CNTP1_RAT
ID CNTP1_RAT Reviewed; 1381 AA.
AC P97846;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Contactin-associated protein 1;
DE Short=Caspr;
DE Short=Caspr1;
DE AltName: Full=Neurexin IV;
DE AltName: Full=Neurexin-4;
DE AltName: Full=Paranodin;
DE AltName: Full=p190;
DE Flags: Precursor;
GN Name=Cntnap1; Synonyms=Caspr, Nrxn4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CONTACTIN.
RC TISSUE=Pituitary tumor;
RX PubMed=9118959; DOI=10.1093/emboj/16.5.978;
RA Peles E., Nativ M., Lustig M., Grumet M., Schilling J., Martinez R.,
RA Plowman G.D., Schlessinger J.;
RT "Identification of a novel contactin-associated transmembrane receptor with
RT multiple domains implicated in protein-protein interactions.";
RL EMBO J. 16:978-988(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9292722; DOI=10.1016/s0896-6273(00)80942-3;
RA Menegoz M., Gaspar P., Le Bert M., Galvez T., Burgaya F., Palfrey C.,
RA Ezan P., Arnos F., Girault J.-A.;
RT "Paranodin, a glycoprotein of neuronal paranodal membranes.";
RL Neuron 19:319-331(1997).
RN [3]
RP CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9396755; DOI=10.1083/jcb.139.6.1495;
RA Einheber S., Zanazzi G., Ching W., Scherer S., Milner T.A., Peles E.,
RA Salzer J.L.;
RT "The axonal membrane protein Caspr, a homologue of neurexin IV, is a
RT component of the septate-like paranodal junctions that assemble during
RT myelination.";
RL J. Cell Biol. 139:1495-1506(1997).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277; ASN-500 AND ASN-598, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Required, with CNTNAP2, for radial and longitudinal
CC organization of myelinated axons. Plays a role in the formation of
CC functional distinct domains critical for saltatory conduction of nerve
CC impulses in myelinated nerve fibers. Demarcates the paranodal region of
CC the axo-glial junction. In association with contactin involved in the
CC signaling between axons and myelinating glial cells.
CC {ECO:0000250|UniProtKB:O54991}.
CC -!- SUBUNIT: Interacts with CNTN1/contactin in cis form.
CC {ECO:0000269|PubMed:9118959}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, paranodal septate
CC junction {ECO:0000269|PubMed:9396755}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. In myelinated
CC nerve fibers of the CNS predominantly found in paranodal axoglial
CC junctions. In unmyelinated nerve fibers of the CNS diffusely
CC distributed along the entire surface. Weak expression is detected in
CC ovary, pancreas, colon, lung, heart, intestine and testis.
CC {ECO:0000269|PubMed:11512672, ECO:0000269|PubMed:9396755}.
CC -!- DEVELOPMENTAL STAGE: Detected on postnatal day 7 in cerebellum. Follows
CC a caudorostral progression according to the myelination process.
CC Appears to redistribute from the internode to the paranodal region
CC during myelin compaction and maturation (PubMed:9396755). Expression
CC reaches maximal levels between days 14 and 18 and remains at the same
CC levels until adulthood. {ECO:0000269|PubMed:9396755}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; U87224; AAB48482.1; -; mRNA.
DR EMBL; AF000114; AAC53342.1; -; mRNA.
DR PIR; T31083; T31083.
DR RefSeq; NP_114450.1; NM_032061.2.
DR AlphaFoldDB; P97846; -.
DR SMR; P97846; -.
DR BioGRID; 249874; 4.
DR IntAct; P97846; 1.
DR MINT; P97846; -.
DR STRING; 10116.ENSRNOP00000027505; -.
DR GlyGen; P97846; 17 sites, 4 N-linked glycans (4 sites).
DR iPTMnet; P97846; -.
DR PhosphoSitePlus; P97846; -.
DR jPOST; P97846; -.
DR PaxDb; P97846; -.
DR PRIDE; P97846; -.
DR ABCD; P97846; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000027505; ENSRNOP00000027505; ENSRNOG00000020277.
DR GeneID; 84008; -.
DR KEGG; rno:84008; -.
DR UCSC; RGD:70902; rat.
DR CTD; 8506; -.
DR RGD; 70902; Cntnap1.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000160825; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; P97846; -.
DR OMA; HCAHPRF; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; P97846; -.
DR PRO; PR:P97846; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020277; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P97846; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
DR GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
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; ISS:BHF-UCL.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
DR GO; GO:0050884; P:neuromuscular process controlling posture; ISS:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
DR GO; GO:0019227; P:neuronal action potential propagation; ISS:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; ISS:BHF-UCL.
DR GO; GO:1990227; P:paranodal junction maintenance; ISO:RGD.
DR GO; GO:0097106; P:postsynaptic density organization; ISO:RGD.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:UniProtKB.
DR GO; GO:0002175; P:protein localization to paranode region of axon; ISS: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..1381
FT /note="Contactin-associated protein 1"
FT /id="PRO_0000019505"
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..1381
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 544..576
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..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1329..1366
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1333..1365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54991"
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:0007744|PubMed:24090084"
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:0007744|PubMed:24090084"
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:0007744|PubMed:24090084"
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"
SQ SEQUENCE 1381 AA; 155868 MW; BC1CE83DB57C1BA4 CRC64;
MMSLRLFSIL LAAVVSGAQG WGYYGCNEEL VGPLYARSLG ASSYYGLFTT ARFARLHGIS
GWSPRIGDPN PWLQIDLMKK HRIRAVATQG AFNSWDWVTR YMLLYGDRVD SWTPFYQQGH
NATFFGNVND SAVVRHDLHY HFTARYIRIV PLAWNPRGKI GLRLGIYGCP YTSNILYFDG
DDAISYRFQR GASQSLWDVF AFSFKTEEKD GLLLHTEGSQ GDYVTLELQG AHLLLHMSLG
SSPIQPRPGH TTVSAGGVLN DLSWHYVRVD RYGREANLTL DGYVHRFVLN GDFERLNLEN
EIFIGGLVGA ARKNLAYRHN FRGCIENVIY NRINIAEMAV QRHSRITFEG NVAFRCLDPV
PHPINFGGPH NFVQVPGFPR RGRLAVSFRF RTWDLTGLLL FSRLGDGLGH 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
DQSCIDPALH CNCDADQPQW RTDKGLLTFV DHLPVTQVVI GDTNRSSSEA QFFLRPLRCY
GDRNSWNTIS FRTGAALRFP PIRANHSLDV SFYFRTSAPS GVFLENMGGP FCQWRRPYVR
VELNTSRDVV FAFDIGNGDE NLTVHSDDFE FNDDEWHLVR AEINVKQARL RVDHRPWVLR
PMPLQTYIWL EYDQPLYVGS AELKRRPFVG CLRAMRLNGV TLNLEGRANA SEGTFPNCTG
HCTHPRFPCF HGGRCVERYS YYTCDCDLTA FDGPYCNHDI GGFFETGTWM RYNLQSALRS
AAQEFSHMLS RPVPGYEPGY IPGYDTPGYV PGYHGPGYRL PDYPRPGRPV PGYRGPVYNV
TGEEVSFSFS TSSAPAVLLY 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 TQVPTPAPAP ASGPGPRDQN LPQILEESRS
E
