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}.
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; 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