O88277 (FAT2_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protocadherin Fat 2 Alternative name(s): Multiple epidermal growth factor-like domains protein 1 Short name=Multiple EGF-like domains protein 1 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 4351 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 | May modulate the extracellular space surronding parallel fibers of cerebellar during development. Plays a role in the migration of epidermal cells By similarity. |
| Subunit structure | Homodimer. Ref.3 |
| Subcellular location | Cell membrane; Single-pass membrane protein Potential. Cell junction By similarity. Nucleus By similarity. |
| Tissue specificity | Cerebellum-specific expression. Expressed in thin parallel fibers of cerebellar granule cells. Ref.1 Ref.3 |
| Developmental stage | In the developing cerebellum, expressed in granule cells in the inner external germinal layer and in migrating granule cells whereas proliferating cells in the outer extessornal germinal layer did not shown expression. Expression levels in the internal granule cell layer peak during the third postnatal week and remain considerably high in the adult cerebellum. Ref.3 |
| Sequence similarities | Contains 33 cadherin domains. Contains 2 EGF-like domains. Contains 1 laminin G-like domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Cell junction Cell membrane Membrane Nucleus |
| Domain | EGF-like domain Repeat Signal Transmembrane Transmembrane helix |
| Ligand | Calcium |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB homophilic cell adhesionInferred from direct assay Ref.3. Source: UniProtKB |
| Cellular_component | cell-cell adherens junction Inferred from sequence or structural similarity. Source: UniProtKB integral to membraneInferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||||
| Chain | 19 – 4351 | 4333 | Protocadherin Fat 2 | PRO_0000004019 | |||||||
Regions | |||||||||||
| Topological domain | 19 – 4050 | 4032 | Extracellular Potential | ||||||||
| Transmembrane | 4051 – 4071 | 21 | Helical; Potential | ||||||||
| Topological domain | 4072 – 4351 | 280 | Cytoplasmic Potential | ||||||||
| Domain | 34 – 148 | 115 | Cadherin 1 | ||||||||
| Domain | 149 – 256 | 108 | Cadherin 2 | ||||||||
| Domain | 363 – 458 | 96 | Cadherin 3 | ||||||||
| Domain | 459 – 564 | 106 | Cadherin 4 | ||||||||
| Domain | 565 – 669 | 105 | Cadherin 5 | ||||||||
| Domain | 716 – 820 | 105 | Cadherin 6 | ||||||||
| Domain | 821 – 925 | 105 | Cadherin 7 | ||||||||
| Domain | 926 – 1032 | 107 | Cadherin 8 | ||||||||
| Domain | 1033 – 1142 | 110 | Cadherin 9 | ||||||||
| Domain | 1138 – 1242 | 105 | Cadherin 10 | ||||||||
| Domain | 1243 – 1346 | 104 | Cadherin 11 | ||||||||
| Domain | 1350 – 1448 | 99 | Cadherin 12 | ||||||||
| Domain | 1449 – 1555 | 107 | Cadherin 13 | ||||||||
| Domain | 1556 – 1660 | 105 | Cadherin 14 | ||||||||
| Domain | 1661 – 1758 | 98 | Cadherin 15 | ||||||||
| Domain | 1759 – 1872 | 114 | Cadherin 16 | ||||||||
| Domain | 1873 – 1968 | 96 | Cadherin 17 | ||||||||
| Domain | 1969 – 2070 | 102 | Cadherin 18 | ||||||||
| Domain | 2071 – 2171 | 101 | Cadherin 19 | ||||||||
| Domain | 2172 – 2272 | 101 | Cadherin 20 | ||||||||
| Domain | 2273 – 2379 | 107 | Cadherin 21 | ||||||||
| Domain | 2380 – 2481 | 102 | Cadherin 22 | ||||||||
| Domain | 2482 – 2585 | 104 | Cadherin 23 | ||||||||
| Domain | 2586 – 2692 | 107 | Cadherin 24 | ||||||||
| Domain | 2693 – 2799 | 107 | Cadherin 25 | ||||||||
| Domain | 2800 – 2908 | 109 | Cadherin 26 | ||||||||
| Domain | 2909 – 3013 | 105 | Cadherin 27 | ||||||||
| Domain | 3014 – 3115 | 102 | Cadherin 28 | ||||||||
| Domain | 3116 – 3220 | 105 | Cadherin 29 | ||||||||
| Domain | 3221 – 3323 | 103 | Cadherin 30 | ||||||||
| Domain | 3324 – 3428 | 105 | Cadherin 31 | ||||||||
| Domain | 3429 – 3533 | 105 | Cadherin 32 | ||||||||
| Domain | 3534 – 3631 | 98 | Cadherin 33 | ||||||||
| Domain | 3775 – 3946 | 172 | Laminin G-like | ||||||||
| Domain | 3949 – 3986 | 38 | EGF-like 1 | ||||||||
| Domain | 3988 – 4024 | 37 | EGF-like 2 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 39 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 210 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 280 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 330 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 459 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 568 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 627 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 789 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 996 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1175 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1276 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1417 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1899 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1998 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2007 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2102 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2165 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2183 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2325 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2368 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2387 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2430 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2470 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2547 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2597 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3127 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3278 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3312 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3432 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3603 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3770 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3774 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3815 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3842 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3875 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3906 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3991 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 3914 ↔ 3946 | By similarity | |||||||||
| Disulfide bond | 3953 ↔ 3964 | By similarity | |||||||||
| Disulfide bond | 3958 ↔ 3974 | By similarity | |||||||||
| Disulfide bond | 3976 ↔ 3985 | By similarity | |||||||||
| Disulfide bond | 3992 ↔ 4003 | By similarity | |||||||||
| Disulfide bond | 3997 ↔ 4012 | By similarity | |||||||||
| Disulfide bond | 4014 ↔ 4023 | By similarity | |||||||||
Sequences
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References
| [1] | "Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening." Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O. Genomics 51:27-34(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Brain. |
| [2] | Lubec G., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 673-681; 2566-2572; 2968-2976 AND 3081-3088, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain. |
| [3] | "MEGF1/fat2 proteins containing extraordinarily large extracellular domains are localized to thin parallel fibers of cerebellar granule cells." Nakayama M., Nakajima D., Yoshimura R., Endo Y., Ohara O. Mol. Cell. Neurosci. 20:563-578(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB011527 mRNA. Translation: BAA32458.1. |
| IPI | IPI00207544. |
| PIR | T00252. |
| RefSeq | NP_075243.1. NM_022954.1. |
| UniGene | Rn.137161. |
3D structure databases | |
| ProteinModelPortal | O88277. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000017106. |
PTM databases | |
| PhosphoSite | O88277. |
Proteomic databases | |
| PaxDb | O88277. |
| PRIDE | O88277. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 65048. |
| KEGG | rno:65048. |
| UCSC | RGD:620656. rat. |
Organism-specific databases | |
| CTD | 2196. |
| RGD | 620656. Fat2. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000046499. |
| HOVERGEN | HBG005641. |
| KO | K16506. |
| OrthoDB | EOG4N5VVX. |
Gene expression databases | |
| ArrayExpress | O88277. |
| Genevestigator | O88277. |
| GermOnline | ENSRNOG00000012575. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 1 hit. 2.60.40.60. 33 hits. |
| InterPro | IPR002126. Cadherin. IPR015919. Cadherin-like. IPR020894. Cadherin_CS. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000742. EG-like_dom. IPR013032. EGF-like_CS. IPR001791. Laminin_G. [Graphical view] |
| Pfam | PF00028. Cadherin. 27 hits. PF00008. EGF. 2 hits. PF02210. Laminin_G_2. 1 hit. [Graphical view] |
| PRINTS | PR00205. CADHERIN. |
| SMART | SM00112. CA. 33 hits. SM00181. EGF. 2 hits. SM00282. LamG. 1 hit. [Graphical view] |
| SUPFAM | SSF49313. Cadherin. 33 hits. SSF49899. ConA_like_lec_gl. 1 hit. |
| PROSITE | PS00232. CADHERIN_1. 14 hits. PS50268. CADHERIN_2. 33 hits. PS00022. EGF_1. 2 hits. PS01186. EGF_2. 2 hits. PS50026. EGF_3. 2 hits. PS50025. LAM_G_DOMAIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 613888. |
Entry information
| Entry name | FAT2_RAT | ||||||||
| Accession | Primary (citable) accession number: O88277 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
