CTP5A_MOUSE
ID CTP5A_MOUSE Reviewed; 1304 AA.
AC Q0V8T9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Contactin-associated protein like 5-1;
DE AltName: Full=Cell recognition molecule Caspr5-1;
DE AltName: Full=Cell recognition molecule Caspr5a;
DE AltName: Full=Contactin-associated protein-like 5a;
DE Flags: Precursor;
GN Name=Cntnap5a; Synonyms=Caspr5-1;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AC098737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000865; CAJ55745.1; -; mRNA.
DR CCDS; CCDS35689.1; -.
DR RefSeq; NP_001070893.1; NM_001077425.1.
DR AlphaFoldDB; Q0V8T9; -.
DR SMR; Q0V8T9; -.
DR BioGRID; 561816; 1.
DR IntAct; Q0V8T9; 1.
DR STRING; 10090.ENSMUSP00000035732; -.
DR GlyConnect; 2233; 1 N-Linked glycan (1 site).
DR GlyGen; Q0V8T9; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q0V8T9; -.
DR PhosphoSitePlus; Q0V8T9; -.
DR PaxDb; Q0V8T9; -.
DR PeptideAtlas; Q0V8T9; -.
DR PRIDE; Q0V8T9; -.
DR ProteomicsDB; 285411; -.
DR DNASU; 636808; -.
DR Ensembl; ENSMUST00000043725; ENSMUSP00000035732; ENSMUSG00000070695.
DR GeneID; 636808; -.
DR KEGG; mmu:636808; -.
DR UCSC; uc007cia.1; mouse.
DR CTD; 636808; -.
DR MGI; MGI:3643623; Cntnap5a.
DR VEuPathDB; HostDB:ENSMUSG00000070695; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000164023; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q0V8T9; -.
DR OMA; GVEPITH; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q0V8T9; -.
DR BioGRID-ORCS; 636808; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cntnap5a; mouse.
DR PRO; PR:Q0V8T9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q0V8T9; protein.
DR Bgee; ENSMUSG00000070695; Expressed in globus pallidus and 72 other tissues.
DR Genevisible; Q0V8T9; MM.
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:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS50022; FA58C_3; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein 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..1304
FT /note="Contactin-associated protein like 5-1"
FT /id="PRO_0000317378"
FT TOPO_DOM 25..1236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1237..1257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1258..1304
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 1020..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 622
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 1304 AA; 145711 MW; 5875C8DF4A92F814 CRC64;
MDSVPRLNSV LTLVLSGLWH LGLTATNYNC DDPLSNFLSL KAFSSSSDIT GSSSSAQLNW
RMGTGGWSPA DSNAQQWLQI DLQNRVEITA VATQGRYGSS DWVTSYRLMF SDTGHNWQPY
NQEDSIWTFV GNMNSDSVVH HKLLHSVRAR FVRFVPLEWN PNGKIGMRVE AYGCSYRSDV
ADFDGRSSLL YRFNQKTMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL
YLNLDDSKAR LSSTVPLVIL GSLLDDQHWH SVLLERVGKQ ANFTVDMNTQ HFRTKGDTDS
LDIDYELSFG GIPVPSKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYSGNVTFSC
SEPQIVPITF INSRSSYLML PGTPQIDGLS VSFQFRTWNE DGLLLSTELS EGSGTLLLIL
EGGTLRLLIK KVARHGTEIL TGSGLNDGLW HSVSINARRN RVTLTLDNDA ASPAPDTSRI
QIYSGKSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGSFSDLH
IDLCSIKDRC LPNYCEHGGH CDQTWTTFYC NCSGTGYTGA TCHDSIYEQS CEVYRHRGHT
AGFFYVDSDG SGPLGPLQVY CNITEDKIWM TVQHNNTELT RVQGSSPENP YSMTLNYGGS
MEQLEALIDG SEYCEQEVIY HCRRSRLLNT PDGAPFTWWI GRSTERHPYW GGAVPGVQQC
GCGLEESCLD SRHFCNCDAD IDEWANDTGL FSFKDHLPVT QIIIMDTNRT NSEAAWRIGP
LRCYGDRHFW NAVSFSTEAS YLHFPTFHTE FSADISFFFK TTALSGVFLE NLGIKDFFRL
EMSSPSEVTF AIDVGNGPIE LLVQSPYPLN DNQWHYIRAE TNLKETSLQV DNLPQSMREA
SEGGHFRLQL NSQLFVGGTS SRQKGFLGCI RSLLLNGHKV DLEERAKVTS GVRPGCPGHC
SSYGSNCHNG GKCVEKHTGY SCDCTNSPYE GPFCRKEISA LFDSGTSVTY MFQEPYPVTK
NTSLSSSAIY TDLAPFKETI MLSFMTTQAP TLLLYLNFSS QNFLAILLSR NGSLQVRYRL
SKDESHVFNM DTENLANRRV HQVKISRDGP ELSIQMDQQL FSYSFSPEVE FRTLRSLVLG
KVTETLDLDP EVARANTLGF VGCLSSVQYN HIAPLKAALR HASIAPVTVQ KTLTESSCGS
MVDSDVNAVT TVHSLSDSFG KTDDHEPLQN AVRSDSAVIG GVIAVVTFIT FCVIGIMTRF
LYQHKQSHRT NQMKKEYPEN LDNSFRNEID LQNTATECKR EYFI
