ID   NFASC_MOUSE             Reviewed;        1240 AA.
AC   Q810U3;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Neurofascin;
DE   Flags: Precursor;
GN   Name=Nfasc;
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].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Dirks P., Montag-Sallaz M., Montag D.;
RT   "Expression patterns of L1-family cell recognition molecules L1, CHL1,
RT   NrCAM, and neurofascin in the mouse brain.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 96-104; 243-260; 335-355; 387-396; 493-509; 573-585;
RP   633-642; 681-719; 810-829 AND 1057-1076, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1226; SER-1227 AND
RP   SER-1231, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Pancreas;
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).
RN   [4]
RP   INTERACTION WITH MYOC.
RX   PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA   Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA   Tomarev S.I.;
RT   "Myocilin mediates myelination in the peripheral nervous system through
RT   ErbB2/3 signaling.";
RL   J. Biol. Chem. 288:26357-26371(2013).
CC   -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved
CC       in neurite extension, axonal guidance, synaptogenesis, myelination and
CC       neuron-glial cell interactions. {ECO:0000250}.
CC   -!- SUBUNIT: Horseshoe-shaped homodimer. Probable constituent of a
CC       NFASC/NRCAM/ankyrin-G complex. Associates with the sodium channel beta-
CC       1 (SCN1B) and beta-3 (SCN3B) subunits. Interacts with GLDN/gliomedin
CC       (By similarity). Interacts with MYOC. {ECO:0000250,
CC       ECO:0000269|PubMed:23897819}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: Homophilic adhesion is primarily mediated by the interaction of
CC       the second Ig-like domains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family. {ECO:0000305}.
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DR   EMBL; AJ543322; CAD65849.1; -; mRNA.
DR   CCDS; CCDS35707.1; -.
DR   RefSeq; NP_874385.1; NM_182716.4.
DR   AlphaFoldDB; Q810U3; -.
DR   SMR; Q810U3; -.
DR   BioGRID; 234609; 10.
DR   DIP; DIP-31976N; -.
DR   IntAct; Q810U3; 4.
DR   STRING; 10090.ENSMUSP00000092148; -.
DR   GlyCosmos; Q810U3; 10 sites, 26 glycans.
DR   GlyGen; Q810U3; 11 sites, 26 N-linked glycans (9 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q810U3; -.
DR   PhosphoSitePlus; Q810U3; -.
DR   SwissPalm; Q810U3; -.
DR   jPOST; Q810U3; -.
DR   MaxQB; Q810U3; -.
DR   PaxDb; 10090-ENSMUSP00000092148; -.
DR   PeptideAtlas; Q810U3; -.
DR   ProteomicsDB; 293538; -.
DR   Antibodypedia; 2194; 262 antibodies from 35 providers.
DR   DNASU; 269116; -.
DR   Ensembl; ENSMUST00000094569.11; ENSMUSP00000092148.5; ENSMUSG00000026442.15.
DR   GeneID; 269116; -.
DR   KEGG; mmu:269116; -.
DR   UCSC; uc007cpe.2; mouse.
DR   AGR; MGI:104753; -.
DR   CTD; 23114; -.
DR   MGI; MGI:104753; Nfasc.
DR   VEuPathDB; HostDB:ENSMUSG00000026442; -.
DR   eggNOG; KOG3513; Eukaryota.
DR   GeneTree; ENSGT00940000157024; -.
DR   InParanoid; Q810U3; -.
DR   OrthoDB; 2912783at2759; -.
DR   PhylomeDB; Q810U3; -.
DR   TreeFam; TF351098; -.
DR   Reactome; R-MMU-447043; Neurofascin interactions.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 269116; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Nfasc; mouse.
DR   PRO; PR:Q810U3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q810U3; Protein.
DR   Bgee; ENSMUSG00000026442; Expressed in retinal neural layer and 137 other cell types or tissues.
DR   ExpressionAtlas; Q810U3; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0033268; C:node of Ranvier; IDA:UniProtKB.
DR   GO; GO:0033010; C:paranodal junction; IDA:UniProtKB.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0097454; C:Schwann cell microvillus; ISO:MGI.
DR   GO; GO:0005918; C:septate junction; IDA:MGI.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR   GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IGI:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:MGI.
DR   GO; GO:0030913; P:paranodal junction assembly; IMP:UniProtKB.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:MGI.
DR   GO; GO:0002175; P:protein localization to paranode region of axon; IMP:MGI.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR   CDD; cd00063; FN3; 4.
DR   CDD; cd05731; Ig3_L1-CAM_like; 1.
DR   CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR   CDD; cd05875; IgI_hNeurofascin_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR   InterPro; IPR026965; NFASC_Ig-like.
DR   PANTHER; PTHR44170:SF12; NEUROFASCIN; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF13882; Bravo_FIGEY; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   Genevisible; Q810U3; MM.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1240
FT                   /note="Neurofascin"
FT                   /id="PRO_0000015050"
FT   TOPO_DOM        25..1110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1111..1131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1132..1240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          41..137
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          143..230
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          244..332
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          337..424
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          430..517
FT                   /note="Ig-like C2-type 5"
FT   DOMAIN          521..603
FT                   /note="Ig-like C2-type 6"
FT   DOMAIN          630..725
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          727..823
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          827..923
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1007..1099
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          710..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1211..1225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         481
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O94856"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94856"
FT   MOD_RES         1160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97685"
FT   MOD_RES         1187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97685"
FT   MOD_RES         1190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97685"
FT   MOD_RES         1226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        446
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        752
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        778
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        866
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        881
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        162..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        268..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        358..408
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        452..501
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        543..592
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   1240 AA;  137975 MW;  6DE8935B5B02E965 CRC64;
     MARQQAPPWV HIALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD HIVDPRDNIL
     IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA
     RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM
     EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA
     ERTPSFMYPQ GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSN KAKFENFNKA
     LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA
     NGNPKPTVQW MVNGEPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN
     AFVSVLDVPP RMLSARNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV
     YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ
     LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ
     DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD
     YVVQFEEDQF QPGVWHDHSR FPGSVNSAVL HLSPYVNYQF RVIAVNEVGS SHPSLPSERY
     RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT
     VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPDTIIGYS GEDLPSAPRR FRVRQPNLET
     INLEWDHPEH PNGILIGYIL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL
     SARTQVGSGE AATEESPAPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA LAATSEATTV
     PIIPTVVPTT VATTIATTTT TTAATTTTTT TESPPTTTAG TKIHETAPDE QSIWNVTVLP
     NSKWANITWK HNFRPGTDFV VEYIDSNHTK KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR
     DNEGISSTVI TFMTSTAYTN NQADIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP
     VREKKDVPLG PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG
     QFNEDGSFIG QYTVKKDKEE TEGNESSEAT SPVNAIYSLA
//