GenomeNet

Database: UniProt
Entry: Q9DF69
LinkDB: Q9DF69
Original site: Q9DF69 
ID   CSPG5_CHICK             Reviewed;         594 AA.
AC   Q9DF69; O13003;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-APR-2019, entry version 86.
DE   RecName: Full=Chondroitin sulfate proteoglycan 5;
DE   AltName: Full=Acidic leucine-rich EGF-like domain-containing brain protein;
DE   Contains:
DE     RecName: Full=Chondroitin sulfate proteoglycan 5, 38 kDa form;
DE   Contains:
DE     RecName: Full=Chondroitin sulfate proteoglycan 5, 80 kDa form;
DE   Flags: Precursor;
GN   Name=CSPG5; Synonyms=CALEB;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 19-32;
RP   158-166; 260-275; 339-348; 388-400; 413-423; 457-466 AND 520-532,
RP   GLYCOSYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, INTERACTION WITH TNC AND TNR, AND FUNCTION.
RC   TISSUE=Eye;
RX   PubMed=9049254; DOI=10.1083/jcb.136.4.895;
RA   Schumacher S., Volkmer H., Buck F., Otto A., Tarnok A., Roth S.,
RA   Rathjen F.G.;
RT   "Chicken acidic leucine-rich EGF-like domain containing brain protein
RT   (CALEB), a neural member of the EGF family of differentiation factors,
RT   is implicated in neurite formation.";
RL   J. Cell Biol. 136:895-906(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, AND INTERACTION WITH
RP   TNC AND TNR.
RC   TISSUE=Brain;
RX   PubMed=11069908; DOI=10.1074/jbc.M007234200;
RA   Schumacher S., Jung M., Noerenberg U., Dorner A.,
RA   Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.;
RT   "CALEB binds via its acidic stretch to the fibrinogen-like domain of
RT   tenascin-C or tenascin-R and its expression is dynamically regulated
RT   after optic nerve lesion.";
RL   J. Biol. Chem. 276:7337-7345(2001).
RN   [3]
RP   INTERACTION WITH TNR, AND MUTAGENESIS OF LEU-372 AND GLU-375.
RX   PubMed=14622101; DOI=10.1046/j.1471-4159.2003.02112.x;
RA   Schumacher S., Stuebe E.-M.;
RT   "Regulated binding of the fibrinogen-like domains of tenascin-R and
RT   tenascin-C to the neural EGF family member CALEB.";
RL   J. Neurochem. 87:1213-1223(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CELL SURFACE PROCESSING.
RX   PubMed=15848802; DOI=10.1016/j.neuron.2005.02.027;
RA   Juettner R., More M.I., Das D., Babich A., Meier J., Henning M.,
RA   Erdmann B., Mueller E.-C., Otto A., Grantyn R., Rathjen F.G.;
RT   "Impaired synapse function during postnatal development in the absence
RT   of CALEB, an EGF-like protein processed by neuronal activity.";
RL   Neuron 46:233-245(2005).
CC   -!- FUNCTION: May function as a growth and differentiation factor
CC       involved in neuritogenesis and more particularly in neurite
CC       extension. {ECO:0000269|PubMed:9049254}.
CC   -!- SUBUNIT: Binds TNC and TNR. The 80 kDa form but not the 140 kDa
CC       form can bind TNC and TNR when expressed at the cell surface.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9049254};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:9049254}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=B;
CC         IsoId=Q9DF69-1; Sequence=Displayed;
CC       Name=2; Synonyms=A;
CC         IsoId=Q9DF69-2; Sequence=VSP_015766, VSP_015767;
CC   -!- TISSUE SPECIFICITY: Expressed in astroglial and neuronal surfaces
CC       in different parts of the embryonic brain. Expressed in adult
CC       brain and retina (at protein level). {ECO:0000269|PubMed:9049254}.
CC   -!- DEVELOPMENTAL STAGE: The 80 kDa and 200 kDa forms were detected
CC       only during embryonic development. The 80 kDa form reaches a
CC       maximum of expression at E14/E15 and then decreases gradually. The
CC       140 kDa form is already detected at E7. The 130 and 140 kDa forms
CC       reach their maximal expression at E20 (at protein level).
CC       {ECO:0000269|PubMed:9049254}.
CC   -!- PTM: Different forms exist: the 140 kDa form (also reported as 130
CC       kDa), which probably consists of the entire protein, and the 38
CC       and 80 kDa forms, which are probably cleaved in their N-terminus.
CC       Increase in synaptic activity, results in shedding of the
CC       extracellular domain and expression at the cell surface of a 38
CC       kDa form. A form of 200 kDa has also been reported, which is
CC       probably hyperglycosylated.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9049254}.
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-
CC       time proteoglycan, the 200 kDa form is the only one containing
CC       chondroitin sulfate glycans. {ECO:0000269|PubMed:9049254}.
DR   EMBL; Y09264; CAA70459.1; -; mRNA.
DR   EMBL; AF292101; AAG29499.1; -; mRNA.
DR   RefSeq; NP_990050.1; NM_204719.1. [Q9DF69-2]
DR   UniGene; Gga.184; -.
DR   IntAct; Q9DF69; 1.
DR   STRING; 9031.ENSGALP00000038516; -.
DR   PRIDE; Q9DF69; -.
DR   GeneID; 395466; -.
DR   KEGG; gga:395466; -.
DR   CTD; 10675; -.
DR   HOVERGEN; HBG081361; -.
DR   InParanoid; Q9DF69; -.
DR   KO; K08116; -.
DR   OrthoDB; 433725at2759; -.
DR   PhylomeDB; Q9DF69; -.
DR   PRO; PR:Q9DF69; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR010555; CSPG5_S_attach_dom.
DR   InterPro; IPR009505; Neural_ProG_Cyt.
DR   Pfam; PF06566; Chon_Sulph_att; 1.
DR   Pfam; PF06567; Neural_ProG_Cyt; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Growth regulation;
KW   Membrane; Neurogenesis; Proteoglycan; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000269|PubMed:9049254}.
FT   CHAIN        19    594       Chondroitin sulfate proteoglycan 5.
FT                                /FTId=PRO_0000042154.
FT   CHAIN         ?    594       Chondroitin sulfate proteoglycan 5, 38
FT                                kDa form.
FT                                /FTId=PRO_0000042155.
FT   CHAIN         ?    594       Chondroitin sulfate proteoglycan 5, 80
FT                                kDa form.
FT                                /FTId=PRO_0000042156.
FT   TOPO_DOM     19    481       Extracellular. {ECO:0000255}.
FT   TRANSMEM    482    502       Helical. {ECO:0000255}.
FT   TOPO_DOM    503    594       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      429    471       EGF-like.
FT   REGION      338    377       Interaction with TNC and TNR.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    413    413       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    425    425       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    432    445       {ECO:0000250}.
FT   DISULFID    439    455       {ECO:0000250}.
FT   DISULFID    457    470       {ECO:0000250}.
FT   VAR_SEQ     544    551       DDPGAPHK -> REAQHRAL (in isoform 2).
FT                                {ECO:0000303|PubMed:9049254}.
FT                                /FTId=VSP_015766.
FT   VAR_SEQ     552    594       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:9049254}.
FT                                /FTId=VSP_015767.
FT   MUTAGEN     372    372       L->I: Partial loss of binding to TNR.
FT                                {ECO:0000269|PubMed:14622101}.
FT   MUTAGEN     375    375       E->Q: Loss of binding to TNR.
FT                                {ECO:0000269|PubMed:14622101}.
SQ   SEQUENCE   594 AA;  61376 MW;  76EAC9DF2228E9B8 CRC64;
     MGVGGTSASD TALSLCPTAP EWPPRNGSSG RAWGGPLQSG APINSTDPLG PQLEPPGGGP
     ATADPTVGCM GCSGEGAASS VPPVPDAAQD PRLGVTGPTD GDGGVVALGS PEEVGSGEQP
     TRAGVGPTEG LTPRPPGLPS PGLGLSSPGP NLGLPSLDLP NPNLGLPDPN LGLPNPSLGL
     PSPGPTPDRP IPNPNPSLDL PDPGLAIQTP NLGLSNPNIP LPSPSPGPGT EPDLLPVAED
     SEVSMELPQP SSSPAPAQRA RGRTDRTWLG APEPISAAPG TAEPPEIIDV DYYDVFDGGH
     GPGGGHGAGG AAQREPGGAA TPWGLHELYD DFTPFDEADF YPTTSFYAEG DDDAEEELEE
     DEEEEEEEDG GLEDENGYRP PASAAPRVPP PPSPTEGTPM ARPRPGERAV PENSSECRSG
     YVRHNSSCRS VCDLVPSYCH NGGQCYLVES HGAFCRCNTQ DYTWHKGTRC EAIVTDFQVL
     CVAVGSAALV LLLLFMLTVF FAKKLYLLKT ENSKLRKTKY RTPSELHNDN FSLSTIAEGS
     HPNDDPGAPH KLQDPLKPGL KDEEPLSILS TAPEEGSKGE PGGCGVPCLH NNLG
//
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