Reviewed,
UniProtKB/Swiss-Prot Q19319 (CADH4_CAEEL)
Last modified
February 9, 2010.
Version 85.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cadherin-4 | ||||
| Gene names |
| ||||
| Organism | Caenorhabditis elegans [Complete proteome] | ||||
| Taxonomic identifier | 6239 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 4292 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Potential calcium-dependent cell-adhesion protein that controls axon guidance in the ventral cord. Ref.3 Ref.5 |
| Subcellular location | Cell membrane; Single-pass type I membrane protein Potential. |
| Tissue specificity | In larvae and adult, it is expressed in various tissues including pharyngeal muscle, hypodermis and gonad. In the nervous system it is expressed in sensory neurons and motor neurons in the ventral cord. Ref.3 |
| Sequence similarities | Contains 28 cadherin domains. Contains 3 EGF-like domains. Contains 1 laminin G-like domain. Contains 1 TSP N-terminal (TSPN) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Cell membrane Membrane |
| Domain | EGF-like domain Repeat Signal Transmembrane |
| Ligand | Calcium |
| Molecular function | Developmental protein |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | axonal fasciculation Ref.5 Inferred from mutant phenotype. Source: WormBase homophilic cell adhesionInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 4292 | 4269 | Cadherin-4 | PRO_0000250582 | |||||||
Regions | |||||||||||
| Topological domain | 24 – 4036 | 4013 | Extracellular Potential | ||||||||
| Transmembrane | 4037 – 4057 | 21 | Potential | ||||||||
| Topological domain | 4058 – 4292 | 235 | Cytoplasmic Potential | ||||||||
| Domain | 46 – 153 | 108 | Cadherin 1 | ||||||||
| Domain | 156 – 275 | 120 | Cadherin 2 | ||||||||
| Domain | 384 – 492 | 109 | Cadherin 3 | ||||||||
| Domain | 493 – 608 | 116 | Cadherin 4 | ||||||||
| Domain | 609 – 720 | 112 | Cadherin 5 | ||||||||
| Domain | 721 – 826 | 106 | Cadherin 6 | ||||||||
| Domain | 827 – 934 | 108 | Cadherin 7 | ||||||||
| Domain | 935 – 1051 | 117 | Cadherin 8 | ||||||||
| Domain | 1047 – 1156 | 110 | Cadherin 9 | ||||||||
| Domain | 1155 – 1262 | 108 | Cadherin 10 | ||||||||
| Domain | 1265 – 1363 | 99 | Cadherin 11 | ||||||||
| Domain | 1364 – 1467 | 104 | Cadherin 12 | ||||||||
| Domain | 1468 – 1570 | 103 | Cadherin 13 | ||||||||
| Domain | 1671 – 1784 | 114 | Cadherin 14 | ||||||||
| Domain | 1881 – 1984 | 104 | Cadherin 15 | ||||||||
| Domain | 2082 – 2186 | 105 | Cadherin 16 | ||||||||
| Domain | 2187 – 2285 | 99 | Cadherin 17 | ||||||||
| Domain | 2286 – 2469 | 184 | Cadherin 18 | ||||||||
| Domain | 2470 – 2572 | 103 | Cadherin 19 | ||||||||
| Domain | 2573 – 2676 | 104 | Cadherin 20 | ||||||||
| Domain | 2677 – 2777 | 101 | Cadherin 21 | ||||||||
| Domain | 2776 – 2879 | 104 | Cadherin 22 | ||||||||
| Domain | 2877 – 2975 | 99 | Cadherin 23 | ||||||||
| Domain | 2976 – 3077 | 102 | Cadherin 24 | ||||||||
| Domain | 3078 – 3180 | 103 | Cadherin 25 | ||||||||
| Domain | 3181 – 3290 | 110 | Cadherin 26 | ||||||||
| Domain | 3291 – 3392 | 102 | Cadherin 27 | ||||||||
| Domain | 3393 – 3518 | 126 | Cadherin 28 | ||||||||
| Domain | 3670 – 3708 | 39 | EGF-like 1 | ||||||||
| Domain | 3721 – 3889 | 169 | Laminin G-like | ||||||||
| Domain | 3750 – 3871 | 122 | TSP N-terminal | ||||||||
| Domain | 3893 – 3930 | 38 | EGF-like 2 | ||||||||
| Domain | 3932 – 3968 | 37 | EGF-like 3 | ||||||||
| Motif | 1090 – 1092 | 3 | Cell attachment site Potential | ||||||||
| Motif | 4171 – 4173 | 3 | Cell attachment site Potential | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 39 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 56 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 196 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 330 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 339 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 365 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 431 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 452 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 584 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 811 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 899 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1192 | 1 | N-linked (GlcNAc...) Ref.4 | ||||||||
| Glycosylation | 1335 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1610 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1895 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2059 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2150 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2216 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2367 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2377 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2404 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2499 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2808 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2880 | 1 | N-linked (GlcNAc...) Ref.4 Ref.2 | ||||||||
| Glycosylation | 2905 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3047 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3107 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3294 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3476 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3691 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4007 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 3674 ↔ 3685 | By similarity | |||||||||
| Disulfide bond | 3679 ↔ 3696 | By similarity | |||||||||
| Disulfide bond | 3698 ↔ 3707 | By similarity | |||||||||
| Disulfide bond | 3862 ↔ 3889 | By similarity | |||||||||
| Disulfide bond | 3897 ↔ 3908 | By similarity | |||||||||
| Disulfide bond | 3902 ↔ 3918 | By similarity | |||||||||
| Disulfide bond | 3920 ↔ 3929 | By similarity | |||||||||
| Disulfide bond | 3936 ↔ 3947 | By similarity | |||||||||
| Disulfide bond | 3941 ↔ 3956 | By similarity | |||||||||
| Disulfide bond | 3958 ↔ 3967 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| [2] | "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins." Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T. Nat. Biotechnol. 21:667-672(2003) [PubMed: 12754521] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2880, MASS SPECTROMETRY. |
| [3] | "The fat-like cadherin CDH-4 controls axon guidance in the ventral cord of C. elegans." Schmitz C., Wacker I., Schwarz V., Hutter H. (In) Proceedings of the 15th international C. elegans meeting, pp.288-288, Los Angeles (2005) Cited for: FUNCTION, TISSUE SPECIFICITY. |
| [4] | "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins." Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T. Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1192 AND ASN-2880, MASS SPECTROMETRY. |
| [5] | "Axon guidance genes identified in a large-scale RNAi screen using the RNAi-hypersensitive Caenorhabditis elegans strain nre-1(hd20) lin-15b(hd126)." Schmitz C., Kinge P., Hutter H. Proc. Natl. Acad. Sci. U.S.A. 104:834-839(2007) [PubMed: 17213328] [Abstract] Cited for: FUNCTION. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z34802, Z35599, Z35662 Genomic DNA. Translation: CAA84339.2. Z35599, Z34802, Z35662 Genomic DNA. Translation: CAA84661.2. Z35662, Z34802, Z35599 Genomic DNA. Translation: CAA84721.2. |
| PIR | T20721. |
| UniGene | Cel.10567 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EDM based on UniProtKB P00740. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | F25F2.2; F25F2.2; F25F2.2; Caenorhabditis elegans. [Genome view] |
| KEGG | cel:F25F2.2. |
| NMPDR | fig|6239.3.peg.9454. |
| UCSC | F25F2.2. c. elegans. |
Organism-specific databases | |
| WormBase | WBGene00000396. cdh-4. |
| WormPep | F25F2.2. CE43309. [WorfDB] |
Phylogenomic databases | |
| eggNOG | meNOG04588. |
| HOGENOM | HBG381695. |
| PhylomeDB | Q19319. |
Gene expression databases | |
| ArrayExpress | Q19319. |
Family and domain databases | |
| InterPro | IPR002126. Cadherin. IPR015919. Cadherin-like. IPR020894. Cadherin_CS. IPR008985. ConA-like_lec_gl. IPR013320. ConA-like_subgrp. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR001791. Laminin_G. IPR012680. Laminin_G_2. [Graphical view] |
| Gene3D | G3DSA:2.60.40.60. Cadherin. 24 hits. G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. |
| Pfam | PF00028. Cadherin. 14 hits. PF02210. Laminin_G_2. 1 hit. [Graphical view] |
| PRINTS | PR00205. CADHERIN. |
| SMART | SM00112. CA. 28 hits. SM00181. EGF. 4 hits. SM00282. LamG. 1 hit. [Graphical view] |
| PROSITE | PS00232. CADHERIN_1. 9 hits. PS50268. CADHERIN_2. 27 hits. PS00022. EGF_1. 4 hits. PS01186. EGF_2. 2 hits. PS50026. EGF_3. 3 hits. PS50025. LAM_G_DOMAIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 888808. |
Entry information
| Entry name | CADH4_CAEEL | ||||||||
| Accession | Primary (citable) accession number: Q19319 Secondary accession number(s): Q19785, Q21606 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| SIMILARITY comments Index of protein domains and families |

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