CSPG5_CHICK
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 03-AUG-2022, entry version 97.
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; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 19-32; 158-166;
RP 260-275; 339-348; 388-400; 413-423; 457-466 AND 520-532, GLYCOSYLATION,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION
RP 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, is
RT implicated in neurite formation.";
RL J. Cell Biol. 136:895-906(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, AND INTERACTION WITH TNC
RP AND TNR.
RC TISSUE=Brain;
RX PubMed=11069908; DOI=10.1074/jbc.m007234200;
RA Schumacher S., Jung M., Noerenberg U., Dorner A., Chiquet-Ehrismann R.,
RA 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 after
RT 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 of
RT 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 involved
CC in neuritogenesis and more particularly in neurite extension.
CC {ECO:0000269|PubMed:9049254}.
CC -!- SUBUNIT: Binds TNC and TNR. The 80 kDa form but not the 140 kDa form
CC 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 in
CC different parts of the embryonic brain. Expressed in adult brain and
CC retina (at protein level). {ECO:0000269|PubMed:9049254}.
CC -!- DEVELOPMENTAL STAGE: The 80 kDa and 200 kDa forms were detected only
CC during embryonic development. The 80 kDa form reaches a maximum of
CC expression at E14/E15 and then decreases gradually. The 140 kDa form is
CC already detected at E7. The 130 and 140 kDa forms reach their maximal
CC expression at E20 (at protein level). {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 and 80
CC kDa forms, which are probably cleaved in their N-terminus. Increase in
CC synaptic activity, results in shedding of the extracellular domain and
CC expression at the cell surface of a 38 kDa form. A form of 200 kDa has
CC also been reported, which is probably hyperglycosylated.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9049254}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-time
CC proteoglycan, the 200 kDa form is the only one containing chondroitin
CC sulfate glycans. {ECO:0000269|PubMed:9049254}.
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DR EMBL; Y09264; CAA70459.1; -; mRNA.
DR EMBL; AF292101; AAG29499.1; -; mRNA.
DR RefSeq; NP_990050.1; NM_204719.1. [Q9DF69-2]
DR AlphaFoldDB; Q9DF69; -.
DR IntAct; Q9DF69; 1.
DR STRING; 9031.ENSGALP00000038516; -.
DR GeneID; 395466; -.
DR KEGG; gga:395466; -.
DR CTD; 10675; -.
DR VEuPathDB; HostDB:geneid_395466; -.
DR eggNOG; ENOG502QXSB; Eukaryota.
DR InParanoid; Q9DF69; -.
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:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048858; P:cell projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0099550; P:trans-synaptic signaling, modulating synaptic transmission; IBA:GO_Central.
DR InterPro; IPR042382; CSPG5.
DR InterPro; IPR010555; CSPG5_S_attach_dom.
DR InterPro; IPR009505; Neural_ProG_Cyt.
DR PANTHER; PTHR15381; PTHR15381; 1.
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; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Growth regulation; Membrane; Neurogenesis;
KW Proteoglycan; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:9049254"
FT CHAIN 19..594
FT /note="Chondroitin sulfate proteoglycan 5"
FT /id="PRO_0000042154"
FT CHAIN ?..594
FT /note="Chondroitin sulfate proteoglycan 5, 38 kDa form"
FT /id="PRO_0000042155"
FT CHAIN ?..594
FT /note="Chondroitin sulfate proteoglycan 5, 80 kDa form"
FT /id="PRO_0000042156"
FT TOPO_DOM 19..481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 429..471
FT /note="EGF-like"
FT REGION 1..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..377
FT /note="Interaction with TNC and TNR"
FT REGION 343..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..373
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 432..445
FT /evidence="ECO:0000250"
FT DISULFID 439..455
FT /evidence="ECO:0000250"
FT DISULFID 457..470
FT /evidence="ECO:0000250"
FT VAR_SEQ 544..551
FT /note="DDPGAPHK -> REAQHRAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9049254"
FT /id="VSP_015766"
FT VAR_SEQ 552..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9049254"
FT /id="VSP_015767"
FT MUTAGEN 372
FT /note="L->I: Partial loss of binding to TNR."
FT /evidence="ECO:0000269|PubMed:14622101"
FT MUTAGEN 375
FT /note="E->Q: Loss of binding to TNR."
FT /evidence="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
