ID A0A8I6GH02_RAT Unreviewed; 1332 AA. AC A0A8I6GH02; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 02-OCT-2024, entry version 14. DE SubName: Full=Contactin associated protein 2 {ECO:0000313|Ensembl:ENSRNOP00000088343.1}; GN Name=Cntnap2 {ECO:0000313|RGD:1307076}; GN Synonyms=AABR07060487.1 {ECO:0000313|Ensembl:ENSRNOP00000088343.1}; 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 {ECO:0000313|Ensembl:ENSRNOP00000088343.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000088343.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000088343.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000088343.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000088343.1}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell junction, paranodal septate junction CC {ECO:0000256|ARBA:ARBA00004403}. CC -!- SIMILARITY: Belongs to the neurexin family. CC {ECO:0000256|ARBA:ARBA00010241}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR Ensembl; ENSRNOT00000008688.8; ENSRNOP00000088343.1; ENSRNOG00000006617.8. DR AGR; RGD:1307076; -. DR AGR; RGD:15003315; -. DR RGD; 15003315; AABR07060487.1. DR RGD; 1307076; Cntnap2. DR GeneTree; ENSGT00940000154516; -. DR OMA; SRVQFNH; -. DR Proteomes; UP000002494; Chromosome 4. DR GO; GO:0030673; C:axolemma; IDA:RGD. DR GO; GO:0030424; C:axon; ISO:RGD. DR GO; GO:0043194; C:axon initial segment; ISO:RGD. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0150048; C:cerebellar granule cell to Purkinje cell synapse; ISO:RGD. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0005769; C:early endosome; ISO:RGD. DR GO; GO:0060076; C:excitatory synapse; ISO:RGD. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD. DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:RGD. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0044309; C:neuron spine; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell. DR GO; GO:0033270; C:paranode region of axon; IDA:RGD. DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD. DR GO; GO:0098794; C:postsynapse; ISO:RGD. DR GO; GO:0098793; C:presynapse; ISO:RGD. DR GO; GO:0048787; C:presynaptic active zone membrane; ISO:RGD. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:0097060; C:synaptic membrane; IDA:RGD. DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD. DR GO; GO:0002020; F:protease binding; IPI:RGD. DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD. DR GO; GO:0099610; P:action potential initiation; ISO:RGD. DR GO; GO:0030534; P:adult behavior; ISO:RGD. DR GO; GO:0008306; P:associative learning; ISO:RGD. DR GO; GO:0007409; P:axonogenesis; ISO:RGD. DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD. DR GO; GO:0008283; P:cell population proliferation; ISO:RGD. DR GO; GO:0022010; P:central nervous system myelination; ISO:RGD. DR GO; GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; ISO:RGD. DR GO; GO:0021549; P:cerebellum development; ISO:RGD. DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD. DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD. DR GO; GO:0042745; P:circadian sleep/wake cycle; ISO:RGD. DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISO:RGD. DR GO; GO:0140059; P:dendrite arborization; ISO:RGD. DR GO; GO:0060996; P:dendritic spine development; ISO:RGD. DR GO; GO:0097062; P:dendritic spine maintenance; ISO:RGD. DR GO; GO:0097061; P:dendritic spine organization; ISO:RGD. DR GO; GO:1990403; P:embryonic brain development; ISO:RGD. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0098976; P:excitatory chemical synaptic transmission; ISO:RGD. DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD. DR GO; GO:1904861; P:excitatory synapse assembly; ISO:RGD. DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD. DR GO; GO:0010467; P:gene expression; ISO:RGD. DR GO; GO:0014009; P:glial cell proliferation; ISO:RGD. DR GO; GO:1905962; P:glutamatergic neuron differentiation; ISO:RGD. DR GO; GO:0007625; P:grooming behavior; ISO:RGD. DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD. DR GO; GO:0006954; P:inflammatory response; ISO:RGD. DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; ISO:RGD. DR GO; GO:1904862; P:inhibitory synapse assembly; ISO:RGD. DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD. DR GO; GO:0007612; P:learning; ISO:RGD. DR GO; GO:0021761; P:limbic system development; ISO:RGD. DR GO; GO:0045475; P:locomotor rhythm; ISO:RGD. DR GO; GO:0007626; P:locomotory behavior; ISO:RGD. DR GO; GO:0099558; P:maintenance of synapse structure; ISO:RGD. DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD. DR GO; GO:0061744; P:motor behavior; ISO:RGD. DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD. DR GO; GO:0042552; P:myelination; ISO:RGD. DR GO; GO:1904456; P:negative regulation of neuronal action potential; ISO:RGD. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD. DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:RGD. DR GO; GO:0061351; P:neural precursor cell proliferation; ISO:RGD. 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:0050884; P:neuromuscular process controlling posture; ISO:RGD. DR GO; GO:0031175; P:neuron projection development; ISO:RGD. DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD. DR GO; GO:0019228; P:neuronal action potential; ISO:RGD. DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:RGD. DR GO; GO:1904457; P:positive regulation of neuronal action potential; ISO:RGD. DR GO; GO:0097106; P:postsynaptic density organization; ISO:RGD. DR GO; GO:0060134; P:prepulse inhibition; IMP:RGD. DR GO; GO:0008104; P:protein localization; ISO:RGD. DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISO:RGD. DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:RGD. DR GO; GO:0002021; P:response to dietary excess; ISO:RGD. DR GO; GO:0009408; P:response to heat; ISO:RGD. DR GO; GO:0009725; P:response to hormone; ISO:RGD. DR GO; GO:0097396; P:response to interleukin-17; ISO:RGD. DR GO; GO:0009642; P:response to light intensity; ISO:RGD. DR GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD. DR GO; GO:1901558; P:response to metformin; ISO:RGD. DR GO; GO:1990834; P:response to odorant; ISO:RGD. DR GO; GO:0048265; P:response to pain; ISO:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD. DR GO; GO:0007622; P:rhythmic behavior; ISO:RGD. DR GO; GO:0035176; P:social behavior; ISO:RGD. DR GO; GO:0001964; P:startle response; IMP:RGD. DR GO; GO:0021756; P:striatum development; ISO:RGD. DR GO; GO:0071109; P:superior temporal gyrus development; ISO:RGD. DR GO; GO:0021794; P:thalamus development; ISO:RGD. DR GO; GO:0031929; P:TOR signaling; ISO:RGD. DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD. DR GO; GO:0042297; P:vocal learning; ISO:RGD. DR GO; GO:0071625; P:vocalization behavior; ISO:RGD. DR GO; GO:0090659; P:walking behavior; ISO:RGD. DR CDD; cd00054; EGF_CA; 2. DR CDD; cd00057; FA58C; 1. DR CDD; cd00110; LamG; 4. DR Gene3D; 2.60.120.1000; -; 1. DR Gene3D; 2.60.120.200; -; 4. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 2. 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 InterPro; IPR050372; Neurexin-related_CASP. DR NCBIfam; NF040941; GGGWT_bact; 1. DR PANTHER; PTHR15036:SF33; CONTACTIN-ASSOCIATED PROTEIN-LIKE 2; 1. DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1. DR Pfam; PF00754; F5_F8_type_C; 1. DR Pfam; PF02210; Laminin_G_2; 4. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00181; EGF; 2. DR SMART; SM00231; FA58C; 1. DR SMART; SM00282; LamG; 4. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4. DR SUPFAM; SSF57196; EGF/Laminin; 1. DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 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 3: Inferred from homology; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00122}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..1332 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5035182176" FT TRANSMEM 1263..1284 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 35..181 FT /note="F5/8 type C" FT /evidence="ECO:0000259|PROSITE:PS50022" FT DOMAIN 187..368 FT /note="Laminin G" FT /evidence="ECO:0000259|PROSITE:PS50025" FT DOMAIN 373..552 FT /note="Laminin G" FT /evidence="ECO:0000259|PROSITE:PS50025" FT DOMAIN 554..591 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 590..642 FT /note="Fibrinogen C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51406" FT DOMAIN 799..963 FT /note="Laminin G" FT /evidence="ECO:0000259|PROSITE:PS50025" FT DOMAIN 964..1002 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 1021..1215 FT /note="Laminin G" FT /evidence="ECO:0000259|PROSITE:PS50025" FT DISULFID 936..963 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122" SQ SEQUENCE 1332 AA; 148162 MW; 7B6FC914B2C7ED7F CRC64; MVISLRAGCR AALSLWILSS FICRAWTAPS SFQKCDEPLV SGLPHVSFSS SSSLSSSYAP GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT GRNWKPYHQD GNIWAFPGNV NSDSVVRHDL QHAVVARYVR IVPLDWNGEG HIGLRAEVYG CSYWADVINF DGHVVLPYRF RNKKMKTLKD VIALKFKTSE SEGVLLHGEG QQGDYITLEL KKAKLVFSLN LGSNQLGPIY GHTSVTSGSL LDDHHWHSVL IERQGRSINL TLDRSMQHFR TNGEFDYLDL DYEITFGGIP FSGKPSSSNR KNFKGCMESI NYNGVNITDL ARRKKLEPSN VGNLSFACVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPSGLL LFSHFADNLG NVEIDLVESK VGVHINTTQT KTSQIDISSG SGLNDGQWHE VRFLAKENFA VLTIDGDEAS AVRTNSPLQV KTGERYYFGG FLNHMNNASH SALQPSFQGC MQLIQVDDQL VNLYEVAQRK PGSFANVTID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTTV VGYNPEKYSV TQLIYSASMD QISAITSSAE YCEQYVSYFC KMSRLLNTPD GSPYTWWVGK ANEKHYYWGG SEPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL IPRGVFLENL GNTDFIKLEL KSSTEVSFSF DVGNGPVEIV VRSPSPLNDD QWHRVTAERN VKQASLQVDR LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFK SGCSGHCTSY GANCENGGKC IEKYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ ALTVTARDTG SRAENSADQQ QHLAPDLAQE QIHFSFSTTK APCILLYVSS LTTDFLAVLV KPTGNLQIRY NLGGTREPFN IDVDHRNMAN GQPHSVNITR HEKTIILKLD HYPAAGYHLP SSSDTIFNSP KSLFLGKVIE TGKIDQEIHK YNTPGFTGCL SRVQFNHIAP LKAALRQTNA SAHVHIQGDL VESNCGASPL TLSPMSSATD PWHLDHLDSA SADFPYNPGQ GQAIRNGVNR NSAIIGGVIA VVIFTILCTL VFLIRYMFRH KGTYHTNEAK GAESAESADA AIMNNDPNFT ETIDESKKEW LI //