Q19350 · Q19350_CAEEL
- ProteinDrosophila CRumBs homolog
- Genecrb-1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1722 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apical part of cell | |
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | calcium ion binding | |
Biological Process | cell differentiation | |
Biological Process | establishment or maintenance of epithelial cell apical/basal polarity | |
Biological Process | heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ19350
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1659-1685 | Helical | ||||
Sequence: ISYLFGPIIAVVIVFAILGCLLLFFVI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MKYQHFLIFCTLVTNALCNRACS | ||||||
Chain | PRO_5004187124 | 24-1722 | ||||
Sequence: RNTCLNGGTCTVNDETRMFQCECPKGFSGLLCQDNCSLHCLHGNCVKGTFGEETCQCSEGWMGSLCDNLVTDDDTAQKCSPQCGDDERCTKGADGSYICQSNEPSCATHTCQNNGTCVAENGNVKCACPPGFVGDHCETDEDECKENFCQNGADCENLKGSYECKCLKGFSGKYCEIQDKKQCTSDYCHNNGQCISTGSDLSCKCSPGFDGAFCELKAEVNECICENPAHVCSLVNGTSRTTQCECPSGFMGADCKELQARPCDREPCLNGGHCVDDGQNLFTCFCLPSFTGIYCGEPVDCLVNGSDCKNGGKCVFALAATTCQCPEGFNGSNCEISNSYRSHPTCSDIRCLNGGSCKLDAEGEPFCVCEEGFDGPFCEPKSGCTINPCQNGGTCQDADGQYFCHCTSGFGGVHCETVDEPSTPIPTLGTFPSFTTSGIDGFSQSKISCEDCVNSSNCLDVESGPVCICDDGYFGQKCDQKHDKCSKVSCPSGQTCSQVNDNVNITAQCGCEIGHFGQQCEMVTSATFSAKSLYIHQSSKFSLGTSSFENIAYELEFSFRTTVENTHLASSENILGEKILSIQLLSGYLVFNMTGNSLEHLLPMRVSDAQWYTVFVKGEDNKIQIEVSTENGFSLVQKSVNGQLEVFLTRFGKISGTHHFIGCMADVRVDGDLIIFADNKRAIDIRKGCTRSEQCTRAYCQNEGICIDHWESSSCKCKPPYLKPNCVYFLPKTTFGHLDQPSIVHLSTSESENHLLRNHIELSFLMHSGKPDAVLFYIGEKHAADVLTNYLVVKIAGGLITVRYRTGGRREIEFSSKNRVDDNQEHHVQIFLDKTTRQIIIDDLIECSEPIISRMSQEFYVDDIVIGASNVVATDSEFYKGYLQDIQINQKSVVIHPTSLTIDKIGKLERTQNVIEGAVSDPMCSSSTCKHGECSETFNDFTCRCSDGSTGKLCDKVDYCKDASCMKGSRCENADNGHYCIFPITISNGSMLTYSLAPTKFMTLPSIEFSIKAHSQNGHIFTLTIDKSTLSAYLFKKRLALATNSGSGTIQKFDSVIADGNWHQIILNPHKVLIDSVKFISDNQLYPAESKSGASLFVGEQEPQEVTFACLDLFKMGEYPTLSFTKVKIPTNSETWNLTDKASVGTGCMSTDQCGLYSTCLNGATCVDIWNKRKCVCPAGFAGENCEDNVNDCKFVDCGKHGYCLDGIDEAKCICNNGFHGEHCELAKDECEGVECHNGGKCVKNRSEKIVCQCGNSWMGDSCNVTKTTNCKDSPCQNFGQCMQKTDTFFECNCMDGYSGELCEQRDVNECNHYDCNRGHCVMTVSGPACQCEMGYTGRFCEKLLNQCSSNTCSSRGACSPVWNNTVCNCDNNWRGAHCQHQMDTCLDFPCNNDGVCRTNDENTFSCECQKFFMGTRCEIEGSCLKAQCVHGECIQLSPETHTCSCNIGYEGDACDKKIDYCKAGPCLNGANCENKLTGYKCTCAVGFEGADCEINIDECALEFCKNGAKCRDKINDYECVCDGTGFEGRNCTTDINECANPNNCINGECTNTLGNYKCACRNGFIGPRCSVRNPCTAQIASNNISSVTCVHGKCVNPVVQIEKNREVAKYECACDRGYTGPTCSQRIKESAMSNISYLFGPIIAVVIVFAILGCLLLFFVIRGNNAMHGHYSPSSHEFTQNRMAMPTVIKLPPQERLI | ||||||
Disulfide bond | 27↔44 | |||||
Sequence: CLNGGTCTVNDETRMFQC | ||||||
Disulfide bond | 46↔55 | |||||
Sequence: CPKGFSGLLC | ||||||
Disulfide bond | 151↔160 | |||||
Sequence: CPPGFVGDHC | ||||||
Disulfide bond | 189↔198 | |||||
Sequence: CLKGFSGKYC | ||||||
Disulfide bond | 228↔237 | |||||
Sequence: CSPGFDGAFC | ||||||
Disulfide bond | 269↔278 | |||||
Sequence: CPSGFMGADC | ||||||
Disulfide bond | 309↔318 | |||||
Sequence: CLPSFTGIYC | ||||||
Disulfide bond | 348↔357 | |||||
Sequence: CPEGFNGSNC | ||||||
Disulfide bond | 392↔401 | |||||
Sequence: CEEGFDGPFC | ||||||
Disulfide bond | 429↔438 | |||||
Sequence: CTSGFGGVHC | ||||||
Disulfide bond | 492↔501 | |||||
Sequence: CDDGYFGQKC | ||||||
Disulfide bond | 534↔543 | |||||
Sequence: CEIGHFGQQC | ||||||
Disulfide bond | 740↔749 | |||||
Sequence: CKPPYLKPNC | ||||||
Disulfide bond | 947↔957 | |||||
Sequence: CSSSTCKHGEC | ||||||
Disulfide bond | 968↔977 | |||||
Sequence: CSDGSTGKLC | ||||||
Disulfide bond | 1200↔1209 | |||||
Sequence: CPAGFAGENC | ||||||
Disulfide bond | 1238↔1247 | |||||
Sequence: CNNGFHGEHC | ||||||
Disulfide bond | 1277↔1286 | |||||
Sequence: CGNSWMGDSC | ||||||
Disulfide bond | 1317↔1326 | |||||
Sequence: CMDGYSGELC | ||||||
Disulfide bond | 1334↔1344 | |||||
Sequence: CNHYDCNRGHC | ||||||
Disulfide bond | 1355↔1364 | |||||
Sequence: CEMGYTGRFC | ||||||
Disulfide bond | 1393↔1402 | |||||
Sequence: CDNNWRGAHC | ||||||
Disulfide bond | 1432↔1441 | |||||
Sequence: CQKFFMGTRC | ||||||
Disulfide bond | 1447↔1457 | |||||
Sequence: CLKAQCVHGEC | ||||||
Disulfide bond | 1469↔1478 | |||||
Sequence: CNIGYEGDAC | ||||||
Disulfide bond | 1507↔1516 | |||||
Sequence: CAVGFEGADC | ||||||
Disulfide bond | 1584↔1593 | |||||
Sequence: CRNGFIGPRC | ||||||
Disulfide bond | 1638↔1647 | |||||
Sequence: CDRGYTGPTC |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-56 | EGF-like | ||||
Sequence: NRACSRNTCLNGGTCTVNDETRMFQCECPKGFSGLLCQ | ||||||
Domain | 125-161 | EGF-like | ||||
Sequence: NEPSCATHTCQNNGTCVAENGNVKCACPPGFVGDHCE | ||||||
Domain | 163-199 | EGF-like | ||||
Sequence: DEDECKENFCQNGADCENLKGSYECKCLKGFSGKYCE | ||||||
Domain | 202-238 | EGF-like | ||||
Sequence: DKKQCTSDYCHNNGQCISTGSDLSCKCSPGFDGAFCE | ||||||
Domain | 242-279 | EGF-like | ||||
Sequence: EVNECICENPAHVCSLVNGTSRTTQCECPSGFMGADCK | ||||||
Domain | 282-319 | EGF-like | ||||
Sequence: QARPCDREPCLNGGHCVDDGQNLFTCFCLPSFTGIYCG | ||||||
Domain | 320-358 | EGF-like | ||||
Sequence: EPVDCLVNGSDCKNGGKCVFALAATTCQCPEGFNGSNCE | ||||||
Domain | 365-402 | EGF-like | ||||
Sequence: SHPTCSDIRCLNGGSCKLDAEGEPFCVCEEGFDGPFCE | ||||||
Domain | 403-439 | EGF-like | ||||
Sequence: PKSGCTINPCQNGGTCQDADGQYFCHCTSGFGGVHCE | ||||||
Domain | 468-502 | EGF-like | ||||
Sequence: SKISCEDCVNSSNCLDVESGPVCICDDGYFGQKCD | ||||||
Domain | 504-544 | EGF-like | ||||
Sequence: KHDKCSKVSCPSGQTCSQVNDNVNITAQCGCEIGHFGQQCE | ||||||
Domain | 553-712 | Laminin G | ||||
Sequence: AKSLYIHQSSKFSLGTSSFENIAYELEFSFRTTVENTHLASSENILGEKILSIQLLSGYLVFNMTGNSLEHLLPMRVSDAQWYTVFVKGEDNKIQIEVSTENGFSLVQKSVNGQLEVFLTRFGKISGTHHFIGCMADVRVDGDLIIFADNKRAIDIRKGC | ||||||
Domain | 714-750 | EGF-like | ||||
Sequence: RSEQCTRAYCQNEGICIDHWESSSCKCKPPYLKPNCV | ||||||
Domain | 756-947 | Laminin G | ||||
Sequence: TTFGHLDQPSIVHLSTSESENHLLRNHIELSFLMHSGKPDAVLFYIGEKHAADVLTNYLVVKIAGGLITVRYRTGGRREIEFSSKNRVDDNQEHHVQIFLDKTTRQIIIDDLIECSEPIISRMSQEFYVDDIVIGASNVVATDSEFYKGYLQDIQINQKSVVIHPTSLTIDKIGKLERTQNVIEGAVSDPMC | ||||||
Domain | 943-978 | EGF-like | ||||
Sequence: SDPMCSSSTCKHGECSETFNDFTCRCSDGSTGKLCD | ||||||
Domain | 1173-1210 | EGF-like | ||||
Sequence: STDQCGLYSTCLNGATCVDIWNKRKCVCPAGFAGENCE | ||||||
Domain | 1212-1248 | EGF-like | ||||
Sequence: NVNDCKFVDCGKHGYCLDGIDEAKCICNNGFHGEHCE | ||||||
Domain | 1250-1287 | EGF-like | ||||
Sequence: AKDECEGVECHNGGKCVKNRSEKIVCQCGNSWMGDSCN | ||||||
Domain | 1290-1327 | EGF-like | ||||
Sequence: KTTNCKDSPCQNFGQCMQKTDTFFECNCMDGYSGELCE | ||||||
Domain | 1330-1365 | EGF-like | ||||
Sequence: DVNECNHYDCNRGHCVMTVSGPACQCEMGYTGRFCE | ||||||
Domain | 1367-1403 | EGF-like | ||||
Sequence: LLNQCSSNTCSSRGACSPVWNNTVCNCDNNWRGAHCQ | ||||||
Domain | 1405-1442 | EGF-like | ||||
Sequence: QMDTCLDFPCNNDGVCRTNDENTFSCECQKFFMGTRCE | ||||||
Domain | 1443-1479 | EGF-like | ||||
Sequence: IEGSCLKAQCVHGECIQLSPETHTCSCNIGYEGDACD | ||||||
Domain | 1481-1517 | EGF-like | ||||
Sequence: KIDYCKAGPCLNGANCENKLTGYKCTCAVGFEGADCE | ||||||
Domain | 1519-1556 | EGF-like | ||||
Sequence: NIDECALEFCKNGAKCRDKINDYECVCDGTGFEGRNCT | ||||||
Domain | 1558-1594 | EGF-like | ||||
Sequence: DINECANPNNCINGECTNTLGNYKCACRNGFIGPRCS | ||||||
Domain | 1609-1648 | EGF-like | ||||
Sequence: SSVTCVHGKCVNPVVQIEKNREVAKYECACDRGYTGPTCS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,722
- Mass (Da)188,385
- Last updated1996-11-01 v1
- ChecksumE74A3B6D9A2BDC31
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284606 EMBL· GenBank· DDBJ | CCD66913.1 EMBL· GenBank· DDBJ | Genomic DNA |