CTP5D_RAT
ID CTP5D_RAT Reviewed; 1305 AA.
AC Q0V8T3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Contactin-associated protein like 5-4;
DE AltName: Full=Cell recognition molecule Caspr5-4;
DE AltName: Full=Cell recognition molecule Caspr5d;
DE AltName: Full=Contactin-associated protein-like 5d;
DE Flags: Precursor;
GN Name=Cntnap5d; Synonyms=Caspr5-4;
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; AABR03084626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03084670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03084735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03084983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000871; CAJ55733.1; -; mRNA.
DR RefSeq; NP_001041331.1; NM_001047866.1.
DR AlphaFoldDB; Q0V8T3; -.
DR SMR; Q0V8T3; -.
DR STRING; 10116.ENSRNOP00000062287; -.
DR GlyGen; Q0V8T3; 5 sites.
DR iPTMnet; Q0V8T3; -.
DR PhosphoSitePlus; Q0V8T3; -.
DR PaxDb; Q0V8T3; -.
DR PRIDE; Q0V8T3; -.
DR GeneID; 297846; -.
DR KEGG; rno:297846; -.
DR UCSC; RGD:1566343; rat.
DR CTD; 620292; -.
DR eggNOG; KOG3516; Eukaryota.
DR InParanoid; Q0V8T3; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q0V8T3; -.
DR PRO; PR:Q0V8T3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 5-4"
FT /id="PRO_0000317384"
FT TOPO_DOM 25..1237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1238..1258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1259..1305
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..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 1014..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 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 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 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; 145919 MW; 0F85F5CCD5498DD8 CRC64;
MNSVRRLNSI LTLVLSGLWH LGLTATNYNC DEPLASFLSP LAFFSSSDLN GRFSPPQLNW
RIGSGGWSPA VSNAHQWLQI DLGNRVEITA VATQGRYGST DWVTSYRLMF SDTGHNWQQY
KQKDSIWTFV GNTNADGVVY HKLLHSMRAR FVRFVPLEWN SNGKIGMRVE VYGCSYKSDI
VGFDGQSTLL YRFNQKTMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL
YLNIDGSKAR LSIIAPLAIL GSLLDDQHWH SVLLERVGKQ ANFTVDRNTQ HFQIKGETDA
LDIDYELSFG GIPVPSKPGT FLKKNFHGCI ENVYYNGVNI IDLAKRRKHQ IYSGNVTFSC
SEPEIVPITF VNSRSSYLLL PGIPQIHGLS VSFHFRTWNE DGLLLSTELS EGSGTLLLIL
DGGSLRLLIK KVARHGTEII TGSSLNDGLW HSVSINARRN RVTLTLDNDA ASPALDTSQL
QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSMGNFSDLH
IDLCSIKDRC LPNYCEHGGH CAQNWTTFYC NCSDTGYTGA TCHDSVYEQS CEVYRHKGHT
AGFFYVDSDG SGPLGPLQVY CNITEDKIWM TVQHNNTELT WVQISNAEKA YAMTFNYGGS
MEQLEALIDG SEHCEQEVTY YCRRSHLLKT PDGAPFTWWI GRSNKRHNYW EGSVPRVQQC
RCVHKENCLD IRSFCNCDAD IGEWAKETGF LSFKDHLPVT QIITTDTNRS KSEAAWKIGP
LRCYGDRHFW NAVSFTTEAS YLYFPTFHAE FSADISFFFK TTALSGVFLE NLGIKDFLRL
EMSSPSEITF TIDVGNGPVE LLIQSPYPLN DNQWHYIRAE RNLKETSLQV DNLPQSMREA
SEEAYFRLHL TSQLFVGGTS SRQKGFLGCM RSLHLNGQNT DLIERAKLMS GVTPGCLGHC
SSYGSNCLNG GKCVEKQSGY SCDCTNSPNE GPFCQKEISA LFNSGTSVTY LFQEPYLVIK
NTSLLSSPIY ADTAPSKETI MLNFLTTQAP TILLYLNFSS QNFLAILLSR NGSLQICFRL
SKIESHVYTM NTENLANGRV HQVKINKDGP ELSIQMDQQL FTYNFSPKVE FWTLKSLVLG
KVTETLGLDP EVAKVNILGF VGCLSSVQYN HIAPLKAALR HSGIAPVTVQ GTLTESGCDS
TLDSDVNAVT TVHSSLDPIG KRDEREPLTD TVQSDSAVIG GIIALVTFVT FCVIGIMIHF
LYLHKQSHCT NQTKEKEYSE NLSNSFRNAI DLQNTASECK REYFI
