ID CTP5B_RAT Reviewed; 1292 AA.
AC Q0V8T5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
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 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; AABR03084824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03084984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03087382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03088686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000869; CAJ55731.1; -; mRNA.
DR RefSeq; NP_001316828.1; NM_001329899.1.
DR AlphaFoldDB; Q0V8T5; -.
DR SMR; Q0V8T5; -.
DR STRING; 10116.ENSRNOP00000044394; -.
DR GlyCosmos; Q0V8T5; 4 sites, No reported glycans.
DR GlyGen; Q0V8T5; 4 sites.
DR PhosphoSitePlus; Q0V8T5; -.
DR PaxDb; 10116-ENSRNOP00000044394; -.
DR GeneID; 304725; -.
DR KEGG; rno:304725; -.
DR AGR; RGD:1592077; -.
DR CTD; 304725; -.
DR RGD; 1565194; Cntnap5b.
DR VEuPathDB; HostDB:ENSRNOG00000029556; -.
DR eggNOG; KOG3516; Eukaryota.
DR HOGENOM; CLU_003504_1_0_1; -.
DR InParanoid; Q0V8T5; -.
DR OrthoDB; 4255614at2759; -.
DR PhylomeDB; Q0V8T5; -.
DR PRO; PR:Q0V8T5; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000029556; Expressed in cerebellum and 2 other cell types or tissues.
DR Genevisible; Q0V8T5; RN.
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; 2.
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:SF75; CONTACTIN-ASSOCIATED PROTEIN LIKE 5-2; 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; 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..1292
FT /note="Contactin-associated protein like 5-2"
FT /id="PRO_0000317382"
FT TOPO_DOM 25..1223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1224..1244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1245..1292
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..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 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
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 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"
SQ SEQUENCE 1292 AA; 144159 MW; 6B7C9670DFF60618 CRC64;
MDSILRLTSI LTWLLSGLWH VGLTATNYNC DDPLASFLSP VAYSSSSDIT GSTSSAQLNW
RMGTGGWSPA DSSAHQWLQL DLGNRVEITA VATQGRYGSA DWVTSYHLMF SDTGHNWQQY
KQENSIWTFA GNLNADSVVH HKLLHSVRAR FIRFVPMEWN RNGNIGMRVE VYGCSYKSDV
ADFDGQSSLL YRFSQKTMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQNGRLVL
YLNLDDKKAW LSSITPSAIL GSLLDDQHWH SVFLERVGKQ VNFTVDRNTQ HFWTKGETEV
LDIDYELSFG GIPVPSKPGT FVKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYSGNVTFSC
SEPQIVPITF VNSRSSYLFL PGTPQIDGLS VSFQFRTWNE DGLLLSTELS EGSGTLLLIL
ESGTLRLLIK KVTGHGTESL TGRSLNDGRW HSVSINVRRN RVTLTVDNDA VSLAPETSGL
QIYSGNSYYF GGCPDNLTVS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH
IDLCSIKDRC LPNYCEHGGH CTQTWTSFYC NCSDTGYTGA TCHNSIYEQS CEIYRHRGNK
AGFFYVDSDG SGPLGPLQVY CNVTEDKIWM TVQHTITELT QVQGSNSEKP YAMTLNYGGS
MEQLEALIDG SEHCEQEVTY RCRRAHLFNT QDEAPFTWWI GRSNERHPYW GGYVPGVQQC
GCGLEESCQE IASNTGFLSS KDHLPVTQII ITNSNRTNSE AAWRIGPLRC YGDRHFWNAV
SFSTEASYLH FSAFHVEFSA DISFFFKTTA LSGIFLENLG IKGFLRLEMS SPSEVIFAID
VGNSPIELLV QSPYPLNDNQ WHYIQAERNI KETLLQVDNL PKNKREVSDQ SNFLLQLSSQ
LFIGGTSSRQ KGFLGCIRSL HLNGQKIDLE ERAKITPGVR PGCPGHCSSY GRNCHNGGKC
VEKHNGYSCD CTNSPFEGPF CQKEMSALFY SGTSVTYMFQ EPYPVAKNTS LSSSAIYKDT
APSKEIVTLS FITAQAPALL LYLKFSPQSF LAILLSRNGS LQIHYQLSKV ESHVFTVGSE
NLANRRVHEV NMNRNGQELS IQVDQQLFSY NFSPEVEFQT VRSLILGKVT ETLVLNPEVT
QANTLGFVGC LSSVQYNHIA PLKAALRHAS IAPVTVQGTL TESSCGSMVE SYANGVTTVY
SSSDPFGNTD EHEPLTNAIQ SDSAFIGGVI AIVTFIAFGV IGIMTHFLYQ HKQSHHTNPM
KEKEYPENLD SSFRNDIDLQ NTVSDCKREY FI
//
