CNTP5_CANLF
ID CNTP5_CANLF Reviewed; 1305 AA.
AC Q0V8T0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Contactin-associated protein-like 5;
DE AltName: Full=Cell recognition molecule Caspr5;
DE Flags: Precursor;
GN Name=CNTNAP5; Synonyms=CASPR5;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=16845472; DOI=10.1007/s00335-005-0157-1;
RA Traut W., Weichenhan D., Himmelbauer H., Winking H.;
RT "New members of the neurexin superfamily: multiple rodent homologues of the
RT human CASPR5 gene.";
RL Mamm. Genome 17:723-731(2006).
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; AAEX02006971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX02006977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000917; CAJ77882.1; -; mRNA.
DR RefSeq; NP_001041573.1; NM_001048108.1.
DR AlphaFoldDB; Q0V8T0; -.
DR SMR; Q0V8T0; -.
DR STRING; 9612.ENSCAFP00000006992; -.
DR PaxDb; Q0V8T0; -.
DR PRIDE; Q0V8T0; -.
DR GeneID; 483874; -.
DR KEGG; cfa:483874; -.
DR CTD; 129684; -.
DR eggNOG; KOG3516; Eukaryota.
DR InParanoid; Q0V8T0; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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; PF00008; EGF; 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 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..1305
FT /note="Contactin-associated protein-like 5"
FT /id="PRO_0000317376"
FT TOPO_DOM 25..1236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1258..1305
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 1000..1198
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 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 1163..1198
FT /evidence="ECO:0000250"
SQ SEQUENCE 1305 AA; 145560 MW; 63A6D9B707D72231 CRC64;
MDSVPRLTGV FTLLLSGLWH LGSSATNYNC DDPLASLLSP MAFSSSSDLT GTHSPAQLNR
RVGTGGWSPA DSNAQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYSLMF SDTGRNWKQY
KQEDSIWTFA GNMNADSVMH HKLLHSVRAR FVRFVPLEWN PSGKIGMRVE VYGCSYKSDV
ADFDGRSSLL YRFNQKLMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL
HLNLDDSKPR LSSSPPSVTL GSLLDDQQWH SVLIERVGKQ VNFSVDKHTQ HFRTKGEADA
LDIDYELSFG GIPVPGKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYTGNVTFSC
SEPQIVPITF VNSSSSYLLL PGTPQIDGLS VSFQFRTWNK DGLLLSTELS EGSGTLLLSL
EGGTVRLVIQ KMTERTAEIL TGSSLNDGLW HSVSINARRD RITLSLDNDA ASPAQDTTRV
QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH
IDLCSIKDRC LPNYCEHGGF CSQSWTTFYC NCSNTGYTGA TCHNSLYEQS CEVYRHQGNT
AGFFYIDSDG SGPLGPLQVY CNITEDKIWT SVQHNNTELT HVRGANPEKP YTMALDYGGS
MEQLEAMIDS SEHCEQEVAY HCRRSRLLNT PDGTPFTWWI GRSNEKHPYW GGAPPGVQQC
ECGLDESCLD VRHFCNCDAD KDEWTNDTGF LSFKDHLPVT QIVITDTNRS NSEAAWRIGP
LRCYGDRHFW NAVSFYTEAS YLHFPTFHAE FSADISFFFK TTALSGVFLE NLGIKDFIRL
EISSPSEITF AIDVGNGPVE LIVHSPSLLN DNQWHYIRAE RNLKETSLQV DSLPRMTRET
SEEGHFRLQL NSQLFVGGTS SRQKGFLGCI RSLHLNGQKL DLEERAKVTS GVRPGCPGHC
STYGSICHNG GKCVEKYSGY FCDCTNSPYE GPFCKKEVSA VFEAGTSVTY MFQEPYPVTK
NISLSSSAIY ADAAPSKENI AFSFVTAQAP SLLLYINSSQ DYLAVLLCKN GSLQVRYQLS
KEETQVFNID AENFANRRMH HLKINREGRE LAIQVDHQLR LSYNFSSEVE FRAIRSLTLG
KVREHLGLDS EIAKANTLGF VGCLSSVQYN QVAPLKAALR HATIAPVTVQ GTLMESSCGS
MVDVDVNTVT TVHSSSDPFG KTDEREPLTN AVRSDSAVIG GVIAVVIFII FSIIGIMTRF
LYQHKQSHRT NQMKEKEYPE NLDSSFRNDI DLQNTVSECK REYFI
