CCN3_MOUSE
ID CCN3_MOUSE Reviewed; 354 AA.
AC Q64299; Q8CA67;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=CCN family member 3 {ECO:0000305};
DE AltName: Full=Cellular communication network factor 3 {ECO:0000250|UniProtKB:P48745};
DE AltName: Full=Nephroblastoma-overexpressed gene protein homolog;
DE AltName: Full=Protein NOV homolog;
DE Short=NovH;
DE Flags: Precursor;
GN Name=Ccn3; Synonyms=Nov {ECO:0000312|MGI:MGI:109185};
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and ICR; TISSUE=Brain;
RX PubMed=8975721; DOI=10.1006/geno.1996.0647;
RA Snaith M.R., Natarajan D., Taylor L.B., Choi C.P., Martinerie C.,
RA Perbal B., Schofield P.N., Boulter C.A.;
RT "Genomic structure and chromosomal mapping of the mouse nov gene.";
RL Genomics 38:425-428(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=8622864;
RA Martinerie C., Chevalier G., Rauscher F.J. III, Perbal B.;
RT "Regulation of nov by WT1: a potential role for nov in nephrogenesis.";
RL Oncogene 12:1479-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Spinal cord;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP INTERACTION WITH NOTCH1.
RX PubMed=12050162; DOI=10.1074/jbc.m203727200;
RA Sakamoto K., Yamaguchi S., Ando R., Miyawaki A., Kabasawa Y., Takagi M.,
RA Li C.L., Perbal B., Katsube K.;
RT "The nephroblastoma overexpressed gene (NOV/ccn3) protein associates with
RT Notch1 extracellular domain and inhibits myoblast differentiation via Notch
RT signaling pathway.";
RL J. Biol. Chem. 277:29399-29405(2002).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15213231; DOI=10.1074/jbc.m403952200;
RA Fu C.T., Bechberger J.F., Ozog M.A., Perbal B., Naus C.C.;
RT "CCN3 (NOV) interacts with connexin43 in C6 glioma cells: possible
RT mechanism of connexin-mediated growth suppression.";
RL J. Biol. Chem. 279:36943-36950(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15611078; DOI=10.1074/jbc.m404903200;
RA Lin C.G., Chen C.C., Leu S.J., Grzeszkiewicz T.M., Lau L.F.;
RT "Integrin-dependent functions of the angiogenic inducer NOV (CCN3):
RT implication in wound healing.";
RL J. Biol. Chem. 280:8229-8237(2005).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20139355; DOI=10.1161/atvbaha.110.203356;
RA Shimoyama T., Hiraoka S., Takemoto M., Koshizaka M., Tokuyama H.,
RA Tokuyama T., Watanabe A., Fujimoto M., Kawamura H., Sato S., Tsurutani Y.,
RA Saito Y., Perbal B., Koseki H., Yokote K.;
RT "CCN3 inhibits neointimal hyperplasia through modulation of smooth muscle
RT cell growth and migration.";
RL Arterioscler. Thromb. Vasc. Biol. 30:675-682(2010).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=21063504; DOI=10.1007/s12079-010-0095-x;
RA Lin Z., Natesan V., Shi H., Hamik A., Kawanami D., Hao C.,
RA Mahabaleshwar G.H., Wang W., Jin Z.G., Atkins G.B., Firth S.M., Rittie L.,
RA Perbal B., Jain M.K.;
RT "A novel role of CCN3 in regulating endothelial inflammation.";
RL J. Cell Commun. Signal. 4:141-153(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=23653360; DOI=10.1074/jbc.m113.454652;
RA Matsushita Y., Sakamoto K., Tamamura Y., Shibata Y., Minamizato T.,
RA Kihara T., Ito M., Katsube K., Hiraoka S., Koseki H., Harada K.,
RA Yamaguchi A.;
RT "CCN3 protein participates in bone regeneration as an inhibitory factor.";
RL J. Biol. Chem. 288:19973-19985(2013).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23705021; DOI=10.1371/journal.pone.0064957;
RA Paradis R., Lazar N., Antinozzi P., Perbal B., Buteau J.;
RT "Nov/Ccn3, a novel transcriptional target of FoxO1, impairs pancreatic
RT beta-cell function.";
RL PLoS ONE 8:E64957-E64957(2013).
RN [12]
RP INDUCTION BY ATHEROSCLEROSIS.
RX PubMed=24722330; DOI=10.1371/journal.pone.0094912;
RA Liu J., Ren Y., Kang L., Zhang L.;
RT "Overexpression of CCN3 inhibits inflammation and progression of
RT atherosclerosis in apolipoprotein E-deficient mice.";
RL PLoS ONE 9:E94912-E94912(2014).
RN [13]
RP INTERACTION WITH ZDHHC22, SUBCELLULAR LOCATION, PROBABLE PALMITOYLATION AT
RP CYS-241, AND MUTAGENESIS OF ASN-227; ASN-229; CYS-241 AND CYS-246.
RX PubMed=29287726; DOI=10.1016/j.bbrc.2017.12.128;
RA Kim Y., Yang H., Min J.K., Park Y.J., Jeong S.H., Jang S.W., Shim S.;
RT "CCN3 secretion is regulated by palmitoylation via ZDHHC22.";
RL Biochem. Biophys. Res. Commun. 495:2573-2578(2018).
CC -!- FUNCTION: Immediate-early protein playing a role in various cellular
CC processes including proliferation, adhesion, migration, differentiation
CC and survival. Acts by binding to integrins or membrane receptors such
CC as NOTCH1. Essential regulator of hematopoietic stem and progenitor
CC cell function. Inhibits myogenic differentiation through the activation
CC of Notch-signaling pathway. Inhibits vascular smooth muscle cells
CC proliferation by increasing expression of cell-cycle regulators such as
CC CDKN2B or CDKN1A independently of TGFB1 signaling. Ligand of integrins
CC ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to
CC stimulate pro-angiogenic activities and induces angiogenesis. In
CC endothelial cells, supports cell adhesion, induces directed cell
CC migration (chemotaxis) and promotes cell survival. Also plays a role in
CC cutaneous wound healing acting as integrin receptor ligand. Supports
CC skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and
CC induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance
CC bFGF-induced DNA synthesis in fibroblasts (By similarity). Involved in
CC bone regeneration as a negative regulator (PubMed:23653360). Enhances
CC the articular chondrocytic phenotype, whereas it repressed the one
CC representing endochondral ossification (By similarity). Impairs
CC pancreatic beta-cell function, inhibits beta-cell proliferation and
CC insulin secretion (PubMed:23705021). Plays a role as negative regulator
CC of endothelial pro-inflammatory activation reducing monocyte adhesion,
CC its anti-inflammatory effects occur secondary to the inhibition of NF-
CC kappaB signaling pathway (By similarity). Contributes to the control
CC and coordination of inflammatory processes in atherosclerosis
CC (PubMed:24722330). Attenuates inflammatory pain through regulation of
CC IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9
CC expression through ITGB1 engagement (By similarity).
CC {ECO:0000250|UniProtKB:P48745, ECO:0000250|UniProtKB:Q9QZQ5,
CC ECO:0000269|PubMed:23653360, ECO:0000269|PubMed:23705021,
CC ECO:0000269|PubMed:24722330}.
CC -!- SUBUNIT: Interacts with FBLN1. Interacts (via CTCK domain) with NOTCH1
CC (via the EGF-like repeat region). Interacts with GJA1/CX43. Interacts
CC with ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB5. Interacts with ZDHHC22;
CC the interaction may lead to CCN3 palmitoylation (PubMed:29287726).
CC {ECO:0000250|UniProtKB:P48745, ECO:0000269|PubMed:29287726}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23705021,
CC ECO:0000269|PubMed:29287726}. Cytoplasm {ECO:0000250|UniProtKB:P48745}.
CC Cell junction, gap junction {ECO:0000250|UniProtKB:P48745}.
CC Note=Localizes at the gap junction in presence of GJA1.
CC {ECO:0000250|UniProtKB:Q9QZQ5}.
CC -!- TISSUE SPECIFICITY: Expressed in large vessels including the ascending
CC aorta, carotid arteries, and the thoracic aorta, in medium-sized
CC vessels such as coronary arteries and small pulmonary veins and also in
CC small vessels. In addition, also found to be present in the heart (at
CC protein level) (PubMed:21063504). Expressed in astrocytes (at protein
CC level) (PubMed:15213231). Detected in brain, bone, lung and muscle
CC tissues (PubMed:20139355, PubMed:23653360). Expressed in skin,
CC expression highly increases 5 days post-wounding, peaking on the 7th
CC day to decline after 9 days (PubMed:15611078). Expressed in pancreatic
CC ducts and beta-cell islets (PubMed:23705021).
CC {ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:15611078,
CC ECO:0000269|PubMed:20139355, ECO:0000269|PubMed:21063504,
CC ECO:0000269|PubMed:23653360, ECO:0000269|PubMed:23705021}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in the early phase of bone
CC regeneration. {ECO:0000269|PubMed:23653360}.
CC -!- INDUCTION: Expression is reduced in atherosclerosis progression.
CC {ECO:0000269|PubMed:24722330}.
CC -!- PTM: May be palmitoylated on Cys-241, which is important for
CC extracellular secretion. {ECO:0000269|PubMed:29287726}.
CC -!- DISRUPTION PHENOTYPE: Mutants develop normally but have enhanced
CC arterial neointimal hyperplasia in response to injury
CC (PubMed:20139355). Animals show an accelerated bone regeneration
CC comparing to in wild-type mice (PubMed:24722330).
CC {ECO:0000269|PubMed:20139355, ECO:0000269|PubMed:24722330}.
CC -!- SIMILARITY: Belongs to the CCN family. {ECO:0000305}.
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DR EMBL; X97863; CAA66457.1; -; Genomic_DNA.
DR EMBL; Y09257; CAA70454.1; -; mRNA.
DR EMBL; X96585; CAA65404.1; -; mRNA.
DR EMBL; AK039481; BAC30363.1; -; mRNA.
DR EMBL; AK081944; BAC38378.1; -; mRNA.
DR EMBL; BC003774; AAH03774.1; -; mRNA.
DR CCDS; CCDS27471.1; -.
DR RefSeq; NP_035060.1; NM_010930.4.
DR AlphaFoldDB; Q64299; -.
DR SMR; Q64299; -.
DR BioGRID; 201813; 1.
DR STRING; 10090.ENSMUSP00000054389; -.
DR GlyConnect; 2635; 3 N-Linked glycans (1 site).
DR GlyGen; Q64299; 2 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q64299; -.
DR EPD; Q64299; -.
DR jPOST; Q64299; -.
DR MaxQB; Q64299; -.
DR PaxDb; Q64299; -.
DR PeptideAtlas; Q64299; -.
DR PRIDE; Q64299; -.
DR ProteomicsDB; 293709; -.
DR Antibodypedia; 13650; 394 antibodies from 36 providers.
DR DNASU; 18133; -.
DR Ensembl; ENSMUST00000050027; ENSMUSP00000054389; ENSMUSG00000037362.
DR GeneID; 18133; -.
DR KEGG; mmu:18133; -.
DR UCSC; uc007vrn.1; mouse.
DR CTD; 4856; -.
DR MGI; MGI:109185; Ccn3.
DR VEuPathDB; HostDB:ENSMUSG00000037362; -.
DR eggNOG; ENOG502QR9V; Eukaryota.
DR GeneTree; ENSGT00940000159963; -.
DR HOGENOM; CLU_063247_1_0_1; -.
DR InParanoid; Q64299; -.
DR OMA; CHTNCPQ; -.
DR OrthoDB; 999958at2759; -.
DR PhylomeDB; Q64299; -.
DR TreeFam; TF326070; -.
DR BioGRID-ORCS; 18133; 5 hits in 72 CRISPR screens.
DR PRO; PR:Q64299; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q64299; protein.
DR Bgee; ENSMUSG00000037362; Expressed in aorta tunica media and 198 other tissues.
DR Genevisible; Q64299; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0005112; F:Notch binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:1990523; P:bone regeneration; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0071603; P:endothelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; ISS:UniProtKB.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:UniProtKB.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1904057; P:negative regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IMP:UniProtKB.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0014909; P:smooth muscle cell migration; ISS:UniProtKB.
DR GO; GO:0048659; P:smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IDA:UniProtKB.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR006208; Glyco_hormone_CN.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR012395; IGFBP_CNN.
DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR InterPro; IPR043973; TSP1_CCN.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF00007; Cys_knot; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF19035; TSP1_CCN; 1.
DR Pfam; PF00093; VWC; 1.
DR PIRSF; PIRSF036495; IGFBP_rP_CNN; 1.
DR SMART; SM00041; CT; 1.
DR SMART; SM00121; IB; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00214; VWC; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS00222; IGFBP_N_1; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cytoplasm; Disulfide bond; Gap junction; Glycoprotein;
KW Growth factor; Lipoprotein; Palmitate; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..354
FT /note="CCN family member 3"
FT /id="PRO_0000014416"
FT DOMAIN 25..99
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 102..168
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 202..247
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 261..335
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT LIPID 241
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:29287726"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 261..298
FT /evidence="ECO:0000250"
FT DISULFID 278..312
FT /evidence="ECO:0000250"
FT DISULFID 289..328
FT /evidence="ECO:0000250"
FT DISULFID 292..330
FT /evidence="ECO:0000250"
FT DISULFID 297..334
FT /evidence="ECO:0000250"
FT MUTAGEN 227
FT /note="N->Q: No effect on extracellular secretion."
FT /evidence="ECO:0000269|PubMed:29287726"
FT MUTAGEN 229
FT /note="N->Q: No effect on extracellular secretion."
FT /evidence="ECO:0000269|PubMed:29287726"
FT MUTAGEN 241
FT /note="C->A: Abolishes extracellular secretion. Inhibits
FT axonal growth of callosal projections when overexpressed."
FT /evidence="ECO:0000269|PubMed:29287726"
FT MUTAGEN 246
FT /note="C->A: Reduces extracellular secretion. No
FT significant effect on axonal growth of callosal projections
FT when overexpressed."
FT /evidence="ECO:0000269|PubMed:29287726"
FT CONFLICT 6
FT /note="R -> G (in Ref. 3; BAC30363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38928 MW; 08ECE8CFC67829DE CRC64;
MSLFLRKRCL CLGFLLFHLL SQVSASLRCP SRCPPKCPSI SPTCAPGVRS VLDGCSCCPV
CARQRGESCS EMRPCDQSSG LYCDRSADPN NQTGICMVPE GDNCVFDGVI YRNGEKFEPN
CQYFCTCRDG QIGCLPRCQL DVLLPGPDCP APRKVAVPGE CCEKWTCGSD EQGTQGTLGG
LALPAYRPEA TVGVEVSDSS INCIEQTTEW SACSKSCGMG VSTRVTNRNR QCEMVKQTRL
CIVRPCEQEP EEVTDKKGKK CLRTKKSLKA IHLQFENCTS LYTYKPRFCG VCSDGRCCTP
HNTKTIQVEF QCLPGEIIKK PVMVIGTCTC YSNCPQNNEA FLQDLELKTS RGEI
