CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000841
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Contactin-associated protein 1 
Protein Synonyms/Alias
 Caspr; Caspr1; MHDNIV; NCP1; Neurexin IV; Neurexin-4; Paranodin 
Gene Name
 Cntnap1 
Gene Synonyms/Alias
 Nrxn4 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1332HDSHPGGKAPLPPSGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 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. 
Sequence Annotation
 DOMAIN 26 169 F5/8 type C.
 DOMAIN 204 356 Laminin G-like 1.
 DOMAIN 390 539 Laminin G-like 2.
 DOMAIN 545 577 EGF-like 1.
 DOMAIN 577 796 Fibrinogen C-terminal.
 DOMAIN 814 958 Laminin G-like 3.
 DOMAIN 962 996 EGF-like 2.
 DOMAIN 1089 1251 Laminin G-like 4.
 MOTIF 1334 1370 SH3-binding (Potential).
 MOD_RES 1384 1384 Phosphoserine.
 CARBOHYD 121 121 N-linked (GlcNAc...) (Potential).
 CARBOHYD 129 129 N-linked (GlcNAc...) (Potential).
 CARBOHYD 277 277 N-linked (GlcNAc...) (Potential).
 CARBOHYD 421 421 N-linked (GlcNAc...) (Potential).
 CARBOHYD 500 500 N-linked (GlcNAc...) (Potential).
 CARBOHYD 519 519 N-linked (GlcNAc...) (Potential).
 CARBOHYD 598 598 N-linked (GlcNAc...) (Potential).
 CARBOHYD 654 654 N-linked (GlcNAc...) (Potential).
 CARBOHYD 665 665 N-linked (GlcNAc...) (Potential).
 CARBOHYD 764 764 N-linked (GlcNAc...) (Potential).
 CARBOHYD 805 805 N-linked (GlcNAc...) (Potential).
 CARBOHYD 844 844 N-linked (GlcNAc...) (Potential).
 CARBOHYD 861 861 N-linked (GlcNAc...) (Potential).
 CARBOHYD 949 949 N-linked (GlcNAc...) (Potential).
 CARBOHYD 957 957 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1079 1079 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1148 1148 N-linked (GlcNAc...) (Potential).
 DISULFID 26 169 By similarity.
 DISULFID 324 356 By similarity.
 DISULFID 507 539 By similarity.
 DISULFID 545 556 By similarity.
 DISULFID 550 565 By similarity.
 DISULFID 567 577 By similarity.
 DISULFID 931 958 By similarity.
 DISULFID 962 975 By similarity.
 DISULFID 969 984 By similarity.
 DISULFID 986 996 By similarity.
 DISULFID 1210 1251 By similarity.  
Keyword
 Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat; SH3-binding; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1385 AA 
Protein Sequence
MMSLRLFSIL LATVVSGAWG WGYYGCNEEL VGPLYARSLG ASSYYGLFTT ARFARLHGIS 60
GWSPRIGDPN PWLQIDLMKK HRIRAVATQG AFNSWDWVTR YMLLYGDRVD SWTPFYQKGH 120
NATFFGNVND SAVVRHDLHY HFTARYIRIV PLAWNPRGKI GLRLGIYGCP YTSSILYFDG 180
DDAISYRFQR GASQSLWDVF AFSFKTEEKD GLLLHTEGSQ GDYVTLELQG AHLLLHMSLG 240
SSPIQPRPGH TTVSLGGVLN DLSWHYVRVD RYGRDANFTL DGYAHHFVLN GDFERLNLEN 300
EIFIGGLVGA ARKNLAYRHN FRGCIENVIY NRINIAEMAV MRHSRITFEG NVAFRCLDPV 360
PHPINFGGPH NFVQVPGFPR RGRLAVSFRF RTWDLTGLLL FSHLGDGLGH VELMLSEGQV 420
NVSIAQTGRK KLQFAAGYRL NDGFWHEVNF VAQENHAVIS IDDVEGAEVR VSYPLLIRTG 480
TSYFFGGCPK PASRWGCHSN QTAFHGCMEL LKVDGQLVNL TLVEFRKLGY FAEVLFDTCG 540
ITDRCSPNMC EHDGRCYQSW DDFICYCELT GYKGVTCHEP LYKESCEAYR LSGKYSGNYT 600
IDPDGSGPLK PFVVYCDIRE NRAWTVVRHD RLWTTRVTGS SMDRPFLGAI QYWNASWEEV 660
SALANASQHC EQWIEFSCYN SRLLNTAGGY PYSFWIGRNE EQHFYWGGSQ PGIQRCACGL 720
DQSCVDPALH CNCDADQPQW RTDKGLLTFV DHLPVTQVVV GDTNRSNSEA QFFLRPLRCY 780
GDRNSWNTIS FHTGAALRFP PIRANHSLDV SFYFRTSAPS GVFLENMGGP FCRWRRPYVR 840
VELNTSRDVV FAFDIGNGDE NLTVHSDDFE FNDDEWHLVR AEINVKQARL RVDHRPWVLR 900
PMPLQTYIWL VYDQPLYVGS AELKRRPFVG CLRAMRLNGV TLNLEGRANA SEGTFPNCTG 960
HCTHPRFPCF HGGRCVERYS YYTCDCDLTA FDGPYCNHDI GGFFETGTWM RYNLQSALRS 1020
AAREFSHMLS RPVPGYEPGY VPGYDTPGYV PGYHGPGYRL PEYPRPGRPV PGYRGPVYNV 1080
TGEEVSFSFS TNSAPAVLLY VSSFVRDYMA VLIKEDGTLQ LRYQLGTSPY VYQLTTRPVT 1140
DGQPHSVNIT RVYRNLFIQV DYFPLTEQKF SLLVDSQLDS PKALYLGRVM ETGVIDPEIQ 1200
RYNTPGFSGC LSGVRFNNVA PLKTHFRTPR PMTAELAEAM RVQGELSESN CGAMPRLVSE 1260
VPPELDPWYL PPDFPYYHDD GWIAILLGFL VAFLLLGLVG MLVLFYLQNH RYKGSYHTNE 1320
PKATHDSHPG GKAPLPPSGP AQAPAPTPAP TQLPTPAPAP APAPASGPGP RDQNLPQILE 1380
ESRSE 1385 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0008088; P:axon cargo transport; IMP:BHF-UCL.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007010; P:cytoskeleton organization; IMP:BHF-UCL.
 GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
 GO:0050884; P:neuromuscular process controlling posture; IMP:BHF-UCL.
 GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
 GO:0030913; P:paranodal junction assembly; IMP:BHF-UCL.
 GO:0002175; P:protein localization to paranode region of axon; IMP:BHF-UCL. 
Interpro
 IPR000421; Coagulation_fac_5/8-C_type_dom.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR000742; EG-like_dom.
 IPR014716; Fibrinogen_a/b/g_C_1.
 IPR002181; Fibrinogen_a/b/g_C_dom.
 IPR008979; Galactose-bd-like.
 IPR001791; Laminin_G.
 IPR003585; Neurexin-like. 
Pfam
 PF00754; F5_F8_type_C
 PF02210; Laminin_G_2 
SMART
 SM00294; 4.1m
 SM00181; EGF
 SM00231; FA58C
 SM00282; LamG 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01285; FA58C_1
 PS01286; FA58C_2
 PS50022; FA58C_3
 PS00514; FIBRINOGEN_C_1
 PS51406; FIBRINOGEN_C_2
 PS50025; LAM_G_DOMAIN 
PRINTS