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P97527 (CNTN5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Contactin-5
Alternative name(s):
Neural recognition molecule NB-2
Gene names
Name:Cntn5
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1099 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons. Probably involved in neuronal activity in the auditory system. Ref.3

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Ref.3.

Tissue specificity

Specifically expressed in the nervous system. Expressed in cerebrum and cerebellum but at low level in spinal chord. In brain, it is expressed in highly restricted regions at postnatal day 7, such as the auditory pathway, including the cochlear nucleus, superior olive, inferior colliculus, medial geniculate nucleus and auditory cortex. Expressed in the accessory olfactory bulb, glomerular and mitral cell layers in the olfactory bulb, anterior thalamic nuclei, layers II-IV of the cerebral cortex, dentate gyrus of the hippocampus and external granule cells and Purkinje cells of the cerebellum. Also expressed in the piriform cortex, inferior olive and facial nucleus. Weakly or not expressed in other parts of the brain. Ref.1 Ref.3

Developmental stage

Expressed after birth, reaching a maximum at postnatal day 14 in the cerebrum and postnatal day 3 in the cerebellum. Then, it decreases abruptly thereafter (at protein level). Ref.3

Sequence similarities

Belongs to the immunoglobulin superfamily. Contactin family.

Contains 4 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   DomainImmunoglobulin domain
Repeat
Signal
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell adhesion

Non-traceable author statement Ref.1. Source: RGD

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 10721054Contactin-5
PRO_0000014721
Propeptide1073 – 109927Removed in mature form Potential
PRO_0000014722

Regions

Domain99 – 19092Ig-like C2-type 1
Domain196 – 28287Ig-like C2-type 2
Domain300 – 38586Ig-like C2-type 3
Domain390 – 47485Ig-like C2-type 4
Domain480 – 56990Ig-like C2-type 5
Domain571 – 66090Ig-like C2-type 6
Domain670 – 76697Fibronectin type-III 1
Domain773 – 86896Fibronectin type-III 2
Domain875 – 96894Fibronectin type-III 3
Domain974 – 106491Fibronectin type-III 4

Amino acid modifications

Lipidation10721GPI-anchor amidated serine Potential
Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation4491N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Potential
Glycosylation7791N-linked (GlcNAc...) Potential
Glycosylation8161N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Glycosylation10021N-linked (GlcNAc...) Potential
Disulfide bond123 ↔ 173 By similarity
Disulfide bond217 ↔ 269 By similarity
Disulfide bond322 ↔ 369 By similarity
Disulfide bond411 ↔ 458 By similarity
Disulfide bond503 ↔ 551 By similarity
Disulfide bond593 ↔ 650 By similarity

Sequences

Sequence LengthMass (Da)Tools
P97527 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 35BC5745164AD203

FASTA1,099120,603
        10         20         30         40         50         60 
MASSWRLILF LSFTSCLSEY SEALSGLSTS YAALLRIKKS STSSAFGSKS RPRYSSPSLG 

        70         80         90        100        110        120 
TLSVSPPSWR GAAQQYHSPV NLYHSPDAFR QDESVDYGPV FVQEPDDIIF PTDSDEKKVA 

       130        140        150        160        170        180 
LNCEVRGNPS PTYRWLRNGT EIDLESDYRY SMIDGTFIIN NPSESRDSGL YQCLATNTFG 

       190        200        210        220        230        240 
SILSREATLQ FAYLGNFSGR TRSAVSVREG QGVVLMCSPP PHSPEIIYSW VFNEFPSFVA 

       250        260        270        280        290        300 
EDSRRFISQE TGNLYISKVQ TSDVGSYICL VKNAVTNARV LSPPTPLTLR NDGVMGEYEP 

       310        320        330        340        350        360 
KIEVHFPTTV TAAKGTTVKM ECFALGNPVP TITWMKVNGY IPSKSRLRKS QAVLEIPNLQ 

       370        380        390        400        410        420 
LDDAGIYECT AENSRGKNSF RGQLQIYTYP HWVQKLNDTQ LDSGSPLQWE CKATGKPRPT 

       430        440        450        460        470        480 
YRWLKNGAPL LPQSRVDTAN GVLAIHSVNQ SDAGMYQCLA ENKYGAIYAS AELKILASPP 

       490        500        510        520        530        540 
SFELNQVKKS IIVTKDREVL IECKPQGSPK PAISWRKGDK AVRGNKRIAI LPDGSLRILN 

       550        560        570        580        590        600 
ASKADEGKYI CQGVNIFGSA EIIASVSVKE PTRIELTPKR TELTVGESIV LNCKAMHDSS 

       610        620        630        640        650        660 
LDVTFYWTLK GQPIDFEKEG GHFESIRAQA SSADLMIRNI LLMHAGRYGC RVQTTADSVS 

       670        680        690        700        710        720 
DEAELLVRGP PGPPGVVIVE EITESTATLS WSPATDNHSP ISSYNLQARS PFSLGWQTVK 

       730        740        750        760        770        780 
TVPEVITGDM ESAMAVDLNP WVEYEFRVVA TNPIGTGDPS IPSRMIRTNE AVPKTAPSNV 

       790        800        810        820        830        840 
SGGSGRRHEL VIAWEPVSEE FQNGEGFGYI VAFRPNGTRG WKEKMVTSSD ASKFIYRDES 

       850        860        870        880        890        900 
VPPLTPFEVK VGVYNNKGDG PFSQIVVICS AEGEPTAAPT DVTATSVSVS EIFVVWKHVK 

       910        920        930        940        950        960 
ESLGRPQGFE IGYWKDTEPE DSAETVRTRG NESFVMLTGL EGDTLYHLTV RAYNGAGYGP 

       970        980        990       1000       1010       1020 
PSREVSATTK RHPPSEPPGN LRWEQQGSQV SLGWEPVRPL ANESEVMGYK VFYRQEGHSK 

      1030       1040       1050       1060       1070       1080 
GQVIETQKPQ AVVPLPEAGV YIIEVRAYSE GGDGTASSQI RVPSYAGGKI TSAQSTLHSL 

      1090 
SKWSSVTLLL ALMLPSSSW 

« Hide

References

[1]"Novel neural adhesion molecules in the contactin/F3 subgroup of the immunoglobulin superfamily: isolation and characterization of cDNAs from rat brain."
Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.
Neurosci. Lett. 218:173-176(1996) [PubMed: 8945756] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Brain.
[2]Erratum
Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.
Neurosci. Lett. 221:221-223(1997)
[3]"Neural recognition molecule NB-2 of the contactin/F3 subgroup in rat: specificity in neurite outgrowth-promoting activity and restricted expression in the brain regions."
Ogawa J., Lee S., Itoh K., Nagata S., Machida T., Takeda Y., Watanabe K.
J. Neurosci. Res. 65:100-110(2001) [PubMed: 11438979] [Abstract]
Cited for: FUNCTION, GPI-ANCHOR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87212 mRNA. Translation: BAA13311.1.
IPIIPI00205420.
RefSeqNP_446198.1. NM_053746.1.
UniGeneRn.10643.

3D structure databases

ProteinModelPortalP97527.
ModBaseSearch...

Protein-protein interaction databases

STRINGP97527.

Proteomic databases

PRIDEP97527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID114589.
KEGGrno:114589.

Organism-specific databases

CTD53942.
RGD621302. Cntn5.

Phylogenomic databases

eggNOGmaNOG09591.
HOVERGENHBG051047.

Gene expression databases

GenevestigatorP97527.

Family and domain databases

InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 10 hits.
KOK06763.
PfamPF00041. fn3. 4 hits.
PF07679. I-set. 5 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 4 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio618737.

Entry information

Entry nameCNTN5_RAT
AccessionPrimary (citable) accession number: P97527
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 1997
Last modified: November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families