CNTP5_CHICK
ID CNTP5_CHICK Reviewed; 1305 AA.
AC Q0V8S9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Contactin-associated protein-like 5;
DE AltName: Full=Cell recognition molecule Caspr5;
DE Flags: Precursor;
GN Name=CNTNAP5; Synonyms=CASPR5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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 -!- TISSUE SPECIFICITY: Expressed in brain.
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; BN000918; CAJ77883.1; -; mRNA.
DR RefSeq; NP_001041544.1; NM_001048079.1.
DR AlphaFoldDB; Q0V8S9; -.
DR SMR; Q0V8S9; -.
DR STRING; 9031.ENSGALP00000018862; -.
DR PaxDb; Q0V8S9; -.
DR PRIDE; Q0V8S9; -.
DR GeneID; 424231; -.
DR KEGG; gga:424231; -.
DR CTD; 129684; -.
DR VEuPathDB; HostDB:geneid_424231; -.
DR eggNOG; KOG3516; Eukaryota.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q0V8S9; -.
DR PhylomeDB; Q0V8S9; -.
DR PRO; PR:Q0V8S9; -.
DR Proteomes; UP000000539; Unplaced.
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; 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; 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 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; EGF-like domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1305
FT /note="Contactin-associated protein-like 5"
FT /id="PRO_0000317385"
FT TOPO_DOM 23..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 23..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 1017..1198
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
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; 145614 MW; 237DC6C2E9A78B3E CRC64;
MDSPALGAVA LLLAGFWHLG LTATNYNCDG ALVSTLPSSA FTSSSEFFST HSPSFAKLNR
RDGAGGWSPL DSNEQQWLQV DLGDRVEIVG VATQGRYGSS DWVTSYTLMF SDTGRNWKQY
RKDDTVWVFT GNSNADSVVH HKLLHSMKAR FLRFVPLKWN VGGHIGLRVE VFGCSYKSDI
ADFDGRSSLL YRFNQKLMST FKDVVSLKFK SMQEDGVLFH GEGQRGDYIT LELQKGKLSL
HINLGDSNLH FTNSHTSVTL GSLLDDQHWH SVLIERFNKQ VNFTVDKHTQ HFRTKGDSDH
LDIDYELSFG GIPVPGKPGT FQRKNFHGCI ENLYYNGVNI IDLAKRRKPQ IYTGNVTFSC
SEPQIVPITF VSSSRSYLLL PGTPQIDGLS VSFQFRTWNK DGLLLSTELS ENSGSLLVYL
HGGRLTLLIQ KVAEDPVEIS EGTNLHDGLW HSLNINARRH RITLTLDNNA ATASHATTVS
RIYSGNSYYF GGCPDNFTDS QCLNPITAFQ GCMRLIFIDN QPKDLILVQQ GSLGNFSDLH
IDLCDIKDRC LPNYCEHGGK CSQSWTTFYC DCNDTSYMGA TCHNSIYEQS CEAYRHQGKT
SDFFYIDSDG SGPLGPLRVF CNITEDKIWT AVQHNNTGLT RVQGAGPEKP YTMSFNYNSS
AEQLEAVINS AEYCEQEAAY HCKKSRLLNT PNGIPFAWWV GRANEKHLYW GGSLPGIQQC
ACGLEESCLD MRYFCNCDAD REEWTNDTGL LAFKDHLPVT QIVITDTNRS NSEAAWKIGP
LHCYGDRQFW NAASFNTEAS YLHFPTFHAE VSADISFFFK TTSLSGVFLE NLGMKDFIRV
EIRSPKEITF SIDVGNGPTE ATVQSPTPLN DNQWHYVRAE RNLKQTSLQV DNLPKKVLEA
PAEGHFRLQL NSQLFVGGTA SRQKGFLGCI RSLHLNGQKL DLEERAKMTP GVKPGCPGHC
SSYGNLCHNG GKCVEKYNGY SCDCTSSAYE GPFCKEEVSA LFEAGTSITY IFQEPYPVTK
NASTSSSAIY ADAITSKENI AFSFLTAHAP SLLLYINTYF HEYLAVILSK NGSLQVRYKL
SKDGLLIFTI DSGNFANREM HHVKINREGR ELIIQVDQVI KLKHNFSEID FKAIKSLTLG
KVTDSLPLDP EVSKANAYGF TGCMSSVWYN HVAPLKAALR HPSIAPVTVK GSLTESSCSS
LMETDVNTAT TIYSSSDPFG KTDEREPLTN AVRSDSAVIG GVIAVVIFII FCIIAIMSRF
LYQHKQAHRS SQTKEKEYPE NLESSFKADI DLQNTVSECK REYFI