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 27-MAR-2024, entry version 97.
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 GlyCosmos; Q0V8T4; 5 sites, No reported glycans.
DR GlyGen; Q0V8T4; 5 sites.
DR PhosphoSitePlus; Q0V8T4; -.
DR PaxDb; 10116-ENSRNOP00000040012; -.
DR GeneID; 301650; -.
DR KEGG; rno:301650; -.
DR UCSC; RGD:1565194; rat.
DR AGR; RGD:1565194; -.
DR CTD; 241175; -.
DR eggNOG; KOG3516; Eukaryota.
DR InParanoid; Q0V8T4; -.
DR OrthoDB; 4255614at2759; -.
DR PhylomeDB; Q0V8T4; -.
DR PRO; PR:Q0V8T4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
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:SF46; CONTACTIN-ASSOCIATED PROTEIN-LIKE 5; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 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; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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
//
