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   27-MAR-2024, entry version 151.
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}. Secreted
CC       {ECO:0000250|UniProtKB:O95196}. Note=Partially enriched in lipid rafts
CC       (By similarity). Also detected in the endoplasmic reticulum and the
CC       Golgi (PubMed:10617623). {ECO:0000250|UniProtKB:Q9ERQ6,
CC       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 tissue maturation.
CC       In the cerebellum the 2 forms coexist while in the cerebrum the
CC       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   BioGRID; 205937; 1.
DR   STRING; 10090.ENSMUSP00000035058; -.
DR   GlyConnect; 2214; 5 N-Linked glycans (1 site).
DR   GlyCosmos; Q71M36; 13 sites, 5 glycans.
DR   GlyGen; Q71M36; 15 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q71M36; -.
DR   PhosphoSitePlus; Q71M36; -.
DR   SwissPalm; Q71M36; -.
DR   MaxQB; Q71M36; -.
DR   PaxDb; 10090-ENSMUSP00000035058; -.
DR   PeptideAtlas; Q71M36; -.
DR   ProteomicsDB; 284043; -. [Q71M36-1]
DR   ProteomicsDB; 284044; -. [Q71M36-2]
DR   ProteomicsDB; 284045; -. [Q71M36-3]
DR   ProteomicsDB; 284046; -. [Q71M36-4]
DR   Antibodypedia; 29949; 278 antibodies from 31 providers.
DR   DNASU; 29873; -.
DR   Ensembl; ENSMUST00000035058.10; ENSMUSP00000035058.6; ENSMUSG00000032482.10. [Q71M36-1]
DR   Ensembl; ENSMUST00000196060.5; ENSMUSP00000143164.2; ENSMUSG00000032482.10. [Q71M36-2]
DR   Ensembl; ENSMUST00000197850.5; ENSMUSP00000143005.2; ENSMUSG00000032482.10. [Q71M36-4]
DR   Ensembl; ENSMUST00000199736.2; ENSMUSP00000142845.2; ENSMUSG00000032482.10. [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   AGR; MGI:1352747; -.
DR   CTD; 10675; -.
DR   MGI; MGI:1352747; Cspg5.
DR   VEuPathDB; HostDB:ENSMUSG00000032482; -.
DR   eggNOG; ENOG502QXSB; Eukaryota.
DR   GeneTree; ENSGT00440000034270; -.
DR   InParanoid; Q71M36; -.
DR   OMA; WEPHAND; -.
DR   OrthoDB; 5322387at2759; -.
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 81 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 148 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA: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:0045211; C: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:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR   InterPro; IPR042382; CSPG5.
DR   InterPro; IPR010555; CSPG5_S_attach_dom.
DR   InterPro; IPR009505; Neural_ProG_Cyt.
DR   PANTHER; PTHR15381:SF1; CHONDROITIN SULFATE PROTEOGLYCAN 5; 1.
DR   PANTHER; PTHR15381; CHONDROITIN SULFATE PROTEOGLYCAN 5 -RELATED; 1.
DR   Pfam; PF06566; Chon_Sulph_att; 1.
DR   Pfam; PF06567; Neural_ProG_Cyt; 1.
DR   Genevisible; Q71M36; MM.
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; Secreted; Signal;
KW   Synapse; 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        38
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:O95196"
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;
FT                   AAF23362/AAQ04777/AAQ04778/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
//