CSPG5_MOUSE
ID CSPG5_MOUSE Reviewed; 566 AA.
AC Q71M36; E9QN54; Q71M37; Q7TNT8; Q8BPJ5; Q9QY32;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chondroitin sulfate proteoglycan 5;
DE AltName: Full=Acidic leucine-rich EGF-like domain-containing brain protein;
DE AltName: Full=Neuroglycan C;
DE Flags: Precursor;
GN Name=Cspg5; Synonyms=Caleb, Ngc {ECO:0000303|PubMed:10617623};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10617623; DOI=10.1074/jbc.275.1.337;
RA Aono S., Keino H., Ono T., Yasuda Y., Tokita Y., Matsui F., Taniguchi M.,
RA Sonta S., Oohira A.;
RT "Genomic organization and expression pattern of mouse neuroglycan C in the
RT cerebellar development.";
RL J. Biol. Chem. 275:337-342(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-566 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9950058; DOI=10.1016/s0168-0102(98)00098-4;
RA Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S., Watanabe E.,
RA Nakanishi Y., Oohira A.;
RT "Cloning and chromosomal mapping of the human gene of neuroglycan C (NGC),
RT a neural transmembrane chondroitin sulfate proteoglycan with an EGF
RT module.";
RL Neurosci. Res. 32:313-322(1998).
RN [6]
RP INTERACTION WITH TNR.
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12885772; DOI=10.1074/jbc.m305577200;
RA Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S.;
RT "CALEB/NGC interacts with the Golgi-associated protein PIST.";
RL J. Biol. Chem. 278:40136-40143(2003).
RN [8]
RP TISSUE SPECIFICITY, MUTAGENESIS OF SER-38 AND SER-123, GLYCOSYLATION AT
RP SER-123, AND SUBCELLULAR LOCATION.
RX PubMed=15331613; DOI=10.1074/jbc.m403263200;
RA Aono S., Tokita Y., Shuo T., Yamauchi S., Matsui F., Nakanishi K.,
RA Hirano K., Sano M., Oohira A.;
RT "Glycosylation site for chondroitin sulfate on the neural part-time
RT proteoglycan, neuroglycan C.";
RL J. Biol. Chem. 279:46536-46541(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-475; SER-483 AND
RP SER-543, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475; SER-477 AND
RP THR-478 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394;
RP SER-396 AND THR-397 (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a growth and differentiation factor involved
CC in neuritogenesis. May induce ERBB3 activation.
CC {ECO:0000269|PubMed:15848802}.
CC -!- SUBUNIT: Binds TNR and probably TNC (By similarity). Interacts with
CC ERBB3 and GOPC. Interacts with MDK; this interaction is independent of
CC the presence of chondroitin sulfate chains and promotes elongation of
CC oligodendroglial precursor-like cells (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ERQ6, ECO:0000269|PubMed:11069908}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10617623};
CC Single-pass type I membrane protein {ECO:0000305}. Synaptic cell
CC membrane {ECO:0000269|PubMed:21183079}; Single-pass type I membrane
CC protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10617623}; Single-pass type I membrane protein
CC {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:10617623,
CC ECO:0000269|PubMed:12885772}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell surface {ECO:0000269|PubMed:15331613}.
CC Note=Partially enriched in lipid rafts (By similarity). Also detected
CC in the endoplasmic reticulum and the Golgi (PubMed:10617623).
CC {ECO:0000250|UniProtKB:Q9ERQ6, ECO:0000269|PubMed:10617623}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=NGC-III;
CC IsoId=Q71M36-1; Sequence=Displayed;
CC Name=2; Synonyms=NGC-I;
CC IsoId=Q71M36-2; Sequence=VSP_015763;
CC Name=3; Synonyms=NGC-II;
CC IsoId=Q71M36-3; Sequence=VSP_015762, VSP_015763;
CC Name=4;
CC IsoId=Q71M36-4; Sequence=VSP_015764;
CC -!- TISSUE SPECIFICITY: Expressed in olfactory bulb, hippocampus, brain
CC stem, spinal cord, cerebrum and cerebellum. Expressed by Purkinje cells
CC in the cerebellum (at protein level). Expressed in immature and mature
CC cerebellum (isoform 1, isoform 2 and isoform 3).
CC {ECO:0000269|PubMed:10617623, ECO:0000269|PubMed:15331613,
CC ECO:0000269|PubMed:9950058}.
CC -!- DEVELOPMENTAL STAGE: The proteoglycan form decreases from birth to
CC adulthood in the cerebellum concomitant with non-proteoglycan form
CC increase. In the cerebrum the maximum of expression of the proteoglycan
CC is detected 15 days after birth and then decreases gradually to reach
CC half-level at adulthood (at protein level).
CC {ECO:0000269|PubMed:10617623}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-time
CC proteoglycan, expressed in part as a proteoglycan exhibiting
CC chondroitin sulfate glycans and in part as a non-proteoglycan form. The
CC relative amount of both forms depends on tissues and tissues
CC maturation. In the cerebellum the 2 forms coexist while in the cerebrum
CC the proteoglycan form is predominant. {ECO:0000269|PubMed:10617623,
CC ECO:0000269|PubMed:15331613}.
CC -!- PTM: Phosphorylated; in intracellular and extracellular parts.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Altered synaptic transmission at early
CC developmental stages. {ECO:0000269|PubMed:15848802}.
CC -!- MISCELLANEOUS: Different forms of various molecular weight have been
CC observed. Such forms are possibly due to different levels of
CC glycosylation, phosphorylation and/or protein cleavage.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ04778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35578.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF133700; AAF23362.1; -; mRNA.
DR EMBL; AF461090; AAQ04777.1; -; mRNA.
DR EMBL; AF461091; AAQ04778.1; ALT_INIT; mRNA.
DR EMBL; AF461092; AAQ04779.1; -; mRNA.
DR EMBL; AC159372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055736; AAH55736.1; -; mRNA.
DR EMBL; AK053891; BAC35578.1; ALT_INIT; mRNA.
DR CCDS; CCDS52936.1; -. [Q71M36-1]
DR CCDS; CCDS81085.1; -. [Q71M36-2]
DR RefSeq; NP_001159745.1; NM_001166273.1. [Q71M36-1]
DR RefSeq; NP_038912.3; NM_013884.3. [Q71M36-2]
DR AlphaFoldDB; Q71M36; -.
DR STRING; 10090.ENSMUSP00000035058; -.
DR GlyConnect; 2214; 5 N-Linked glycans (1 site).
DR GlyGen; Q71M36; 13 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q71M36; -.
DR PhosphoSitePlus; Q71M36; -.
DR MaxQB; Q71M36; -.
DR PaxDb; Q71M36; -.
DR PeptideAtlas; Q71M36; -.
DR PRIDE; Q71M36; -.
DR ProteomicsDB; 284043; -. [Q71M36-1]
DR ProteomicsDB; 284044; -. [Q71M36-2]
DR ProteomicsDB; 284045; -. [Q71M36-3]
DR ProteomicsDB; 284046; -. [Q71M36-4]
DR Antibodypedia; 29949; 264 antibodies from 31 providers.
DR DNASU; 29873; -.
DR Ensembl; ENSMUST00000035058; ENSMUSP00000035058; ENSMUSG00000032482. [Q71M36-1]
DR Ensembl; ENSMUST00000196060; ENSMUSP00000143164; ENSMUSG00000032482. [Q71M36-2]
DR Ensembl; ENSMUST00000197850; ENSMUSP00000143005; ENSMUSG00000032482. [Q71M36-4]
DR Ensembl; ENSMUST00000199736; ENSMUSP00000142845; ENSMUSG00000032482. [Q71M36-3]
DR GeneID; 29873; -.
DR KEGG; mmu:29873; -.
DR UCSC; uc009rtq.2; mouse. [Q71M36-1]
DR UCSC; uc009rtr.2; mouse. [Q71M36-2]
DR UCSC; uc009rtt.1; mouse. [Q71M36-3]
DR UCSC; uc009rtu.1; mouse. [Q71M36-4]
DR CTD; 10675; -.
DR MGI; MGI:1352747; Cspg5.
DR VEuPathDB; HostDB:ENSMUSG00000032482; -.
DR eggNOG; ENOG502QXSB; Eukaryota.
DR GeneTree; ENSGT00440000034270; -.
DR InParanoid; Q71M36; -.
DR OMA; NIGAFCX; -.
DR OrthoDB; 433725at2759; -.
DR PhylomeDB; Q71M36; -.
DR TreeFam; TF338636; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-MMU-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR BioGRID-ORCS; 29873; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Cspg5; mouse.
DR PRO; PR:Q71M36; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q71M36; protein.
DR Bgee; ENSMUSG00000032482; Expressed in visual cortex and 146 other tissues.
DR Genevisible; Q71M36; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
DR GO; GO:0048858; P:cell projection morphogenesis; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0106091; P:glial cell projection elongation; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0099550; P:trans-synaptic signaling, modulating synaptic transmission; IMP:SynGO.
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; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Growth regulation; Membrane; Neurogenesis;
KW Phosphoprotein; Proteoglycan; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..566
FT /note="Chondroitin sulfate proteoglycan 5"
FT /id="PRO_0000042152"
FT TOPO_DOM 31..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 371..413
FT /note="EGF-like"
FT REGION 56..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..301
FT /note="Interaction with TNC and TNR"
FT /evidence="ECO:0000269|PubMed:11069908"
FT REGION 442..460
FT /note="Interaction with GOPC"
FT /evidence="ECO:0000250"
FT REGION 531..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000269|PubMed:15331613"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 374..387
FT /evidence="ECO:0000250"
FT DISULFID 381..397
FT /evidence="ECO:0000250"
FT DISULFID 399..412
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10617623"
FT /id="VSP_015762"
FT VAR_SEQ 487..513
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10617623,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015763"
FT VAR_SEQ 514..566
FT /note="DDPSAPHKIQDPLKSRLKEEESFNIQNSMSPKLEGGKGDQDDLGVNCLQNNL
FT T -> VTYLPHISPFACLCPCLPLPPCPLALSQSRQSPNSFEDQLRATQWCRERCIDSL
FT TV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015764"
FT MUTAGEN 38
FT /note="S->A: No effect on chondroitin sulfate attachment."
FT /evidence="ECO:0000269|PubMed:15331613"
FT MUTAGEN 123
FT /note="S->A: No chondroitin sulfate attachment. no effect
FT on transport to the cell surface."
FT /evidence="ECO:0000269|PubMed:15331613"
FT CONFLICT 317
FT /note="T -> N (in Ref. 1; AAF23362/AAQ04777/AAQ04778/
FT AAQ04779)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="N -> H (in Ref. 3; AAH55736)"
FT /evidence="ECO:0000305"
FT MOD_RES Q71M36-2:475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q71M36-2:477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q71M36-2:478
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q71M36-3:394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q71M36-3:396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q71M36-3:397
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 566 AA; 60406 MW; 8AB75BA1ACB11BDE CRC64;
MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR
EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE
AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE
VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP
DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL
LLPSQKPGVG PGTGQPTNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR
VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ
VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA
EGSHPNVRKF CDTPRVSSPH ARALAHYDNI VCQDDPSAPH KIQDPLKSRL KEEESFNIQN
SMSPKLEGGK GDQDDLGVNC LQNNLT
