CNTP5_HUMAN
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 03-AUG-2022, entry version 138.
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}.
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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 GlyGen; Q8WYK1; 5 sites.
DR iPTMnet; Q8WYK1; -.
DR PhosphoSitePlus; Q8WYK1; -.
DR BioMuta; CNTNAP5; -.
DR DMDM; 74716461; -.
DR MassIVE; Q8WYK1; -.
DR PaxDb; Q8WYK1; -.
DR PeptideAtlas; Q8WYK1; -.
DR PRIDE; Q8WYK1; -.
DR ProteomicsDB; 75163; -.
DR Antibodypedia; 33412; 20 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 CTD; 129684; -.
DR DisGeNET; 129684; -.
DR GeneCards; CNTNAP5; -.
DR HGNC; HGNC:18748; CNTNAP5.
DR HPA; ENSG00000155052; Tissue enriched (brain).
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; GVEPITH; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q8WYK1; -.
DR TreeFam; TF321823; -.
DR PathwayCommons; Q8WYK1; -.
DR SignaLink; Q8WYK1; -.
DR BioGRID-ORCS; 129684; 6 hits in 1059 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 cortical plate and 69 other tissues.
DR Genevisible; Q8WYK1; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR028874; Caspr5.
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:SF70; PTHR15036:SF70; 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; 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 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
