NFASC_MOUSE
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 03-AUG-2022, entry version 160.
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; 8.
DR DIP; DIP-31976N; -.
DR IntAct; Q810U3; 4.
DR STRING; 10090.ENSMUSP00000092148; -.
DR GlyGen; Q810U3; 10 sites, 26 N-linked glycans (9 sites).
DR iPTMnet; Q810U3; -.
DR PhosphoSitePlus; Q810U3; -.
DR SwissPalm; Q810U3; -.
DR jPOST; Q810U3; -.
DR MaxQB; Q810U3; -.
DR PaxDb; Q810U3; -.
DR PeptideAtlas; Q810U3; -.
DR PRIDE; Q810U3; -.
DR ProteomicsDB; 293538; -.
DR Antibodypedia; 2194; 227 antibodies from 35 providers.
DR DNASU; 269116; -.
DR Ensembl; ENSMUST00000094569; ENSMUSP00000092148; ENSMUSG00000026442.
DR GeneID; 269116; -.
DR KEGG; mmu:269116; -.
DR UCSC; uc007cpe.2; mouse.
DR CTD; 23114; -.
DR MGI; MGI:104753; Nfasc.
DR VEuPathDB; HostDB:ENSMUSG00000026442; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000157024; -.
DR InParanoid; Q810U3; -.
DR OrthoDB; 434404at2759; -.
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 73 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 135 other tissues.
DR ExpressionAtlas; Q810U3; baseline and differential.
DR Genevisible; Q810U3; MM.
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:0005887; C:integral component of plasma membrane; 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:0007422; P:peripheral nervous system development; IEA:InterPro.
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 Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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.
DR PANTHER; PTHR10075; PTHR10075; 2.
DR PANTHER; PTHR10075:SF35; PTHR10075:SF35; 2.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
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
