862142 ~-6K 2944(HAPLN2)(+)Loci: 2560 154878363-154895942 ~-18K 2945(BCAN)(+)Loci: 3838 154905181-154913813 ~-9K 2947(NES)(-)Loci: 2561 155097294-155118266 ~-21K 2961(NTRK1)(+)Loci: 3839 155171256-155281786 ~-111K 2965(ARHGEF11)(-)Loci: 2550 151897823-151900928 ~-3K 2658(SNAPAP)(+)Link out to UCSC