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Q8WYK1 (CNTP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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-associated protein-like 5
Alternative name(s):
Cell recognition molecule Caspr5
Gene names
Name:CNTNAP5
Synonyms:CASPR5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in the correct development and proper functioning of the peripheral and central nervous system and be involved in cell adhesion and intercellular communication.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Sequence similarities

Belongs to the neurexin family.

Contains 2 EGF-like domains.

Contains 1 F5/8 type C domain.

Contains 1 fibrinogen C-terminal domain.

Contains 4 laminin G-like domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 13061282Contactin-associated protein-like 5
PRO_0000317377

Regions

Topological domain25 – 12371213Extracellular Potential
Transmembrane1238 – 125821Helical; Potential
Topological domain1259 – 130648Cytoplasmic Potential
Domain30 – 174145F5/8 type C
Domain180 – 360181Laminin G-like 1
Domain367 – 544178Laminin G-like 2
Domain546 – 58338EGF-like 1
Domain584 – 790207Fibrinogen C-terminal
Domain791 – 956166Laminin G-like 3
Domain957 – 99539EGF-like 2
Domain1013 – 1199187Laminin G-like 4
Compositional bias44 – 474Poly-Ser

Amino acid modifications

Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 174 By similarity
Disulfide bond329 ↔ 360 By similarity
Disulfide bond512 ↔ 544 By similarity
Disulfide bond550 ↔ 561 By similarity
Disulfide bond555 ↔ 570 By similarity
Disulfide bond572 ↔ 582 By similarity
Disulfide bond929 ↔ 956 By similarity
Disulfide bond960 ↔ 973 By similarity
Disulfide bond967 ↔ 982 By similarity
Disulfide bond984 ↔ 994 By similarity
Disulfide bond1164 ↔ 1199 By similarity

Natural variations

Natural variant4521S → L.
Corresponds to variant rs17727261 [ dbSNP | Ensembl ].
VAR_038518
Natural variant11951T → M.
Corresponds to variant rs34165507 [ dbSNP | Ensembl ].
VAR_038519

Experimental info

Sequence conflict3531T → TV in BAB71205. Ref.4
Sequence conflict4491L → P in BAB71205. Ref.4
Sequence conflict957 – 9626PGHCSS → SIKKLK in BAB71205. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8WYK1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 132F8B1D9200C68E

FASTA1,306145,623
        10         20         30         40         50         60 
MDSLPRLTSV LTLLFSGLWH LGLTATNYNC DDPLASLLSP MAFSSSSDLT GTHSPAQLNW 

        70         80         90        100        110        120 
RVGTGGWSPA DSNAQQWLQM DLGNRVEITA VATQGRYGSS DWVTSYSLMF SDTGRNWKQY 

       130        140        150        160        170        180 
KQEDSIWTFA GNMNADSVVH HKLLHSVRAR FVRFVPLEWN PSGKIGMRVE VYGCSYKSDV 

       190        200        210        220        230        240 
ADFDGRSSLL YRFNQKLMST LKDVISLKFK SMQGDGVLFH GEGQRGDHIT LELQKGRLAL 

       250        260        270        280        290        300 
HLNLGDSKAR LSSSLPSATL GSLLDDQHWH SVLIERVGKQ VNFTVDKHTQ HFRTKGETDA 

       310        320        330        340        350        360 
LDIDYELSFG GIPVPGKPGT FLKKNFHGCI ENLYYNGVNI IDLAKRRKHQ IYTGNVTFSC 

       370        380        390        400        410        420 
SEPQIVPITF VNSSGSYLLL PGTPQIDGLS VSFQFRTWNK DGLLLSTELS EGSGTLLLSL 

       430        440        450        460        470        480 
EGGILRLVIQ KMTERVAEIL TGSNLNDGLW HSVSINARRN RITLTLDDEA APPAPDSTWV 

       490        500        510        520        530        540 
QIYSGNSYYF GGCPDNLTDS QCLNPIKAFQ GCMRLIFIDN QPKDLISVQQ GSLGNFSDLH 

       550        560        570        580        590        600 
IDLCSIKDRC LPNYCEHGGS CSQSWTTFYC NCSDTSYTGA TCHNSIYEQS CEVYRHQGNT 

       610        620        630        640        650        660 
AGFFYIDSDG SGPLGPLQVY CNITEDKIWT SVQHNNTELT RVRGANPEKP YAMALDYGGS 

       670        680        690        700        710        720 
MEQLEAVIDG SEHCEQEVAY HCRRSRLLNT PDGTPFTWWI GRSNERHPYW GGSPPGVQQC 

       730        740        750        760        770        780 
ECGLDESCLD IQHFCNCDAD KDEWTNDTGF LSFKDHLPVT QIVITDTDRS NSEAAWRIGP 

       790        800        810        820        830        840 
LRCYGDRRFW NAVSFYTEAS YLHFPTFHAE FSADISFFFK TTALSGVFLE NLGIKDFIRL 

       850        860        870        880        890        900 
EISSPSEITF AIDVGNGPVE LVVQSPSLLN DNQWHYVRAE RNLKETSLQV DNLPRSTRET 

       910        920        930        940        950        960 
SEEGHFRLQL NSQLFVGGTS SRQKGFLGCI RSLHLNGQKM DLEERAKVTS GVRPGCPGHC 

       970        980        990       1000       1010       1020 
SSYGSICHNG GKCVEKHNGY LCDCTNSPYE GPFCKKEVSA VFEAGTSVTY MFQEPYPVTK 

      1030       1040       1050       1060       1070       1080 
NISLSSSAIY TDSAPSKENI ALSFVTTQAP SLLLFINSSS QDFVVVLLCK NGSLQVRYHL 

      1090       1100       1110       1120       1130       1140 
NKEETHVFTI DADNFANRRM HHLKINREGR ELTIQMDQQL RLSYNFSPEV EFRVIRSLTL 

      1150       1160       1170       1180       1190       1200 
GKVTENLGLD SEVAKANAMG FAGCMSSVQY NHIAPLKAAL RHATVAPVTV HGTLTESSCG 

      1210       1220       1230       1240       1250       1260 
FMVDSDVNAV TTVHSSSDPF GKTDEREPLT NAVRSDSAVI GGVIAVVIFI IFCIIGIMTR 

      1270       1280       1290       1300 
FLYQHKQSHR TSQMKEKEYP ENLDSSFRNE IDLQNTVSEC KREYFI 

« Hide

References

« Hide 'large scale' references
[1]"In vitro and in vivo studies on the involvement of neural cell adhesion molecules and chondroitin sulfate proteoglycans in defining discrete axonal pathways of the rat cerebral cortex."
Takeuchi K., Watanabe N., Kawano T., Kawamura K.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB077881 mRNA. Translation: BAB83897.1.
AC019105 Genomic DNA. Translation: AAY14716.1.
AC019159 Genomic DNA. Translation: AAX88894.1.
AC074362 Genomic DNA. Translation: AAX81997.1.
AC079154 Genomic DNA. Translation: AAY15042.1.
AC097715 Genomic DNA. Translation: AAY24250.1.
AC104648 Genomic DNA. Translation: AAX88904.1.
CH471103 Genomic DNA. Translation: EAW95266.1.
AK056528 mRNA. Translation: BAB71205.1.
CCDSCCDS46401.1.
RefSeqNP_570129.1. NM_130773.3.
UniGeneHs.660653.

3D structure databases

ProteinModelPortalQ8WYK1.
SMRQ8WYK1. Positions 8-174, 180-582, 791-1188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000399013.

PTM databases

PhosphoSiteQ8WYK1.

Polymorphism databases

DMDM74716461.

Proteomic databases

PaxDbQ8WYK1.
PRIDEQ8WYK1.

Protocols and materials databases

DNASU129684.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000431078; ENSP00000399013; ENSG00000155052.
GeneID129684.
KEGGhsa:129684.
UCSCuc002tno.3. human.

Organism-specific databases

CTD129684.
GeneCardsGC02P124879.
HGNCHGNC:18748. CNTNAP5.
MIM610519. gene.
neXtProtNX_Q8WYK1.
PharmGKBPA134898715.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291100.
HOVERGENHBG057718.
InParanoidQ8WYK1.
OMANFANRRM.
OrthoDBEOG7GXP9N.
PhylomeDBQ8WYK1.
TreeFamTF321823.

Gene expression databases

BgeeQ8WYK1.
CleanExHS_CNTNAP5.
GenevestigatorQ8WYK1.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
2.60.120.260. 1 hit.
InterProIPR028874. Caspr5.
IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR008979. Galactose-bd-like.
IPR001791. Laminin_G.
[Graphical view]
PANTHERPTHR10127:SF605. PTHR10127:SF605. 1 hit.
PfamPF00754. F5_F8_type_C. 1 hit.
PF02210. Laminin_G_2. 4 hits.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00231. FA58C. 1 hit.
SM00282. LamG. 4 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
SSF56496. SSF56496. 1 hit.
PROSITEPS50026. EGF_3. 2 hits.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50025. LAM_G_DOMAIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi129684.
NextBio82625.
PROQ8WYK1.
SOURCESearch...

Entry information

Entry nameCNTP5_HUMAN
AccessionPrimary (citable) accession number: Q8WYK1
Secondary accession number(s): Q4ZFW2 expand/collapse secondary AC list , Q4ZG21, Q53R09, Q53RX1, Q53SG3, Q584P3, Q96MS7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM