CTP5B_MOUSE
ID CTP5B_MOUSE Reviewed; 1292 AA.
AC Q0V8T8; Q2PAX9; Q8BUT8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Contactin-associated protein like 5-2;
DE AltName: Full=Cell recognition molecule Caspr5-2;
DE AltName: Full=Cell recognition molecule Caspr5b;
DE AltName: Full=Contactin-associated protein-like 5b;
DE Flags: Precursor;
GN Name=Cntnap5b; Synonyms=Caspr5-2;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-1292.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Brain;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0V8T8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0V8T8-2; Sequence=VSP_030943;
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC38563.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC102217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK082656; BAC38563.1; ALT_SEQ; mRNA.
DR EMBL; AM076974; CAJ28927.1; -; mRNA.
DR EMBL; BN000866; CAJ55746.1; -; mRNA.
DR CCDS; CCDS35682.1; -. [Q0V8T8-1]
DR RefSeq; NP_766439.2; NM_172851.2. [Q0V8T8-1]
DR AlphaFoldDB; Q0V8T8; -.
DR SMR; Q0V8T8; -.
DR STRING; 10090.ENSMUSP00000083944; -.
DR GlyGen; Q0V8T8; 4 sites.
DR iPTMnet; Q0V8T8; -.
DR PhosphoSitePlus; Q0V8T8; -.
DR MaxQB; Q0V8T8; -.
DR PaxDb; Q0V8T8; -.
DR PeptideAtlas; Q0V8T8; -.
DR PRIDE; Q0V8T8; -.
DR ProteomicsDB; 285412; -. [Q0V8T8-1]
DR ProteomicsDB; 285413; -. [Q0V8T8-2]
DR DNASU; 241175; -.
DR Ensembl; ENSMUST00000086738; ENSMUSP00000083944; ENSMUSG00000067028. [Q0V8T8-1]
DR GeneID; 241175; -.
DR KEGG; mmu:241175; -.
DR UCSC; uc007cfy.1; mouse. [Q0V8T8-1]
DR CTD; 241175; -.
DR MGI; MGI:3664583; Cntnap5b.
DR VEuPathDB; HostDB:ENSMUSG00000067028; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000164023; -.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q0V8T8; -.
DR OMA; DMYVQVD; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q0V8T8; -.
DR TreeFam; TF321823; -.
DR BioGRID-ORCS; 241175; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Cntnap5b; mouse.
DR PRO; PR:Q0V8T8; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q0V8T8; protein.
DR Bgee; ENSMUSG00000067028; Expressed in spermatid and 31 other tissues.
DR ExpressionAtlas; Q0V8T8; baseline and differential.
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; 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 Alternative splicing; Cell adhesion; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1292
FT /note="Contactin-associated protein like 5-2"
FT /id="PRO_0000317379"
FT TOPO_DOM 25..1224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1225..1245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1246..1292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..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..777
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DOMAIN 778..943
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 944..982
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 987..1185
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 1044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..174
FT /evidence="ECO:0000250"
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 916..943
FT /evidence="ECO:0000250"
FT DISULFID 947..960
FT /evidence="ECO:0000250"
FT DISULFID 954..969
FT /evidence="ECO:0000250"
FT DISULFID 971..981
FT /evidence="ECO:0000250"
FT DISULFID 1150..1185
FT /evidence="ECO:0000250"
FT VAR_SEQ 774..831
FT /note="RHFWNAVSFSTEAAYLHIPTFHAEFSADISFFFKTTALSGVFLENLGVKNFL
FT RLEMSS -> P (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030943"
SQ SEQUENCE 1292 AA; 144260 MW; CED9FDC0FFD89503 CRC64;
MDSVPRLTSI LTLVLSGLWH VGLTATNYNC DDPLASFLSP KAFSSSSDLT GSSSSAQLNG
RMGTGGWSPE NSSAHQWLQL DLGNRVEITA VATQGRYGSS DWVTSYCLIF SDTGHNWQQY
KQGDSIWTFI GNMNANSVVH HKLLHAVRAR FVRFVPLEWN PNGKIGMRVE VYGCFYKSDV
ADFDGRSSLL YRFNQKTMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQNGRLAL
YLNLDDSKAR LSSITPSAIL GSLLDDQHWH SVLLERVGKQ ANFTVDRNTQ HFRTNGDTDA
LDIDYELSFG GIPVPSKPGT FLKKNFQGCI ENLYYNGVNI IDLAKRRKHQ IYSGNVTFSC
SEPQIVPITF VNSRSSYLLL PGTPQIDGLS VSFQFRTWNE DGLLLSTELS EGSGTLLLIL
EGGTLRLLIK NVAGHGTESL TGRSLNNGQW HSVNINARRN RVTLTLDNDP ASPALETPWL
QIYSGYSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH
IDLCSIKDRC FPNYCEHGGH CTQTWTNFYC NCSNTGYTGA TCHDSIYEQS CEVYRHRGNT
AGYFYVDSDG SGPLRPLQVY CNVTEDKIWM TVQHNNTELT WIQGSNTEKP YVMNLNYGGS
MEQLEALIDG SEHCEQEVTY YCRRSHLLNT PDGAPFAWWT GRSNERHPYW GGYFPGDQKC
GCGLEESCLE MSNDTGFLSF KDHLPVTQII ISDTNRSNSE AAWRIGPLRC YGDRHFWNAV
SFSTEAAYLH IPTFHAEFSA DISFFFKTTA LSGVFLENLG VKNFLRLEMS SPSEVIFAID
VGNGPMELLV QSPYPLNDNQ WHYIQAERNI KETLLHVDNL PKSMRMASEE GHFLLQLNSQ
LFVGGTSSRQ KGFLGCIRSL HLNGQKVDLE ERAKITSGVR PGCAGHCNSY GRNCQNGGKC
VEKHIGYTCD CTNSPYEGPF CKKEISALFY SGTSVTYMFQ EPYPVTKNTS LSSSAIYKDT
APSKEAITLS FMTAQAPTLL LYLNFSSQNF LAILLSRNGS LQIQYRLSKE ESHVFTISTE
NLANRRVHQV KMSRDGPELS IQMDQQLFSY NFPPEVEFQT VRSLILGKVT ETLGLDPEVA
KANTLGFVGC LSSVQYNHIA PLKAALRHAS ISPVTVQGTL TESSCDSMID SDVTGVTTVY
SPSVPFGKTD EHEPLTNTIQ SDSAFIGGVI AIVTFITFCV LGIMVHFLYQ QKQSHRTNQM
KEKEYPDNLD SSFRNDIDLQ NTAIECKREY FI
