ID CNTP5_HUMAN Reviewed; 1306 AA. AC Q8WYK1; Q4ZFW2; Q4ZG21; Q53R09; Q53RX1; Q53SG3; Q584P3; Q96MS7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 24-JAN-2024, entry version 144. DE RecName: Full=Contactin-associated protein-like 5; DE AltName: Full=Cell recognition molecule Caspr5; DE Flags: Precursor; GN Name=CNTNAP5; Synonyms=CASPR5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Takeuchi K., Watanabe N., Kawano T., Kawamura K.; RT "In vitro and in vivo studies on the involvement of neural cell adhesion RT molecules and chondroitin sulfate proteoglycans in defining discrete axonal RT pathways of the rat cerebral cortex."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). CC -!- FUNCTION: May play a role in the correct development and proper CC functioning of the peripheral and central nervous system and be CC involved in cell adhesion and intercellular communication. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}. 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 EMBL; AB077881; BAB83897.1; -; mRNA. DR EMBL; AC019105; AAY14716.1; -; Genomic_DNA. DR EMBL; AC019159; AAX88894.1; -; Genomic_DNA. DR EMBL; AC074362; AAX81997.1; -; Genomic_DNA. DR EMBL; AC079154; AAY15042.1; -; Genomic_DNA. DR EMBL; AC097715; AAY24250.1; -; Genomic_DNA. DR EMBL; AC104648; AAX88904.1; -; Genomic_DNA. DR EMBL; CH471103; EAW95266.1; -; Genomic_DNA. DR EMBL; AK056528; BAB71205.1; -; mRNA. DR CCDS; CCDS46401.1; -. DR RefSeq; NP_570129.1; NM_130773.3. DR AlphaFoldDB; Q8WYK1; -. DR SMR; Q8WYK1; -. DR BioGRID; 126204; 2. DR IntAct; Q8WYK1; 1. DR STRING; 9606.ENSP00000399013; -. DR GlyCosmos; Q8WYK1; 5 sites, No reported glycans. DR GlyGen; Q8WYK1; 5 sites. DR iPTMnet; Q8WYK1; -. DR PhosphoSitePlus; Q8WYK1; -. DR BioMuta; CNTNAP5; -. DR DMDM; 74716461; -. DR MassIVE; Q8WYK1; -. DR PaxDb; 9606-ENSP00000399013; -. DR PeptideAtlas; Q8WYK1; -. DR ProteomicsDB; 75163; -. DR Antibodypedia; 33412; 22 antibodies from 7 providers. DR DNASU; 129684; -. DR Ensembl; ENST00000431078.1; ENSP00000399013.1; ENSG00000155052.15. DR GeneID; 129684; -. DR KEGG; hsa:129684; -. DR UCSC; uc002tno.5; human. DR AGR; HGNC:18748; -. DR CTD; 129684; -. DR DisGeNET; 129684; -. DR GeneCards; CNTNAP5; -. DR HGNC; HGNC:18748; CNTNAP5. DR HPA; ENSG00000155052; Group enriched (brain, retina). DR MIM; 610519; gene. DR neXtProt; NX_Q8WYK1; -. DR OpenTargets; ENSG00000155052; -. DR PharmGKB; PA134898715; -. DR VEuPathDB; HostDB:ENSG00000155052; -. DR eggNOG; KOG3516; Eukaryota. DR GeneTree; ENSGT00940000160532; -. DR HOGENOM; CLU_003504_1_0_1; -. DR InParanoid; Q8WYK1; -. DR OMA; CIVAIMS; -. DR OrthoDB; 4255614at2759; -. DR PhylomeDB; Q8WYK1; -. DR TreeFam; TF321823; -. DR PathwayCommons; Q8WYK1; -. DR SignaLink; Q8WYK1; -. DR BioGRID-ORCS; 129684; 8 hits in 1137 CRISPR screens. DR ChiTaRS; CNTNAP5; human. DR GenomeRNAi; 129684; -. DR Pharos; Q8WYK1; Tbio. DR PRO; PR:Q8WYK1; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8WYK1; Protein. DR Bgee; ENSG00000155052; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 69 other cell types or tissues. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. 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; 1. 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:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 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; 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; PS01286; FA58C_2; 1. DR PROSITE; PS50022; FA58C_3; 1. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 4. DR Genevisible; Q8WYK1; HS. PE 2: Evidence at transcript level; KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Membrane; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..1306 FT /note="Contactin-associated protein-like 5" FT /id="PRO_0000317377" FT TOPO_DOM 25..1237 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1238..1258 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1259..1306 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..174 FT /note="F5/8 type C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DOMAIN 180..360 FT /note="Laminin G-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 367..544 FT /note="Laminin G-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 546..583 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 584..790 FT /note="Fibrinogen C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739" FT DOMAIN 791..956 FT /note="Laminin G-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT DOMAIN 957..995 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1013..1199 FT /note="Laminin G-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122" FT CARBOHYD 282 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 496 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 571 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 622 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 30..174 FT /evidence="ECO:0000250" FT DISULFID 329..360 FT /evidence="ECO:0000250" FT DISULFID 512..544 FT /evidence="ECO:0000250" FT DISULFID 550..561 FT /evidence="ECO:0000250" FT DISULFID 555..570 FT /evidence="ECO:0000250" FT DISULFID 572..582 FT /evidence="ECO:0000250" FT DISULFID 929..956 FT /evidence="ECO:0000250" FT DISULFID 960..973 FT /evidence="ECO:0000250" FT DISULFID 967..982 FT /evidence="ECO:0000250" FT DISULFID 984..994 FT /evidence="ECO:0000250" FT DISULFID 1164..1199 FT /evidence="ECO:0000250" FT VARIANT 452 FT /note="S -> L (in dbSNP:rs17727261)" FT /id="VAR_038518" FT VARIANT 1195 FT /note="T -> M (in dbSNP:rs34165507)" FT /id="VAR_038519" FT CONFLICT 353 FT /note="T -> TV (in Ref. 4; BAB71205)" FT /evidence="ECO:0000305" FT CONFLICT 449 FT /note="L -> P (in Ref. 4; BAB71205)" FT /evidence="ECO:0000305" FT CONFLICT 957..962 FT /note="PGHCSS -> SIKKLK (in Ref. 4; BAB71205)" FT /evidence="ECO:0000305" SQ SEQUENCE 1306 AA; 145623 MW; 132F8B1D9200C68E CRC64; MDSLPRLTSV LTLLFSGLWH LGLTATNYNC DDPLASLLSP MAFSSSSDLT GTHSPAQLNW RVGTGGWSPA DSNAQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYSLMF SDTGRNWKQY KQEDSIWTFA GNMNADSVVH HKLLHSVRAR FVRFVPLEWN PSGKIGMRVE VYGCSYKSDV ADFDGRSSLL YRFNQKLMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL HLNLGDSKAR LSSSLPSATL GSLLDDQHWH SVLIERVGKQ VNFTVDKHTQ HFRTKGETDA LDIDYELSFG GIPVPGKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYTGNVTFSC SEPQIVPITF VNSSGSYLLL PGTPQIDGLS VSFQFRTWNK DGLLLSTELS EGSGTLLLSL EGGILRLVIQ KMTERVAEIL TGSNLNDGLW HSVSINARRN RITLTLDDEA APPAPDSTWV QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH IDLCSIKDRC LPNYCEHGGS CSQSWTTFYC NCSDTSYTGA TCHNSIYEQS CEVYRHQGNT AGFFYIDSDG SGPLGPLQVY CNITEDKIWT SVQHNNTELT RVRGANPEKP YAMALDYGGS MEQLEAVIDG SEHCEQEVAY HCRRSRLLNT PDGTPFTWWI GRSNERHPYW GGSPPGVQQC ECGLDESCLD IQHFCNCDAD KDEWTNDTGF LSFKDHLPVT QIVITDTDRS NSEAAWRIGP LRCYGDRRFW NAVSFYTEAS YLHFPTFHAE FSADISFFFK TTALSGVFLE NLGIKDFIRL EISSPSEITF AIDVGNGPVE LVVQSPSLLN DNQWHYVRAE RNLKETSLQV DNLPRSTRET SEEGHFRLQL NSQLFVGGTS SRQKGFLGCI RSLHLNGQKM DLEERAKVTS GVRPGCPGHC SSYGSICHNG GKCVEKHNGY LCDCTNSPYE GPFCKKEVSA VFEAGTSVTY MFQEPYPVTK NISLSSSAIY TDSAPSKENI ALSFVTTQAP SLLLFINSSS QDFVVVLLCK NGSLQVRYHL NKEETHVFTI DADNFANRRM HHLKINREGR ELTIQMDQQL RLSYNFSPEV EFRVIRSLTL GKVTENLGLD SEVAKANAMG FAGCMSSVQY NHIAPLKAAL RHATVAPVTV HGTLTESSCG FMVDSDVNAV TTVHSSSDPF GKTDEREPLT NAVRSDSAVI GGVIAVVIFI IFCIIGIMTR FLYQHKQSHR TSQMKEKEYP ENLDSSFRNE IDLQNTVSEC KREYFI //