LOCUS       NP_114450               1381 aa            linear   ROD 02-APR-2024
DEFINITION  contactin-associated protein 1 precursor [Rattus norvegicus].
ACCESSION   NP_114450 XP_001081472
VERSION     NP_114450.1
DBSOURCE    REFSEQ: accession NM_032061.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1381)
  AUTHORS   Morato,X., Lujan,R., Goncalves,N., Watanabe,M., Altafaj,X.,
            Carvalho,A.L., Fernandez-Duenas,V., Cunha,R.A. and Ciruela,F.
  TITLE     Metabotropic glutamate type 5 receptor requires
            contactin-associated protein 1 to control memory formation
  JOURNAL   Hum Mol Genet 27 (20), 3528-3541 (2018)
   PUBMED   30010864
  REMARK    GeneRIF: The physical interaction, co-distribution and functional
            role of Caspr1-mGlu5R interplay in memory formation was
            characterized.
REFERENCE   2  (residues 1 to 1381)
  AUTHORS   Zhao,W.D., Liu,D.X., Wei,J.Y., Miao,Z.W., Zhang,K., Su,Z.K.,
            Zhang,X.W., Li,Q., Fang,W.G., Qin,X.X., Shang,D.S., Li,B., Li,Q.C.,
            Cao,L., Kim,K.S. and Chen,Y.H.
  TITLE     Caspr1 is a host receptor for meningitis-causing Escherichia coli
  JOURNAL   Nat Commun 9 (1), 2296 (2018)
   PUBMED   29895952
  REMARK    GeneRIF: E. coli exploits Caspr1 as a host receptor for penetration
            of the blood-brain barrier, resulting in meningitis
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1381)
  AUTHORS   Hengel,H., Magee,A., Mahanjah,M., Vallat,J.M., Ouvrier,R.,
            Abu-Rashid,M., Mahamid,J., Schule,R., Schulze,M., Krageloh-Mann,I.,
            Bauer,P., Zuchner,S., Sharkia,R. and Schols,L.
  TITLE     CNTNAP1 mutations cause CNS hypomyelination and neuropathy with or
            without arthrogryposis
  JOURNAL   Neurol Genet 3 (2), e144 (2017)
   PUBMED   28374019
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1381)
  AUTHORS   Vallat,J.M., Nizon,M., Magee,A., Isidor,B., Magy,L., Pereon,Y.,
            Richard,L., Ouvrier,R., Cogne,B., Devaux,J., Zuchner,S. and
            Mathis,S.
  TITLE     Contactin-Associated Protein 1 (CNTNAP1) Mutations Induce
            Characteristic Lesions of the Paranodal Region
  JOURNAL   J Neuropathol Exp Neurol 75 (12), 1155-1159 (2016)
   PUBMED   27818385
REFERENCE   5  (residues 1 to 1381)
  AUTHORS   Hu,B., Arpag,S., Zhang,X., Mobius,W., Werner,H., Sosinsky,G.,
            Ellisman,M., Zhang,Y., Hamilton,A., Chernoff,J. and Li,J.
  TITLE     Tuning PAK Activity to Rescue Abnormal Myelin Permeability in HNPP
  JOURNAL   PLoS Genet 12 (9), e1006290 (2016)
   PUBMED   27583434
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1381)
  AUTHORS   Arroyo,E.J., Xu,T., Poliak,S., Watson,M., Peles,E. and Scherer,S.S.
  TITLE     Internodal specializations of myelinated axons in the central
            nervous system
  JOURNAL   Cell Tissue Res 305 (1), 53-66 (2001)
   PUBMED   11512672
REFERENCE   7  (residues 1 to 1381)
  AUTHORS   Poliak,S., Gollan,L., Martinez,R., Custer,A., Einheber,S.,
            Salzer,J.L., Trimmer,J.S., Shrager,P. and Peles,E.
  TITLE     Caspr2, a new member of the neurexin superfamily, is localized at
            the juxtaparanodes of myelinated axons and associates with K+
            channels
  JOURNAL   Neuron 24 (4), 1037-1047 (1999)
   PUBMED   10624965
REFERENCE   8  (residues 1 to 1381)
  AUTHORS   Einheber,S., Zanazzi,G., Ching,W., Scherer,S., Milner,T.A.,
            Peles,E. and Salzer,J.L.
  TITLE     The axonal membrane protein Caspr, a homologue of neurexin IV, is a
            component of the septate-like paranodal junctions that assemble
            during myelination
  JOURNAL   J Cell Biol 139 (6), 1495-1506 (1997)
   PUBMED   9396755
REFERENCE   9  (residues 1 to 1381)
  AUTHORS   Menegoz,M., Gaspar,P., Le Bert,M., Galvez,T., Burgaya,F.,
            Palfrey,C., Ezan,P., Arnos,F. and Girault,J.A.
  TITLE     Paranodin, a glycoprotein of neuronal paranodal membranes
  JOURNAL   Neuron 19 (2), 319-331 (1997)
   PUBMED   9292722
REFERENCE   10 (residues 1 to 1381)
  AUTHORS   Peles,E., Nativ,M., Lustig,M., Grumet,M., Schilling,J.,
            Martinez,R., Plowman,G.D. and Schlessinger,J.
  TITLE     Identification of a novel contactin-associated transmembrane
            receptor with multiple domains implicated in protein-protein
            interactions
  JOURNAL   EMBO J 16 (5), 978-988 (1997)
   PUBMED   9118959
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U87224.1, AF000114.1, CB610334.1 and BF393814.1.
            
            On Jun 25, 2006 this sequence version replaced XP_001081472.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U87224.1, AF000114.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1381
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="10"
                     /map="10q31"
     Protein         1..1381
                     /product="contactin-associated protein 1 precursor"
                     /note="neurexin IV; p190; caspr1; paranodin; neurexin-4"
                     /calculated_mol_wt=153822
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2065
     mat_peptide     21..1381
                     /product="Contactin-associated protein 1.
                     /id=PRO_0000019505"
                     /note="propagated from UniProtKB/Swiss-Prot (P97846.1)"
                     /calculated_mol_wt=153822
     Region          37..168
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(63,91,96)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Region          176..331
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Region          363..514
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            500
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            519
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Region          545..574
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          585..>659
                     /region_name="FReD"
                     /note="Fibrinogen-related domains (FReDs); C terminal
                     globular domain of fibrinogen. Fibrinogen is involved in
                     blood clotting, being activated by thrombin to assemble
                     into fibrin clots. The N-termini of 2 times 3 chains come
                     together to form a globular...; cl00085"
                     /db_xref="CDD:412152"
     Region          <596..>617
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     Site            598
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0007744|PubMed:24090084; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            654
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            665
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            764
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Region          788..938
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Site            805
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            844
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            861
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            957
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            1079
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Region          1089..1219
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            1148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     Site            1285..1305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P97846.1)"
     Region          1305..1323
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     Region          1317..1381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P97846.1)"
     Region          1329..1366
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P97846.1)"
     Site            1380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54991; propagated from
                     UniProtKB/Swiss-Prot (P97846.1)"
     CDS             1..1381
                     /gene="Cntnap1"
                     /gene_synonym="Caspr"
                     /coded_by="NM_032061.2:154..4299"
                     /db_xref="GeneID:84008"
                     /db_xref="RGD:70902"
ORIGIN      
        1 mmslrlfsil laavvsgaqg wgyygcneel vgplyarslg assyyglftt arfarlhgis
       61 gwsprigdpn pwlqidlmkk hriravatqg afnswdwvtr ymllygdrvd swtpfyqqgh
      121 natffgnvnd savvrhdlhy hftaryiriv plawnprgki glrlgiygcp ytsnilyfdg
      181 ddaisyrfqr gasqslwdvf afsfkteekd glllhtegsq gdyvtlelqg ahlllhmslg
      241 sspiqprpgh ttvsaggvln dlswhyvrvd rygreanltl dgyvhrfvln gdferlnlen
      301 eifigglvga arknlayrhn frgcienviy nriniaemav qrhsritfeg nvafrcldpv
      361 phpinfggph nfvqvpgfpr rgrlavsfrf rtwdltglll fsrlgdglgh velmlsegqv
      421 nvsiaqtgrk klqfaagyrl ndgfwhevnf vaqenhavis iddvegaevr vsypllirtg
      481 tsyffggcpk pasrwgchsn qtafhgcmel lkvdgqlvnl tlvefrklgy faevlfdtcg
      541 itdrcspnmc ehdgrcyqsw ddficycelt gykgvtchep lykesceayr lsgkysgnyt
      601 idpdgsgplk pfvvycdire nrawtvvrhd rlwttrvtgs smdrpflgai qywnasweev
      661 salanasqhc eqwiefscyn srllntaggy pysfwigrne eqhfywggsq pgiqrcacgl
      721 dqscidpalh cncdadqpqw rtdkglltfv dhlpvtqvvi gdtnrsssea qfflrplrcy
      781 gdrnswntis frtgaalrfp piranhsldv sfyfrtsaps gvflenmggp fcqwrrpyvr
      841 velntsrdvv fafdigngde nltvhsddfe fnddewhlvr aeinvkqarl rvdhrpwvlr
      901 pmplqtyiwl eydqplyvgs aelkrrpfvg clramrlngv tlnlegrana segtfpnctg
      961 hcthprfpcf hggrcverys yytcdcdlta fdgpycnhdi ggffetgtwm rynlqsalrs
     1021 aaqefshmls rpvpgyepgy ipgydtpgyv pgyhgpgyrl pdyprpgrpv pgyrgpvynv
     1081 tgeevsfsfs tssapavlly vssfvrdyma vlikedgtlq lryqlgtspy vyqlttrpvt
     1141 dgqphsvnit rvyrnlfiqv dyfplteqkf sllvdsqlds pkalylgrvm etgvidpeiq
     1201 ryntpgfsgc lsgvrfnnva plkthfrtpr pmtaelaeam rvqgelsesn cgamprlvse
     1261 vppeldpwyl ppdfpyyhdd gwiaillgfl vaflllglvg mlvlfylqnh rykgsyhtne
     1321 pkathdshpg gkaplppsgp aqapaptpap tqvptpapap asgpgprdqn lpqileesrs
     1381 e
//
