Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Contactin-associated protein 1

Gene

Cntnap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Seems to play a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Seems to demarcate the paranodal region of the axo-glial junction. In association with contactin may have a role in the signaling between axons and myelinating glial cells. Mice that lack CNTAP1 exhibit tremor, ataxia, and significant motor paresis. Normal paranodal junctions fail to form, and the organization of the paranodal loops is disrupted. Contactin is undetectable in the paranodes, and potassium channels are displaced from the juxtaparanodal into the paranodal domains. Also results in a severe decrease in peripheral nerve conduction velocity.

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cytoskeleton organization Source: BHF-UCL
  • neuromuscular process controlling balance Source: BHF-UCL
  • neuromuscular process controlling posture Source: BHF-UCL
  • neuronal action potential propagation Source: BHF-UCL
  • neuron projection development Source: MGI
  • neuron projection morphogenesis Source: BHF-UCL
  • paranodal junction assembly Source: BHF-UCL
  • protein localization to paranode region of axon Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Contactin-associated protein 1
Short name:
Caspr
Short name:
Caspr1
Alternative name(s):
MHDNIV
NCP1
Neurexin IV
Neurexin-4
Paranodin
Gene namesi
Name:Cntnap1
Synonyms:Nrxn4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1858201. Cntnap1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 12841264ExtracellularSequence analysisAdd
BLAST
Transmembranei1285 – 130521HelicalSequence analysisAdd
BLAST
Topological domaini1306 – 138580CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: BHF-UCL
  • myelin sheath Source: UniProtKB
  • paranode region of axon Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 13851365Contactin-associated protein 1PRO_0000019504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 169By similarity
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence analysis
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi324 ↔ 356By similarity
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence analysis
Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence analysis
Disulfide bondi507 ↔ 539By similarity
Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi545 ↔ 556By similarity
Disulfide bondi550 ↔ 565By similarity
Disulfide bondi567 ↔ 577By similarity
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence analysis
Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence analysis
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence analysis
Glycosylationi764 – 7641N-linked (GlcNAc...)Sequence analysis
Glycosylationi805 – 8051N-linked (GlcNAc...)Sequence analysis
Glycosylationi844 – 8441N-linked (GlcNAc...)Sequence analysis
Glycosylationi861 – 8611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi931 ↔ 958By similarity
Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence analysis
Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi962 ↔ 975By similarity
Disulfide bondi969 ↔ 984By similarity
Disulfide bondi986 ↔ 996By similarity
Glycosylationi1079 – 10791N-linked (GlcNAc...)Sequence analysis
Glycosylationi1148 – 11481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1210 ↔ 1251By similarity
Modified residuei1384 – 13841PhosphoserineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO54991.
PaxDbiO54991.
PRIDEiO54991.

PTM databases

iPTMnetiO54991.
PhosphoSiteiO54991.
SwissPalmiO54991.

Expressioni

Tissue specificityi

Expressed in brain. In myelinated nerve fibers predominantly found in paranodal axoglial junctions. In the internodal region of myelinated axons in the CNS and the PNS also found as a thin line apposing the inner mesaxon of the myelin sheath. In PNS neurons this line forms a circumferential ring that apposes the innermost aspect of Schmidt-Lanterman incisures.1 Publication

Gene expression databases

BgeeiO54991.
CleanExiMM_CNTNAP1.
GenevisibleiO54991. MM.

Interactioni

Subunit structurei

Interacts with contactin in cis form.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiO54991. 2 interactions.
MINTiMINT-4091273.
STRINGi10090.ENSMUSP00000099398.

Structurei

3D structure databases

ProteinModelPortaliO54991.
SMRiO54991. Positions 41-580, 787-1026, 1058-1262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 169144F5/8 type CPROSITE-ProRule annotationAdd
BLAST
Domaini204 – 356153Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini390 – 539150Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini545 – 57733EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini577 – 796220Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini814 – 958145Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini962 – 99635EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini1089 – 1251163Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1334 – 137037SH3-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the neurexin family.Curated
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation
Contains 4 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3516. Eukaryota.
ENOG410XPHG. LUCA.
GeneTreeiENSGT00760000118991.
HOGENOMiHOG000230964.
HOVERGENiHBG057718.
InParanoidiO54991.
KOiK07379.
OMAiRHDLHYH.
OrthoDBiEOG7GXP9N.
TreeFamiTF321823.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 1 hit.
3.90.215.10. 1 hit.
InterProiIPR028872. Caspr1.
IPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000421. FA58C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR008979. Galactose-bd-like.
IPR001791. Laminin_G.
IPR003585. Neurexin-like.
[Graphical view]
PANTHERiPTHR10127:SF4. PTHR10127:SF4. 2 hits.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF02210. Laminin_G_2. 4 hits.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
SM00231. FA58C. 1 hit.
SM00282. LamG. 4 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS50026. EGF_3. 2 hits.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50025. LAM_G_DOMAIN. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSLRLFSIL LATVVSGAWG WGYYGCNEEL VGPLYARSLG ASSYYGLFTT
60 70 80 90 100
ARFARLHGIS GWSPRIGDPN PWLQIDLMKK HRIRAVATQG AFNSWDWVTR
110 120 130 140 150
YMLLYGDRVD SWTPFYQKGH NATFFGNVND SAVVRHDLHY HFTARYIRIV
160 170 180 190 200
PLAWNPRGKI GLRLGIYGCP YTSSILYFDG DDAISYRFQR GASQSLWDVF
210 220 230 240 250
AFSFKTEEKD GLLLHTEGSQ GDYVTLELQG AHLLLHMSLG SSPIQPRPGH
260 270 280 290 300
TTVSLGGVLN DLSWHYVRVD RYGRDANFTL DGYAHHFVLN GDFERLNLEN
310 320 330 340 350
EIFIGGLVGA ARKNLAYRHN FRGCIENVIY NRINIAEMAV MRHSRITFEG
360 370 380 390 400
NVAFRCLDPV PHPINFGGPH NFVQVPGFPR RGRLAVSFRF RTWDLTGLLL
410 420 430 440 450
FSHLGDGLGH VELMLSEGQV NVSIAQTGRK KLQFAAGYRL NDGFWHEVNF
460 470 480 490 500
VAQENHAVIS IDDVEGAEVR VSYPLLIRTG TSYFFGGCPK PASRWGCHSN
510 520 530 540 550
QTAFHGCMEL LKVDGQLVNL TLVEFRKLGY FAEVLFDTCG ITDRCSPNMC
560 570 580 590 600
EHDGRCYQSW DDFICYCELT GYKGVTCHEP LYKESCEAYR LSGKYSGNYT
610 620 630 640 650
IDPDGSGPLK PFVVYCDIRE NRAWTVVRHD RLWTTRVTGS SMDRPFLGAI
660 670 680 690 700
QYWNASWEEV SALANASQHC EQWIEFSCYN SRLLNTAGGY PYSFWIGRNE
710 720 730 740 750
EQHFYWGGSQ PGIQRCACGL DQSCVDPALH CNCDADQPQW RTDKGLLTFV
760 770 780 790 800
DHLPVTQVVV GDTNRSNSEA QFFLRPLRCY GDRNSWNTIS FHTGAALRFP
810 820 830 840 850
PIRANHSLDV SFYFRTSAPS GVFLENMGGP FCRWRRPYVR VELNTSRDVV
860 870 880 890 900
FAFDIGNGDE NLTVHSDDFE FNDDEWHLVR AEINVKQARL RVDHRPWVLR
910 920 930 940 950
PMPLQTYIWL VYDQPLYVGS AELKRRPFVG CLRAMRLNGV TLNLEGRANA
960 970 980 990 1000
SEGTFPNCTG HCTHPRFPCF HGGRCVERYS YYTCDCDLTA FDGPYCNHDI
1010 1020 1030 1040 1050
GGFFETGTWM RYNLQSALRS AAREFSHMLS RPVPGYEPGY VPGYDTPGYV
1060 1070 1080 1090 1100
PGYHGPGYRL PEYPRPGRPV PGYRGPVYNV TGEEVSFSFS TNSAPAVLLY
1110 1120 1130 1140 1150
VSSFVRDYMA VLIKEDGTLQ LRYQLGTSPY VYQLTTRPVT DGQPHSVNIT
1160 1170 1180 1190 1200
RVYRNLFIQV DYFPLTEQKF SLLVDSQLDS PKALYLGRVM ETGVIDPEIQ
1210 1220 1230 1240 1250
RYNTPGFSGC LSGVRFNNVA PLKTHFRTPR PMTAELAEAM RVQGELSESN
1260 1270 1280 1290 1300
CGAMPRLVSE VPPELDPWYL PPDFPYYHDD GWIAILLGFL VAFLLLGLVG
1310 1320 1330 1340 1350
MLVLFYLQNH RYKGSYHTNE PKATHDSHPG GKAPLPPSGP AQAPAPTPAP
1360 1370 1380
TQLPTPAPAP APAPASGPGP RDQNLPQILE ESRSE
Length:1,385
Mass (Da):156,312
Last modified:July 27, 2011 - v2
Checksum:iB10BA6F150C27BA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti689 – 6891G → S in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1134 – 11363LTT → VTR in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1262 – 12621P → Q in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1313 – 13131K → Q in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1326 – 13261D → H in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1329 – 13291P → S in AAB96760 (PubMed:11395000).Curated
Sequence conflicti1347 – 13471T → I in AAB96760 (PubMed:11395000).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039833 mRNA. Translation: AAB96760.1.
AL590969 Genomic DNA. Translation: CAM19571.1.
CCDSiCCDS25455.1.
PIRiT14158.
RefSeqiNP_058062.2. NM_016782.2.
UniGeneiMm.474527.

Genome annotation databases

EnsembliENSMUST00000103109; ENSMUSP00000099398; ENSMUSG00000017167.
GeneIDi53321.
KEGGimmu:53321.
UCSCiuc007lnt.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039833 mRNA. Translation: AAB96760.1.
AL590969 Genomic DNA. Translation: CAM19571.1.
CCDSiCCDS25455.1.
PIRiT14158.
RefSeqiNP_058062.2. NM_016782.2.
UniGeneiMm.474527.

3D structure databases

ProteinModelPortaliO54991.
SMRiO54991. Positions 41-580, 787-1026, 1058-1262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO54991. 2 interactions.
MINTiMINT-4091273.
STRINGi10090.ENSMUSP00000099398.

PTM databases

iPTMnetiO54991.
PhosphoSiteiO54991.
SwissPalmiO54991.

Proteomic databases

MaxQBiO54991.
PaxDbiO54991.
PRIDEiO54991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103109; ENSMUSP00000099398; ENSMUSG00000017167.
GeneIDi53321.
KEGGimmu:53321.
UCSCiuc007lnt.1. mouse.

Organism-specific databases

CTDi8506.
MGIiMGI:1858201. Cntnap1.

Phylogenomic databases

eggNOGiKOG3516. Eukaryota.
ENOG410XPHG. LUCA.
GeneTreeiENSGT00760000118991.
HOGENOMiHOG000230964.
HOVERGENiHBG057718.
InParanoidiO54991.
KOiK07379.
OMAiRHDLHYH.
OrthoDBiEOG7GXP9N.
TreeFamiTF321823.

Miscellaneous databases

NextBioi310125.
PROiO54991.
SOURCEiSearch...

Gene expression databases

BgeeiO54991.
CleanExiMM_CNTNAP1.
GenevisibleiO54991. MM.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 1 hit.
3.90.215.10. 1 hit.
InterProiIPR028872. Caspr1.
IPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000421. FA58C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR008979. Galactose-bd-like.
IPR001791. Laminin_G.
IPR003585. Neurexin-like.
[Graphical view]
PANTHERiPTHR10127:SF4. PTHR10127:SF4. 2 hits.
PfamiPF00754. F5_F8_type_C. 1 hit.
PF02210. Laminin_G_2. 4 hits.
[Graphical view]
SMARTiSM00294. 4.1m. 1 hit.
SM00231. FA58C. 1 hit.
SM00282. LamG. 4 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEiPS50026. EGF_3. 2 hits.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50025. LAM_G_DOMAIN. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Axon-glia interactions and the domain organization of myelinated axons requires neurexin IV/Caspr/Paranodin."
    Bhat M.A., Rios J.C., Lu Y., Garcia-Fresco G.P., Ching W., St Martin M., Li J., Einheber S., Chesler M., Rosenbluth J., Salzer J.L., Bellen H.J.
    Neuron 30:369-383(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Internodal specializations of myelinated axons in the central nervous system."
    Arroyo E.J., Xu T., Poliak S., Watson M., Peles E., Scherer S.S.
    Cell Tissue Res. 305:53-66(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiCNTP1_MOUSE
AccessioniPrimary (citable) accession number: O54991
Secondary accession number(s): A2A4K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.