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CTP5C_MOUSE
ID   CTP5C_MOUSE             Reviewed;        1305 AA.
AC   Q0V8T7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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. {ECO:0000269|PubMed:16845472}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 6 dpc in brain.
CC       {ECO:0000269|PubMed:16845472}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR   EMBL; AC118684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT025622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT025736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000867; CAJ55747.1; -; mRNA.
DR   CCDS; CCDS37671.1; -.
DR   RefSeq; NP_001075122.1; NM_001081653.1.
DR   AlphaFoldDB; Q0V8T7; -.
DR   SMR; Q0V8T7; -.
DR   STRING; 10090.ENSMUSP00000075416; -.
DR   GlyConnect; 2234; 3 N-Linked glycans (1 site).
DR   GlyGen; Q0V8T7; 5 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; Q0V8T7; -.
DR   PhosphoSitePlus; Q0V8T7; -.
DR   MaxQB; Q0V8T7; -.
DR   PaxDb; Q0V8T7; -.
DR   PRIDE; Q0V8T7; -.
DR   ProteomicsDB; 285414; -.
DR   DNASU; 620292; -.
DR   Ensembl; ENSMUST00000076038; ENSMUSP00000075416; ENSMUSG00000038048.
DR   GeneID; 620292; -.
DR   KEGG; mmu:620292; -.
DR   UCSC; uc008dew.1; mouse.
DR   CTD; 620292; -.
DR   MGI; MGI:3646013; Cntnap5c.
DR   VEuPathDB; HostDB:ENSMUSG00000038048; -.
DR   eggNOG; KOG3516; Eukaryota.
DR   GeneTree; ENSGT00940000164023; -.
DR   HOGENOM; CLU_003504_1_0_1; -.
DR   InParanoid; Q0V8T7; -.
DR   OMA; SHYICNG; -.
DR   OrthoDB; 338397at2759; -.
DR   PhylomeDB; Q0V8T7; -.
DR   TreeFam; TF321823; -.
DR   BioGRID-ORCS; 620292; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Cntnap5c; mouse.
DR   PRO; PR:Q0V8T7; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q0V8T7; protein.
DR   Bgee; ENSMUSG00000038048; Expressed in pyramidal layer of CA1 and 15 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProt.
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; 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   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..1305
FT                   /note="Contactin-associated protein like 5-3"
FT                   /id="PRO_0000317380"
FT   TOPO_DOM        25..1235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1236..1256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1257..1305
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..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          1013..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        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        571
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1023
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1057
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  146242 MW;  623EB2D81A4D9953 CRC64;
     MDSVPRLNSV FTLVLSGLWH FGLTATNYNC DDPLTSFLSL RAFSSSSDLT GRSSPAQLNW
     RMGTGGWSPA DSNAQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYRLMF SDTGHNWQQY
     TQEGSIWRFV GNMNANSVVH HKLLNSVRAR FVRFVPLEWN PNGKIGMRVE VYGCSYRSDV
     ADFDGWSSLL YRFNQKTMST LKDVISLKFK SIQRDGVLFH GEGQRGDHIT LELQNGRLAL
     YLNLDDSKAQ VSSTAPLATL GSLLDDQHWH SVLLERVGKQ ANFTVDKNTQ HFQTKGETDA
     LDIDYELSFG GIPVPSKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYSGNVTFSC
     SEPQTVPITF VNSRSSYLLL TGTPQIDGLS VSFQFRTWNE DGLLLSTELS EGSGTLLLIL
     EGGTLRLLIK KLARHGTEIF TGSGLNDGMW HSVSISARRN RVTLTLDNDA ASLPPDTSWL
     QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGSFSDLH
     IDLCSIKDRC LPNYCEHGGQ CAQTWTNFYC NCSDTGYTGA TCHDSIYEQS CEVYRHRGKT
     AEFFYVDSDG SGPLGPLQVF CNITEDKIWM TVQHNNTGLT WVQGSNPEKP YAMTLNYGGS
     LEQLEALIDG SEHCEQEVTY YCKRSRLLNT PDGVPFTWWI GRSNEKHPYW GGSLPGVQQC
     GCGLEESCLD IRHFCNCDAD TDEWTNDTGY LSFKDHLPVT QIIITDTNRS KSEAAWRIGP
     LRCYGDRHFW NAVSFSTEAS FLHFPTFRVE FSADIFFFFK TTALSGVFLE ILGIKDFLRL
     EMSSPSEVIF AIDVGNGPID LLVQSPYPLN DNQWHYIRAE RNLKETSLQV DNLPQSMREA
     SEEGHFQFQL NSQLFVGGKS SRQKGFFGCI RSLHLNGQNI DLEERAKVTS GVRPGCPGHC
     SSYGRNCQNG GKCVEKHIGY SCDCTNSPYE GPFCQKEISA LFDSDTSVTY MFQEPYSVTK
     NTNLSSSAIY TDTAPSKEII MLSFMTAQAP TLLLYLNFSS QNFLAILLSW NGSLQIHYQL
     SKEESHVFTI NTENLANRRV HQVKMSRDGP ELSIQMDQQL FSYTFSLESE FQRARSLVLG
     KVTETLGLDP EVARANTLGF VGCLSSVQYN HITPLKAALR HASISPVTVQ RTLTESSCVS
     MVDSDANAVT TVYSSTDPFG ERDEREPLTN AVPSDLAVIG GIIAVVTFIS FSVIGIMTHF
     FYQHKRSHYA SQMKEKEYPE NVDSSSRNDI DLQNTTRECK QEDFI
 
 
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