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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}.
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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
 
 
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