CNTP4_MOUSE
ID CNTP4_MOUSE Reviewed; 1310 AA.
AC Q99P47; Q8K002;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Contactin-associated protein-like 4;
DE AltName: Full=Cell recognition molecule Caspr4;
DE Flags: Precursor;
GN Name=Cntnap4; Synonyms=Caspr4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Spiegel I., Schaeren-Wiemers N., Peles E.;
RT "Identification of two new members of the Caspr family.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24870235; DOI=10.1038/nature13248;
RA Karayannis T., Au E., Patel J.C., Kruglikov I., Markx S., Delorme R.,
RA Heron D., Salomon D., Glessner J., Restituito S., Gordon A.,
RA Rodriguez-Murillo L., Roy N.C., Gogos J.A., Rudy B., Rice M.E.,
RA Karayiorgou M., Hakonarson H., Keren B., Huguet G., Bourgeron T.,
RA Hoeffer C., Tsien R.W., Peles E., Fishell G.;
RT "Cntnap4 differentially contributes to GABAergic and dopaminergic synaptic
RT transmission.";
RL Nature 511:236-240(2014).
CC -!- FUNCTION: Presynaptic protein involved in both dopaminergic synaptic
CC transmission and GABAergic system, thereby participating in the
CC structural maturation of inhibitory interneuron synapses. Involved in
CC the dopaminergic synaptic transmission by attenuating dopamine release
CC through a presynaptic mechanism. Also participates in the GABAergic
CC system. {ECO:0000269|PubMed:24870235}.
CC -!- SUBUNIT: Interacts with TIAM1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000269|PubMed:24870235}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24870235}. Note=Specifically present within the
CC presynaptic compartment of synapses. {ECO:0000269|PubMed:24870235}.
CC -!- TISSUE SPECIFICITY: Specifically present in developing cortical
CC interneurons: highly expressed in cortical parvalbumin (PV) cells and
CC midbrain dopaminergic neurons and is localized presynaptically (at
CC protein level). Also present in the substantia nigra pars compacta
CC (SnC) and ventral tegmental area (VTA) midbrain dopaminergic projection
CC populations. {ECO:0000269|PubMed:24870235}.
CC -!- DISRUPTION PHENOTYPE: Synaptic defects characterized by increased
CC dopamine but decreased GABA signaling. A reduction in the output of
CC cortical parvalbumin (PV)-positive GABAergic basket cells is observed,
CC together with an increase of midbrain dopaminergic release in the
CC nucleus accumbens. Increased dopaminergic signaling induces behavior
CC abnormalities, characterized by severe and highly penetrant over-
CC grooming behavior, resulting in whisker, face and sometimes body hair
CC loss but rarely lesions. The over-grooming phenotype can be
CC pharmacologically reversed following administration of haloperidol
CC drug. {ECO:0000269|PubMed:24870235}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; AF333770; AAG52890.1; -; mRNA.
DR EMBL; AK142816; BAE25200.1; -; mRNA.
DR EMBL; CH466525; EDL11532.1; -; Genomic_DNA.
DR EMBL; BC034628; AAH34628.1; -; mRNA.
DR CCDS; CCDS40482.1; -.
DR RefSeq; NP_569724.2; NM_130457.2.
DR AlphaFoldDB; Q99P47; -.
DR SMR; Q99P47; -.
DR STRING; 10090.ENSMUSP00000112511; -.
DR GlyConnect; 2232; 6 N-Linked glycans (2 sites).
DR GlyGen; Q99P47; 13 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q99P47; -.
DR PhosphoSitePlus; Q99P47; -.
DR MaxQB; Q99P47; -.
DR PaxDb; Q99P47; -.
DR PRIDE; Q99P47; -.
DR ProteomicsDB; 285525; -.
DR DNASU; 170571; -.
DR Ensembl; ENSMUST00000034225; ENSMUSP00000034225; ENSMUSG00000031772.
DR GeneID; 170571; -.
DR KEGG; mmu:170571; -.
DR UCSC; uc009nnj.1; mouse.
DR CTD; 85445; -.
DR MGI; MGI:2183572; Cntnap4.
DR VEuPathDB; HostDB:ENSMUSG00000031772; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000157674; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q99P47; -.
DR OMA; LSTQNWS; -.
DR OrthoDB; 338397at2759; -.
DR BioGRID-ORCS; 170571; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cntnap4; mouse.
DR PRO; PR:Q99P47; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99P47; protein.
DR Bgee; ENSMUSG00000031772; Expressed in substantia nigra and 91 other tissues.
DR ExpressionAtlas; Q99P47; baseline and differential.
DR Genevisible; Q99P47; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:2000821; P:regulation of grooming behavior; IMP:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0032225; P:regulation of synaptic transmission, dopaminergic; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR028875; CASPR4.
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 PANTHER; PTHR15036:SF40; PTHR15036:SF40; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00181; EGF; 2.
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 membrane; Cell projection; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1310
FT /note="Contactin-associated protein-like 4"
FT /id="PRO_0000019511"
FT TOPO_DOM 28..1243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1265..1310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..179
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 214..346
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 400..529
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 551..588
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 589..794
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 795..960
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 960..999
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1048..1204
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..179
FT /evidence="ECO:0000250"
FT DISULFID 334..366
FT /evidence="ECO:0000250"
FT DISULFID 517..549
FT /evidence="ECO:0000250"
FT DISULFID 555..566
FT /evidence="ECO:0000250"
FT DISULFID 560..575
FT /evidence="ECO:0000250"
FT DISULFID 577..587
FT /evidence="ECO:0000250"
FT DISULFID 933..960
FT /evidence="ECO:0000250"
FT DISULFID 964..977
FT /evidence="ECO:0000250"
FT DISULFID 971..986
FT /evidence="ECO:0000250"
FT DISULFID 988..998
FT /evidence="ECO:0000250"
FT DISULFID 1169..1204
FT /evidence="ECO:0000250"
FT CONFLICT 993
FT /note="Y -> F (in Ref. 1; AAG52890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1310 AA; 144730 MW; BEC6AB0A11DE6A14 CRC64;
MNMGSVAGAV LKMLLLLSTQ NWNRVEAGNS YDCDEPLVSA LPQASFSSSS ELSSSHGPGF
ARLNRRDGAG GWSPLVSNKY QWLQIDLGER MEVTSVATQG GYGSSNWVTS YLLMFSDSGR
NWKQYRQEDS IWGFSGNANA DSVVYYRLQP SIKARFLRFI PLEWNPKGRI GMRIEVFGCA
YRSVVIDLDG KSSLLYRFDQ NSLSPIRDII SLKFKTMESD GILLHRAGPA GDHITLELRR
GKLFLLINSG DARLTSSSTL INLTLGSLLD DQHWHSVLIQ RLGKQVNFTV DEHRRHFHAQ
GEFNYLDLDY EISFGGISAP AKSVSLPYKH FHGCLENLFY NGVDVIGLVK EHSPQIITMG
NASFSCSQPQ SMPLTFLSPR SYLVLPASTK EEAISASFQF RTWNKAGLLL FSELQLVSGS
LLLLLSDGKL KLTLYQPGKS PSDITAGAGL GDGQWHSVSL SAKRNHLSVV VDGHISPASP
WLGPEQVNSG GVFYFGGCPD KGFGSKCKSP LGGFQGCMRL ISINNKMVDL IAVQQGALGN
FSDLQIDSCG ISDRCLPNSC EHGGECSQSW STFHCNCTNT GYTGATCHSS VYEQSCEAYK
HQGNASGFYY IDSDGSGPLQ PFLLYCNMTE TAWTVMQHNG SDLMRVRNTH SENAHTGVFE
YTASMEQLQA AINRAEHCQQ ELVYYCKKSR LVNQQDGSPR SWWVGRTNET QTYWGGSLPV
HQKCTCGLEG NCIDAQYHCN CDADLNEWTN DTGFLSYKEH LPVTKIVITD TGRPHSEAAY
KLGPLLCRGD RPFWNAASFN TEASYLHFPT FHGELSADVS FFFKTTALSG VFLENLGITD
FIRIELRSPT TVTFSFDVGN GPFELSVHSP THFNDNQWHH VRVERNMKEA SLRVDELPPK
IQAAPTDGHV LLQLNSQLFV GGTATRQRGF LGCIRSLQLN GMALDLEERA TVTPGVQPGC
RGHCGSYGKL CRHGGKCREK PSGFFCDCSS SAYAGPFCSK EISAYFGSGS SVIYNFQENY
SLSKNSSFHA ASFHGDMKLS REMIKFSFRT TRAPSLLLHM SSFYKEYLSI IIAKNGSLQI
RYKLNKYHEP DVISFDLKSM ADGQLHHIKI NREEGMVFVE IDENTRRQTY LSSGTEFSAV
KSLVLGRMLE YSDVDQETAL AAAHGFTGCL SAVQFSHIAP LKAALQPGPP APVTVTGHVT
ESSCVAPSGT DATSRERTHS FADHSGTMDD REPLTHAIKS DSAVIGGLIA VVIFILLCVS
AIAVRIYQQK RLYKRNEAKR SENVDSAEAV LKSELHIQNA VGENQKEYFF
