CNTP1_MOUSE
ID CNTP1_MOUSE Reviewed; 1385 AA.
AC O54991; A2A4K6;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Contactin-associated protein 1;
DE Short=Caspr;
DE Short=Caspr1;
DE AltName: Full=MHDNIV;
DE AltName: Full=NCP1;
DE AltName: Full=Neurexin IV;
DE AltName: Full=Neurexin-4;
DE AltName: Full=Paranodin;
DE Flags: Precursor;
GN Name=Cntnap1; Synonyms=Nrxn4;
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], POSSIBLE FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11395000; DOI=10.1016/s0896-6273(01)00294-x;
RA Bhat M.A., Rios J.C., Lu Y., Garcia-Fresco G.P., Ching W., St Martin M.,
RA Li J., Einheber S., Chesler M., Rosenbluth J., Salzer J.L., Bellen H.J.;
RT "Axon-glia interactions and the domain organization of myelinated axons
RT requires neurexin IV/Caspr/Paranodin.";
RL Neuron 30:369-383(2001).
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 TISSUE SPECIFICITY.
RX PubMed=11512672; DOI=10.1007/s004410100403;
RA Arroyo E.J., Xu T., Poliak S., Watson M., Peles E., Scherer S.S.;
RT "Internodal specializations of myelinated axons in the central nervous
RT system.";
RL Cell Tissue Res. 305:53-66(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25378149; DOI=10.1523/jneurosci.3369-14.2014;
RA Gordon A., Adamsky K., Vainshtein A., Frechter S., Dupree J.L.,
RA Rosenbluth J., Peles E.;
RT "Caspr and caspr2 are required for both radial and longitudinal
RT organization of myelinated axons.";
RL J. Neurosci. 34:14820-14826(2014).
CC -!- FUNCTION: Required, with CNTNAP2, for radial and longitudinal
CC organization of myelinated axons (PubMed:25378149). Plays a role in the
CC formation of functional distinct domains critical for saltatory
CC conduction of nerve impulses in myelinated nerve fibers. Demarcates the
CC paranodal region of the axo-glial junction. In association with
CC contactin involved in the signaling between axons and myelinating glial
CC cells (PubMed:25378149, PubMed:11395000). {ECO:0000269|PubMed:11395000,
CC ECO:0000269|PubMed:25378149}.
CC -!- SUBUNIT: Interacts with CNTN1/contactin in cis form.
CC {ECO:0000250|UniProtKB:P97846}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, paranodal septate
CC junction {ECO:0000269|PubMed:25378149}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. In myelinated nerve fibers
CC predominantly found in paranodal axoglial junctions. In the internodal
CC region of myelinated axons in the CNS and the PNS also found as a thin
CC line apposing the inner mesaxon of the myelin sheath. In PNS neurons
CC this line forms a circumferential ring that apposes the innermost
CC aspect of Schmidt-Lanterman incisures. {ECO:0000269|PubMed:11512672,
CC ECO:0000269|PubMed:25378149}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit tremor, ataxia, and
CC significant motor paresis. Normal paranodal junctions fail to form, and
CC the organization of the paranodal loops is disrupted. Contactin is
CC undetectable in the paranodes, and potassium channels are displaced
CC from the juxtaparanodal into the paranodal domains. Also results in a
CC severe decrease in peripheral nerve conduction velocity
CC (PubMed:11395000, PubMed:25378149). Double mutants CNTNAP1 and CNTNAP2
CC have wider Ranvier nodes compared to wild-type littermates
CC (PubMed:25378149). {ECO:0000269|PubMed:11395000,
CC ECO:0000269|PubMed:25378149}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; AF039833; AAB96760.1; -; mRNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25455.1; -.
DR PIR; T14158; T14158.
DR RefSeq; NP_058062.2; NM_016782.2.
DR AlphaFoldDB; O54991; -.
DR SMR; O54991; -.
DR BioGRID; 207284; 15.
DR IntAct; O54991; 8.
DR MINT; O54991; -.
DR STRING; 10090.ENSMUSP00000099398; -.
DR GlyConnect; 2230; 11 N-Linked glycans (10 sites).
DR GlyGen; O54991; 17 sites, 9 N-linked glycans (10 sites).
DR iPTMnet; O54991; -.
DR PhosphoSitePlus; O54991; -.
DR SwissPalm; O54991; -.
DR MaxQB; O54991; -.
DR PaxDb; O54991; -.
DR PeptideAtlas; O54991; -.
DR PRIDE; O54991; -.
DR ProteomicsDB; 283588; -.
DR ABCD; O54991; 1 sequenced antibody.
DR Antibodypedia; 2336; 240 antibodies from 35 providers.
DR DNASU; 53321; -.
DR Ensembl; ENSMUST00000103109; ENSMUSP00000099398; ENSMUSG00000017167.
DR GeneID; 53321; -.
DR KEGG; mmu:53321; -.
DR UCSC; uc007lnt.1; mouse.
DR CTD; 8506; -.
DR MGI; MGI:1858201; Cntnap1.
DR VEuPathDB; HostDB:ENSMUSG00000017167; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000160825; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; O54991; -.
DR OMA; HCAHPRF; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; O54991; -.
DR TreeFam; TF321823; -.
DR BioGRID-ORCS; 53321; 3 hits in 72 CRISPR screens.
DR PRO; PR:O54991; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54991; protein.
DR Bgee; ENSMUSG00000017167; Expressed in superior frontal gyrus and 73 other tissues.
DR Genevisible; O54991; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0005918; C:septate junction; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0019227; P:neuronal action potential propagation; IMP:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; IMP:BHF-UCL.
DR GO; GO:1990227; P:paranodal junction maintenance; IMP:MGI.
DR GO; GO:0097106; P:postsynaptic density organization; IMP:MGI.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:UniProtKB.
DR GO; GO:0002175; P:protein localization to paranode region of axon; IMP:BHF-UCL.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR028872; Caspr1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF43; PTHR15036:SF43; 3.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 4.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3-binding; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1385
FT /note="Contactin-associated protein 1"
FT /id="PRO_0000019504"
FT TOPO_DOM 21..1284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1285..1305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1306..1385
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..169
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 204..356
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 390..539
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 545..577
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 577..796
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 814..958
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 962..996
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1089..1251
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1317..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1334..1370
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1333..1369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..169
FT /evidence="ECO:0000250"
FT DISULFID 324..356
FT /evidence="ECO:0000250"
FT DISULFID 507..539
FT /evidence="ECO:0000250"
FT DISULFID 545..556
FT /evidence="ECO:0000250"
FT DISULFID 550..565
FT /evidence="ECO:0000250"
FT DISULFID 567..577
FT /evidence="ECO:0000250"
FT DISULFID 931..958
FT /evidence="ECO:0000250"
FT DISULFID 962..975
FT /evidence="ECO:0000250"
FT DISULFID 969..984
FT /evidence="ECO:0000250"
FT DISULFID 986..996
FT /evidence="ECO:0000250"
FT DISULFID 1210..1251
FT /evidence="ECO:0000250"
FT CONFLICT 689
FT /note="G -> S (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134..1136
FT /note="LTT -> VTR (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1262
FT /note="P -> Q (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1313
FT /note="K -> Q (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1326
FT /note="D -> H (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1329
FT /note="P -> S (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
FT CONFLICT 1347
FT /note="T -> I (in Ref. 1; AAB96760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1385 AA; 156312 MW; B10BA6F150C27BA2 CRC64;
MMSLRLFSIL LATVVSGAWG WGYYGCNEEL VGPLYARSLG ASSYYGLFTT ARFARLHGIS
GWSPRIGDPN PWLQIDLMKK HRIRAVATQG AFNSWDWVTR YMLLYGDRVD SWTPFYQKGH
NATFFGNVND SAVVRHDLHY HFTARYIRIV PLAWNPRGKI GLRLGIYGCP YTSSILYFDG
DDAISYRFQR GASQSLWDVF AFSFKTEEKD GLLLHTEGSQ GDYVTLELQG AHLLLHMSLG
SSPIQPRPGH TTVSLGGVLN DLSWHYVRVD RYGRDANFTL DGYAHHFVLN GDFERLNLEN
EIFIGGLVGA ARKNLAYRHN FRGCIENVIY NRINIAEMAV MRHSRITFEG NVAFRCLDPV
PHPINFGGPH NFVQVPGFPR RGRLAVSFRF RTWDLTGLLL FSHLGDGLGH VELMLSEGQV
NVSIAQTGRK KLQFAAGYRL NDGFWHEVNF VAQENHAVIS IDDVEGAEVR VSYPLLIRTG
TSYFFGGCPK PASRWGCHSN QTAFHGCMEL LKVDGQLVNL TLVEFRKLGY FAEVLFDTCG
ITDRCSPNMC EHDGRCYQSW DDFICYCELT GYKGVTCHEP LYKESCEAYR LSGKYSGNYT
IDPDGSGPLK PFVVYCDIRE NRAWTVVRHD RLWTTRVTGS SMDRPFLGAI QYWNASWEEV
SALANASQHC EQWIEFSCYN SRLLNTAGGY PYSFWIGRNE EQHFYWGGSQ PGIQRCACGL
DQSCVDPALH CNCDADQPQW RTDKGLLTFV DHLPVTQVVV GDTNRSNSEA QFFLRPLRCY
GDRNSWNTIS FHTGAALRFP PIRANHSLDV SFYFRTSAPS GVFLENMGGP FCRWRRPYVR
VELNTSRDVV FAFDIGNGDE NLTVHSDDFE FNDDEWHLVR AEINVKQARL RVDHRPWVLR
PMPLQTYIWL VYDQPLYVGS AELKRRPFVG CLRAMRLNGV TLNLEGRANA SEGTFPNCTG
HCTHPRFPCF HGGRCVERYS YYTCDCDLTA FDGPYCNHDI GGFFETGTWM RYNLQSALRS
AAREFSHMLS RPVPGYEPGY VPGYDTPGYV PGYHGPGYRL PEYPRPGRPV PGYRGPVYNV
TGEEVSFSFS TNSAPAVLLY VSSFVRDYMA VLIKEDGTLQ LRYQLGTSPY VYQLTTRPVT
DGQPHSVNIT RVYRNLFIQV DYFPLTEQKF SLLVDSQLDS PKALYLGRVM ETGVIDPEIQ
RYNTPGFSGC LSGVRFNNVA PLKTHFRTPR PMTAELAEAM RVQGELSESN CGAMPRLVSE
VPPELDPWYL PPDFPYYHDD GWIAILLGFL VAFLLLGLVG MLVLFYLQNH RYKGSYHTNE
PKATHDSHPG GKAPLPPSGP AQAPAPTPAP TQLPTPAPAP APAPASGPGP RDQNLPQILE
ESRSE
