CNTN5_RAT
ID CNTN5_RAT Reviewed; 1099 AA.
AC P97527;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Contactin-5;
DE AltName: Full=Neural recognition molecule NB-2;
DE Flags: Precursor;
GN Name=Cntn5;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8945756; DOI=10.1016/s0304-3940(96)13156-6;
RA Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.;
RT "Novel neural adhesion molecules in the contactin/F3 subgroup of the
RT immunoglobulin superfamily: isolation and characterization of cDNAs from
RT rat brain.";
RL Neurosci. Lett. 218:173-176(1996).
RN [2]
RP ERRATUM OF PUBMED:8945756.
RA Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.;
RL Neurosci. Lett. 221:221-223(1997).
RN [3]
RP FUNCTION, GPI-ANCHOR, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11438979; DOI=10.1002/jnr.1133.abs;
RA Ogawa J., Lee S., Itoh K., Nagata S., Machida T., Takeda Y., Watanabe K.;
RT "Neural recognition molecule NB-2 of the contactin/F3 subgroup in rat:
RT specificity in neurite outgrowth-promoting activity and restricted
RT expression in the brain regions.";
RL J. Neurosci. Res. 65:100-110(2001).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity in
CC the cerebral cortical neurons but not in hippocampal neurons. Probably
CC involved in neuronal activity in the auditory system.
CC {ECO:0000269|PubMed:11438979}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the nervous system.
CC Expressed in cerebrum and cerebellum but at low level in spinal chord.
CC In brain, it is expressed in highly restricted regions at postnatal day
CC 7, such as the auditory pathway, including the cochlear nucleus,
CC superior olive, inferior colliculus, medial geniculate nucleus and
CC auditory cortex. Expressed in the accessory olfactory bulb, glomerular
CC and mitral cell layers in the olfactory bulb, anterior thalamic nuclei,
CC layers II-IV of the cerebral cortex, dentate gyrus of the hippocampus
CC and external granule cells and Purkinje cells of the cerebellum. Also
CC expressed in the piriform cortex, inferior olive and facial nucleus.
CC Weakly or not expressed in other parts of the brain.
CC {ECO:0000269|PubMed:11438979, ECO:0000269|PubMed:8945756}.
CC -!- DEVELOPMENTAL STAGE: Expressed after birth, reaching a maximum at
CC postnatal day 14 in the cerebrum and postnatal day 3 in the cerebellum.
CC Then, it decreases abruptly thereafter (at protein level).
CC {ECO:0000269|PubMed:11438979}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; D87212; BAA13311.1; -; mRNA.
DR RefSeq; NP_446198.1; NM_053746.1.
DR RefSeq; XP_017450897.1; XM_017595408.1.
DR RefSeq; XP_017450898.1; XM_017595409.1.
DR RefSeq; XP_017450899.1; XM_017595410.1.
DR AlphaFoldDB; P97527; -.
DR SMR; P97527; -.
DR STRING; 10116.ENSRNOP00000009418; -.
DR GlyGen; P97527; 9 sites.
DR PaxDb; P97527; -.
DR PRIDE; P97527; -.
DR Ensembl; ENSRNOT00000009418; ENSRNOP00000009418; ENSRNOG00000007038.
DR GeneID; 114589; -.
DR KEGG; rno:114589; -.
DR UCSC; RGD:621302; rat.
DR CTD; 53942; -.
DR RGD; 621302; Cntn5.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000158183; -.
DR InParanoid; P97527; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P97527; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P97527; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:RGD.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0099054; P:presynapse assembly; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR032989; Contactin-5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR44170:SF17; PTHR44170:SF17; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1072
FT /note="Contactin-5"
FT /id="PRO_0000014721"
FT PROPEP 1073..1099
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014722"
FT DOMAIN 99..190
FT /note="Ig-like C2-type 1"
FT DOMAIN 196..282
FT /note="Ig-like C2-type 2"
FT DOMAIN 300..385
FT /note="Ig-like C2-type 3"
FT DOMAIN 390..474
FT /note="Ig-like C2-type 4"
FT DOMAIN 480..569
FT /note="Ig-like C2-type 5"
FT DOMAIN 571..660
FT /note="Ig-like C2-type 6"
FT DOMAIN 673..771
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 776..873
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 878..972
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 977..1067
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 958..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1072
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 217..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 322..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 411..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 503..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 593..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1099 AA; 120603 MW; 35BC5745164AD203 CRC64;
MASSWRLILF LSFTSCLSEY SEALSGLSTS YAALLRIKKS STSSAFGSKS RPRYSSPSLG
TLSVSPPSWR GAAQQYHSPV NLYHSPDAFR QDESVDYGPV FVQEPDDIIF PTDSDEKKVA
LNCEVRGNPS PTYRWLRNGT EIDLESDYRY SMIDGTFIIN NPSESRDSGL YQCLATNTFG
SILSREATLQ FAYLGNFSGR TRSAVSVREG QGVVLMCSPP PHSPEIIYSW VFNEFPSFVA
EDSRRFISQE TGNLYISKVQ TSDVGSYICL VKNAVTNARV LSPPTPLTLR NDGVMGEYEP
KIEVHFPTTV TAAKGTTVKM ECFALGNPVP TITWMKVNGY IPSKSRLRKS QAVLEIPNLQ
LDDAGIYECT AENSRGKNSF RGQLQIYTYP HWVQKLNDTQ LDSGSPLQWE CKATGKPRPT
YRWLKNGAPL LPQSRVDTAN GVLAIHSVNQ SDAGMYQCLA ENKYGAIYAS AELKILASPP
SFELNQVKKS IIVTKDREVL IECKPQGSPK PAISWRKGDK AVRGNKRIAI LPDGSLRILN
ASKADEGKYI CQGVNIFGSA EIIASVSVKE PTRIELTPKR TELTVGESIV LNCKAMHDSS
LDVTFYWTLK GQPIDFEKEG GHFESIRAQA SSADLMIRNI LLMHAGRYGC RVQTTADSVS
DEAELLVRGP PGPPGVVIVE EITESTATLS WSPATDNHSP ISSYNLQARS PFSLGWQTVK
TVPEVITGDM ESAMAVDLNP WVEYEFRVVA TNPIGTGDPS IPSRMIRTNE AVPKTAPSNV
SGGSGRRHEL VIAWEPVSEE FQNGEGFGYI VAFRPNGTRG WKEKMVTSSD ASKFIYRDES
VPPLTPFEVK VGVYNNKGDG PFSQIVVICS AEGEPTAAPT DVTATSVSVS EIFVVWKHVK
ESLGRPQGFE IGYWKDTEPE DSAETVRTRG NESFVMLTGL EGDTLYHLTV RAYNGAGYGP
PSREVSATTK RHPPSEPPGN LRWEQQGSQV SLGWEPVRPL ANESEVMGYK VFYRQEGHSK
GQVIETQKPQ AVVPLPEAGV YIIEVRAYSE GGDGTASSQI RVPSYAGGKI TSAQSTLHSL
SKWSSVTLLL ALMLPSSSW
