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CTP5C_RAT
ID   CTP5C_RAT               Reviewed;        1307 AA.
AC   Q0V8T4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Contactin-associated protein like 5-3;
DE   AltName: Full=Cell recognition molecule Caspr5-3;
DE   AltName: Full=Cell recognition molecule Caspr5c;
DE   AltName: Full=Contactin-associated protein-like 5c;
DE   Flags: Precursor;
GN   Name=Cntnap5c; Synonyms=Caspr5-3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(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   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; AABR03084915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03084985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03085702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03086240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03086399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03086675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03086698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03086915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03087310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000870; CAJ55732.1; -; mRNA.
DR   RefSeq; NP_001041338.1; NM_001047873.1.
DR   AlphaFoldDB; Q0V8T4; -.
DR   SMR; Q0V8T4; -.
DR   STRING; 10116.ENSRNOP00000040012; -.
DR   GlyGen; Q0V8T4; 5 sites.
DR   PaxDb; Q0V8T4; -.
DR   GeneID; 301650; -.
DR   KEGG; rno:301650; -.
DR   UCSC; RGD:1565194; rat.
DR   CTD; 241175; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   InParanoid; Q0V8T4; -.
DR   OrthoDB; 338397at2759; -.
DR   PhylomeDB; Q0V8T4; -.
DR   PRO; PR:Q0V8T4; -.
DR   Proteomes; UP000002494; 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:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR001881; EGF-like_Ca-bd_dom.
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; SM00179; EGF_CA; 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; Glycoprotein; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1307
FT                   /note="Contactin-associated protein like 5-3"
FT                   /id="PRO_0000317383"
FT   TOPO_DOM        25..1238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1239..1259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1260..1307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..175
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          181..361
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          368..545
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          547..584
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          585..792
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DOMAIN          793..958
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          959..997
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1019..1200
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        600
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        330..361
FT                   /evidence="ECO:0000250"
FT   DISULFID        513..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        551..562
FT                   /evidence="ECO:0000250"
FT   DISULFID        556..571
FT                   /evidence="ECO:0000250"
FT   DISULFID        573..583
FT                   /evidence="ECO:0000250"
FT   DISULFID        931..958
FT                   /evidence="ECO:0000250"
FT   DISULFID        962..975
FT                   /evidence="ECO:0000250"
FT   DISULFID        969..984
FT                   /evidence="ECO:0000250"
FT   DISULFID        986..996
FT                   /evidence="ECO:0000250"
FT   DISULFID        1165..1200
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1307 AA;  145719 MW;  BA9E0BED62A92660 CRC64;
     MDFVPRLNSV LTLVLSGLWH FGLTATNCDN CDDPLASFLS LRAFSSSSDV TGSSSPAHLN
     WRMGTGGWSP AYSNAQQWLQ IDLGNRVEIT AVATQGRYGS SDWVTSYRLM FSDTGHNWQE
     YKQEDNIWTF VGNMNADSVV HHKLLHSVRA RFVRFVPLKW NPDGKIGMRM EVYGCSYRSD
     VADFDGHSSL LYRFNQKTMS TLKDMISLKF KSMQGDGVLL HGEGQRGDYI TLELQNGRLA
     LYLNLDGGQA RLSSIAPSAI LGSLLDDQQW HSVLLERVGK QTNFTVDTNT EHFQIKAETD
     ALDIDYELSF GGIPIPSKPG TFLKKSFHGC IENLYYNGVN IIDLAKRRKH QIYSGNVTFS
     CSEPQIVPIT FVNSRSSYLL LPGTPRIDGL SVSFQFRTWN EDGLLLSTEL SESSGTLLLI
     LEGGTLRLLI KKVAGHGTEI ITGSGLNDGL WHFVSINARR NRVTLTLDND AASLPPDISW
     LQIYSGNSYY FGGCPDNLTD SQCLNPIKAF QGCMRLIFID NQPKDLISVQ QGSLGNFSDL
     HIDLCSIKDR CLPNYCEHGG HCVQTWTTFY CNCSNTGYTG ATCHDSIYEQ SCEVYRHRGN
     NTSGFFFVDS DGSGPLEPLQ LYCNITEDKI WMTIQHNITE LTQVQGSNAE KPYSMTLNYG
     GSMDQLVALI DGSEYCEQEV TYHCRRSRLL NTPDGAPFTW WIGRSNEKHH YWGGSVPGIQ
     KCGCGLEQSC LDIGHFCNCD ADTDEWANDT GFLSFKDHLP VTQIIITDTN RSNSEAAWRI
     GPLRCYGDRH FWNAVSFSTE ASYLHFPTSH VEFSIDISFF FKTTALSGVF IENLGIKDFL
     RLELSSPSEV TFAIDVGNGP TELLVQSPSP LNDNQWHYIQ AERNLKETSL QVDNFPRIMR
     ETTEKGHFQL QLNSQMFVGG TSSRQKGFLG CIRSLHLNGQ NIDLEERGMV TSGVRPGCPG
     HCSSYGNNCH NGGKCVEKHN SYSCDCTKSP YEGPFCQKEI SALFDSTTSI TYMFQEPYPV
     SKNTSTSSSA IYTDTVLSKE TILLSFVTAQ APTLLLYLNF STPSFLALLL SRNGSLQILY
     HLSKGESHMF TVSTENLANR RVHHVKMNRD GTELSIQMDQ QLFSYNFPLE AEFLTVRSLI
     LGKVTETLGL DPRVARANSL GFIGCLSSVQ YNHIAPLKAA LRHASIAPAT VQGSLREFSC
     GSMVDSDVNA VTTVYSSSDP FGKTDDHDPL TNAVLSDSAV IGGVIAVVTF ITFCVIGIMT
     RFLYQHKQSH CTSQKKEKEY SENLDSSFRH DIDLQSTTSK CKREYFI
 
 
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