GenomeNet

Database: UniProt
Entry: Q99P47
LinkDB: Q99P47
Original site: Q99P47 
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   10-APR-2019, entry version 137.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   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
RT   synaptic transmission.";
RL   Nature 511:236-240(2014).
CC   -!- FUNCTION: Presynaptic protein involved in both dopaminergic
CC       synaptic transmission and GABAergic system, thereby participating
CC       in the structural maturation of inhibitory interneuron synapses.
CC       Involved in the dopaminergic synaptic transmission by attenuating
CC       dopamine release through a presynaptic mechanism. Also
CC       participates in the GABAergic system.
CC       {ECO:0000269|PubMed:24870235}.
CC   -!- SUBUNIT: Interacts with TIAM1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
CC       membrane {ECO:0000269|PubMed:24870235}; Single-pass type I
CC       membrane protein {ECO:0000269|PubMed:24870235}. Note=Specifically
CC       present within the presynaptic compartment of synapses.
CC   -!- TISSUE SPECIFICITY: Specifically present in developing cortical
CC       interneurons: highly expressed in cortical parvalbumin (PV) cells
CC       and midbrain dopaminergic neurons and is localized presynaptically
CC       (at protein level). Also present in the substantia nigra pars
CC       compacta (SnC) and ventral tegmental area (VTA) midbrain
CC       dopaminergic projection populations.
CC       {ECO:0000269|PubMed:24870235}.
CC   -!- DISRUPTION PHENOTYPE: Synaptic defects characterized by increased
CC       dopamine but decreased GABA signaling. A reduction in the output
CC       of cortical parvalbumin (PV)-positive GABAergic basket cells is
CC       observed, together with an increase of midbrain dopaminergic
CC       release in the nucleus accumbens. Increased dopaminergic signaling
CC       induces behavior abnormalities, characterized by severe and highly
CC       penetrant over-grooming behavior, resulting in whisker, face and
CC       sometimes body hair loss but rarely lesions. The over-grooming
CC       phenotype can be pharmacologically reversed following
CC       administration of haloperidol drug. {ECO:0000269|PubMed:24870235}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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   UniGene; Mm.209232; -.
DR   UniGene; Mm.403088; -.
DR   ProteinModelPortal; Q99P47; -.
DR   SMR; Q99P47; -.
DR   STRING; 10090.ENSMUSP00000112511; -.
DR   iPTMnet; Q99P47; -.
DR   PhosphoSitePlus; Q99P47; -.
DR   MaxQB; Q99P47; -.
DR   PaxDb; Q99P47; -.
DR   PRIDE; Q99P47; -.
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   eggNOG; KOG3516; Eukaryota.
DR   eggNOG; ENOG410XPHG; LUCA.
DR   GeneTree; ENSGT00940000157674; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; Q99P47; -.
DR   OrthoDB; 338397at2759; -.
DR   PRO; PR:Q99P47; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000031772; Expressed in 102 organ(s), highest expression level in substantia nigra.
DR   ExpressionAtlas; Q99P47; baseline and differential.
DR   Genevisible; Q99P47; MM.
DR   GO; GO:0030054; C:cell 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:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   Gene3D; 2.60.120.260; -; 1.
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; PTHR43925:SF2; PTHR43925:SF2; 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 junction; Cell membrane; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1310       Contactin-associated protein-like 4.
FT                                /FTId=PRO_0000019511.
FT   TOPO_DOM     28   1243       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1244   1264       Helical. {ECO:0000255}.
FT   TOPO_DOM   1265   1310       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       33    179       F5/8 type C. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00081}.
FT   DOMAIN      214    346       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      400    529       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      551    588       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      589    794       Fibrinogen C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00739}.
FT   DOMAIN      795    960       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      960    999       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1048   1204       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   CARBOHYD    262    262       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    287    287       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    540    540       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    576    576       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    604    604       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    639    639       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    708    708       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    750    750       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1019   1019       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1025   1025       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1075   1075       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     33    179       {ECO:0000250}.
FT   DISULFID    334    366       {ECO:0000250}.
FT   DISULFID    517    549       {ECO:0000250}.
FT   DISULFID    555    566       {ECO:0000250}.
FT   DISULFID    560    575       {ECO:0000250}.
FT   DISULFID    577    587       {ECO:0000250}.
FT   DISULFID    933    960       {ECO:0000250}.
FT   DISULFID    964    977       {ECO:0000250}.
FT   DISULFID    971    986       {ECO:0000250}.
FT   DISULFID    988    998       {ECO:0000250}.
FT   DISULFID   1169   1204       {ECO:0000250}.
FT   CONFLICT    993    993       Y -> F (in Ref. 1; AAG52890).
FT                                {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
//
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