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Contactin-associated protein 1 (Caspr) (Caspr1) (Neurexin IV) (Neurexin-4) (p190)

 CNTP1_HUMAN             Reviewed;        1384 AA.
P78357;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
20-JUN-2018, entry version 167.
RecName: Full=Contactin-associated protein 1;
Short=Caspr;
Short=Caspr1;
AltName: Full=Neurexin IV;
AltName: Full=Neurexin-4;
AltName: Full=p190;
Flags: Precursor;
Name=CNTNAP1; Synonyms=CASPR, NRXN4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CONTACTIN.
TISSUE=Neuroblastoma;
PubMed=9118959; DOI=10.1093/emboj/16.5.978;
Peles E., Nativ M., Lustig M., Grumet M., Schilling J., Martinez R.,
Plowman G.D., Schlessinger J.;
"Identification of a novel contactin-associated transmembrane receptor
with multiple domains implicated in protein-protein interactions.";
EMBO J. 16:978-988(1997).
[2]
INVOLVEMENT IN LCCS7, AND FUNCTION.
PubMed=24319099; DOI=10.1093/hmg/ddt618;
Laquerriere A., Maluenda J., Camus A., Fontenas L., Dieterich K.,
Nolent F., Zhou J., Monnier N., Latour P., Gentil D., Heron D.,
Desguerres I., Landrieu P., Beneteau C., Delaporte B., Bellesme C.,
Baumann C., Capri Y., Goldenberg A., Lyonnet S., Bonneau D.,
Estournet B., Quijano-Roy S., Francannet C., Odent S.,
Saint-Frison M.H., Sigaudy S., Figarella-Branger D., Gelot A.,
Mussini J.M., Lacroix C., Drouin-Garraud V., Malinge M.C.,
Attie-Bitach T., Bessieres B., Bonniere M., Encha-Razavi F.,
Beaufrere A.M., Khung-Savatovsky S., Perez M.J., Vasiljevic A.,
Mercier S., Roume J., Trestard L., Saugier-Veber P., Cordier M.P.,
Layet V., Legendre M., Vigouroux-Castera A., Lunardi J., Bayes M.,
Jouk P.S., Rigonnot L., Granier M., Sternberg D., Warszawski J.,
Gut I., Gonzales M., Tawk M., Melki J.;
"Mutations in CNTNAP1 and ADCY6 are responsible for severe
arthrogryposis multiplex congenita with axoglial defects.";
Hum. Mol. Genet. 23:2279-2289(2014).
[3]
VARIANTS LCCS7 ARG-323 AND 623-TRP--GLU-1384 DEL.
PubMed=27782105; DOI=10.1038/ejhg.2016.142;
Nizon M., Cogne B., Vallat J.M., Joubert M., Liet J.M., Simon L.,
Vincent M., Kuery S., Boisseau P., Schmitt S., Mercier S.,
Beneteau C., Larrose C., Coste M., Latypova X., Pereon Y.,
Mussini J.M., Bezieau S., Isidor B.;
"Two novel variants in CNTNAP1 in two siblings presenting with
congenital hypotonia and hypomyelinating neuropathy.";
Eur. J. Hum. Genet. 25:150-152(2016).
[4]
INVOLVEMENT IN DISEASE, VARIANTS 623-TRP--GLU-1384 DEL;
671-GLN--GLU-1384 DEL AND CYS-764, AND FUNCTION.
PubMed=27818385; DOI=10.1093/jnen/nlw093;
Vallat J.M., Nizon M., Magee A., Isidor B., Magy L., Pereon Y.,
Richard L., Ouvrier R., Cogne B., Devaux J., Zuchner S., Mathis S.;
"Contactin-Associated Protein 1 (CNTNAP1) Mutations Induce
Characteristic Lesions of the Paranodal Region.";
J. Neuropathol. Exp. Neurol. 75:1155-1159(2016).
[5]
INVOLVEMENT IN LCCS7.
PubMed=28254648; DOI=10.1016/j.ejmg.2017.02.006;
Lakhani S., Doan R., Almureikhi M., Partlow J.N., Al Saffar M.,
Elsaid M.F., Alaaraj N., James Barkovich A., Walsh C.A., Ben-Omran T.;
"Identification of a novel CNTNAP1 mutation causing arthrogryposis
multiplex congenita with cerebral and cerebellar atrophy.";
Eur. J. Med. Genet. 60:245-249(2017).
[6]
VARIANT PRO-388.
PubMed=27668699; DOI=10.1002/mus.25416;
Mehta P., Kuespert M., Bale T., Brownstein C.A., Towne M.C.,
De Girolami U., Shi J., Beggs A.H., Darras B.T., Wegner M., Piao X.,
Agrawal P.B.;
"Novel mutation in CNTNAP1 results in congenital hypomyelinating
neuropathy.";
Muscle Nerve 55:761-765(2017).
[7]
VARIANT LCCS7 672-TRP--GLU-1384 DEL, VARIANTS 671-GLN--GLU-1384 DEL
AND CYS-764, AND FUNCTION.
PubMed=28374019; DOI=10.1212/NXG.0000000000000144;
Hengel H., Magee A., Mahanjah M., Vallat J.M., Ouvrier R.,
Abu-Rashid M., Mahamid J., Schuele R., Schulze M., Kraegeloh-Mann I.,
Bauer P., Zuechner S., Sharkia R., Schoels L.;
"CNTNAP1 mutations cause CNS hypomyelination and neuropathy with or
without arthrogryposis.";
Neurol. Genet. 3:E144-E144(2017).
-!- FUNCTION: Required, with CNTNAP2, for radial and longitudinal
organization of myelinated axons. Plays a role in the formation of
functional distinct domains critical for saltatory conduction of
nerve impulses in myelinated nerve fibers. Demarcates the
paranodal region of the axo-glial junction. In association with
contactin involved in the signaling between axons and myelinating
glial cells. {ECO:0000269|PubMed:24319099,
ECO:0000269|PubMed:27818385, ECO:0000269|PubMed:28374019}.
-!- SUBUNIT: Interacts with CNTN1/contactin in cis form.
{ECO:0000269|PubMed:9118959}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-1751903, EBI-389883;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Cell junction, paranodal septate
junction {ECO:0000250|UniProtKB:O54991}.
-!- TISSUE SPECIFICITY: Predominantly expressed in brain. Weak
expression detected in ovary, pancreas, colon, lung, heart,
intestine and testis.
-!- DISEASE: Lethal congenital contracture syndrome 7 (LCCS7)
[MIM:616286]: A form of lethal congenital contracture syndrome, an
autosomal recessive disorder characterized by degeneration of
anterior horn neurons, extreme skeletal muscle atrophy and
congenital non-progressive joint contractures. The contractures
can involve the upper or lower limbs and/or the vertebral column,
leading to various degrees of flexion or extension limitations
evident at birth. LCCS7 is a severe axoglial disease characterized
by congenital distal joint contractures, polyhydramnios, reduced
fetal movements, and motor paralysis leading to death early in the
neonatal period. {ECO:0000269|PubMed:24319099,
ECO:0000269|PubMed:27782105, ECO:0000269|PubMed:28254648,
ECO:0000269|PubMed:28374019}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in CNTNAP1 are associated with congenital
hypomyelinating neuropathy (CHN). Patients show polyhydramnios and
reduced fetal movements, they were hypotonic and required
ventilatory support at birth. But no arthrogryposis is noted.
Patients die often early in the neonatal period.
{ECO:0000269|PubMed:27668699, ECO:0000269|PubMed:27818385,
ECO:0000269|PubMed:28374019}.
-!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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EMBL; U87223; AAB48481.1; -; mRNA.
CCDS; CCDS11436.1; -.
RefSeq; NP_003623.1; NM_003632.2.
RefSeq; XP_016880727.1; XM_017025238.1.
UniGene; Hs.408730; -.
ProteinModelPortal; P78357; -.
BioGrid; 114078; 15.
CORUM; P78357; -.
IntAct; P78357; 11.
MINT; P78357; -.
STRING; 9606.ENSP00000264638; -.
iPTMnet; P78357; -.
PhosphoSitePlus; P78357; -.
BioMuta; CNTNAP1; -.
DMDM; 17433016; -.
EPD; P78357; -.
MaxQB; P78357; -.
PaxDb; P78357; -.
PeptideAtlas; P78357; -.
PRIDE; P78357; -.
ProteomicsDB; 57588; -.
DNASU; 8506; -.
Ensembl; ENST00000264638; ENSP00000264638; ENSG00000108797.
GeneID; 8506; -.
KEGG; hsa:8506; -.
UCSC; uc002iay.4; human.
CTD; 8506; -.
DisGeNET; 8506; -.
EuPathDB; HostDB:ENSG00000108797.11; -.
GeneCards; CNTNAP1; -.
HGNC; HGNC:8011; CNTNAP1.
HPA; HPA011772; -.
MalaCards; CNTNAP1; -.
MIM; 602346; gene.
MIM; 616286; phenotype.
neXtProt; NX_P78357; -.
OpenTargets; ENSG00000108797; -.
Orphanet; 2680; Hypomyelination neuropathy - arthrogryposis.
PharmGKB; PA26691; -.
eggNOG; KOG3516; Eukaryota.
eggNOG; ENOG410XPHG; LUCA.
GeneTree; ENSGT00760000118991; -.
HOGENOM; HOG000230964; -.
HOVERGEN; HBG057718; -.
InParanoid; P78357; -.
KO; K07379; -.
OMA; RHDLHYH; -.
OrthoDB; EOG091G00LF; -.
PhylomeDB; P78357; -.
TreeFam; TF321823; -.
Reactome; R-HSA-447043; Neurofascin interactions.
SignaLink; P78357; -.
ChiTaRS; CNTNAP1; human.
GenomeRNAi; 8506; -.
PRO; PR:P78357; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108797; -.
CleanEx; HS_CNTNAP1; -.
ExpressionAtlas; P78357; baseline and differential.
Genevisible; P78357; HS.
GO; GO:0016021; C:integral component of membrane; ISS:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
GO; GO:0033270; C:paranode region of axon; ISS:BHF-UCL.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0022010; P:central nervous system myelination; IMP:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
GO; GO:0019227; P:neuronal action potential propagation; ISS:BHF-UCL.
GO; GO:0030913; P:paranodal junction assembly; IMP:UniProtKB.
GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:UniProtKB.
GO; GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.120.260; -; 1.
InterPro; IPR028872; Caspr1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000421; FA58C.
InterPro; IPR036056; Fibrinogen-like_C.
InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR001791; Laminin_G.
InterPro; IPR003585; Neurexin-like.
PANTHER; PTHR43925:SF5; PTHR43925:SF5; 1.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF02210; Laminin_G_2; 4.
SMART; SM00294; 4.1m; 1.
SMART; SM00231; FA58C; 1.
SMART; SM00282; LamG; 4.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF49899; SSF49899; 5.
SUPFAM; SSF56496; SSF56496; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01285; FA58C_1; 1.
PROSITE; PS01286; FA58C_2; 1.
PROSITE; PS50022; FA58C_3; 1.
PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 4.
1: Evidence at protein level;
Cell adhesion; Cell junction; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3-binding; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1384 Contactin-associated protein 1.
/FTId=PRO_0000019503.
TOPO_DOM 20 1283 Extracellular. {ECO:0000255}.
TRANSMEM 1284 1304 Helical. {ECO:0000255}.
TOPO_DOM 1305 1384 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 168 F5/8 type C. {ECO:0000255|PROSITE-
ProRule:PRU00081}.
DOMAIN 203 355 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 389 538 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 540 577 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 576 795 Fibrinogen C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00739}.
DOMAIN 813 956 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 957 996 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1088 1250 Laminin G-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
MOTIF 1328 1369 SH3-binding. {ECO:0000255}.
MOD_RES 1383 1383 Phosphoserine.
{ECO:0000250|UniProtKB:O54991}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 499 499 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 597 597 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 653 653 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 664 664 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 763 763 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 804 804 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 843 843 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 860 860 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 948 948 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 956 956 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1078 1078 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1147 1147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 168 {ECO:0000250}.
DISULFID 323 355 {ECO:0000250}.
DISULFID 506 538 {ECO:0000250}.
DISULFID 544 555 {ECO:0000250}.
DISULFID 549 564 {ECO:0000250}.
DISULFID 566 576 {ECO:0000250}.
DISULFID 930 957 {ECO:0000250}.
DISULFID 961 974 {ECO:0000250}.
DISULFID 968 983 {ECO:0000250}.
DISULFID 985 995 {ECO:0000250}.
DISULFID 1209 1250 {ECO:0000250}.
VARIANT 323 323 C -> R (in LCCS7; dbSNP:rs768554986).
{ECO:0000269|PubMed:27782105}.
/FTId=VAR_078818.
VARIANT 388 388 R -> P (probable disease-associated
mutation found in a patient with
congenital hypomyelinating neuropathy;
dbSNP:rs779027563).
{ECO:0000269|PubMed:27668699}.
/FTId=VAR_078819.
VARIANT 522 522 V -> L (in dbSNP:rs35437096).
/FTId=VAR_050267.
VARIANT 623 1384 Missing (in LCCS7; also found in a
patient with congenital hypomyelinating
neuropathy).
{ECO:0000269|PubMed:27782105,
ECO:0000269|PubMed:27818385}.
/FTId=VAR_078820.
VARIANT 671 1384 Missing (probable disease-associated
mutation found in a patient with
congenital hypomyelinating neuropathy).
{ECO:0000269|PubMed:27818385,
ECO:0000269|PubMed:28374019}.
/FTId=VAR_078821.
VARIANT 672 1384 Missing (in LCCS7).
{ECO:0000269|PubMed:28374019}.
/FTId=VAR_078822.
VARIANT 764 764 R -> C (probable disease-associated
mutation found in a patient with
congenital hypomyelinating neuropathy;
dbSNP:rs761805324).
{ECO:0000269|PubMed:27818385,
ECO:0000269|PubMed:28374019}.
/FTId=VAR_078823.
SEQUENCE 1384 AA; 156267 MW; 7727A13DF626DDCA CRC64;
MMHLRLFCIL LAAVSGAEGW GYYGCDEELV GPLYARSLGA SSYYSLLTAP RFARLHGISG
WSPRIGDPNP WLQIDLMKKH RIRAVATQGS FNSWDWVTRY MLLYGDRVDS WTPFYQRGHN
STFFGNVNES AVVRHDLHFH FTARYIRIVP LAWNPRGKIG LRLGLYGCPY KADILYFDGD
DAISYRFPRG VSRSLWDVFA FSFKTEEKDG LLLHAEGAQG DYVTLELEGA HLLLHMSLGS
SPIQPRPGHT TVSAGGVLND QHWHYVRVDR FGRDVNFTLD GYVQRFILNG DFERLNLDTE
MFIGGLVGAA RKNLAYRHNF RGCIENVIFN RVNIADLAVR RHSRITFEGK VAFRCLDPVP
HPINFGGPHN FVQVPGFPRR GRLAVSFRFR TWDLTGLLLF SRLGDGLGHV ELTLSEGQVN
VSIAQSGRKK LQFAAGYRLN DGFWHEVNFV AQENHAVISI DDVEGAEVRV SYPLLIRTGT
SYFFGGCPKP ASRWDCHSNQ TAFHGCMELL KVDGQLVNLT LVEGRRLGFY AEVLFDTCGI
TDRCSPNMCE HDGRCYQSWD DFICYCELTG YKGETCHTPL YKESCEAYRL SGKTSGNFTI
DPDGSGPLKP FVVYCDIREN RAWTVVRHDR LWTTRVTGSS MERPFLGAIQ YWNASWEEVS
ALANASQHCE QWIEFSCYNS RLLNTAGGYP YSFWIGRNEE QHFYWGGSQP GIQRCACGLD
RSCVDPALYC NCDADQPQWR TDKGLLTFVD HLPVTQVVIG DTNRSTSEAQ FFLRPLRCYG
DRNSWNTISF HTGAALRFPP IRANHSLDVS FYFRTSAPSG VFLENMGGPY CQWRRPYVRV
ELNTSRDVVF AFDVGNGDEN LTVHSDDFEF NDDEWHLVRA EINVKQARLR VDHRPWVLRP
MPLQTYIWME YDQPLYVGSA ELKRRPFVGC LRAMRLNGVT LNLEGRANAS EGTSPNCTGH
CAHPRLPCFH GGRCVERYSY YTCDCDLTAF DGPYCNHDIG GFFEPGTWMR YNLQSALRSA
AREFSHMLSR PVPGYEPGYI PGYDTPGYVP GYHGPGYRLP DYPRPGRPVP GYRGPVYNVT
GEEVSFSFST SSAPAVLLYV SSFVRDYMAV LIKDDGTLQL RYQLGTSPYV YQLTTRPVTD
GQPHSINITR VYRNLFIQVD YFPLTEQKFS LLVDSQLDSP KALYLGRVME TGVIDPEIQR
YNTPGFSGCL SGVRFNNVAP LKTHFRTPRP MTAELAEALR VQGELSESNC GAMPRLVSEV
PPELDPWYLP PDFPYYHDEG WVAILLGFLV AFLLLGLVGM LVLFYLQNHR YKGSYHTNEP
KAAHEYHPGS KPPLPTSGPA QVPTPTAAPN QAPASAPAPA PTPAPAPGPR DQNLPQILEE
SRSE


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