O75427 · LRCH4_HUMAN
- ProteinLeucine-rich repeat and calponin homology domain-containing protein 4
- GeneLRCH4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids683 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Accessory protein that regulates signaling by multiple TLRs, acting as a broad-spanning regulator of the innate immune response. In macrophages, binds LPS and promotes proper docking of LPS in lipid raft membrane. May be required for lipid raft maintenance.
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 | plasma membrane | |
Cellular Component | PML body | |
Biological Process | membrane raft assembly | |
Biological Process | nervous system development | |
Biological Process | positive regulation of toll-like receptor signaling pathway |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeucine-rich repeat and calponin homology domain-containing protein 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75427
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 653-673 | Helical | ||||
Sequence: LWPPSGLGGFVVFYVVLMLLL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051135 | 642 | in dbSNP:rs3197597 | |||
Sequence: V → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 851 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000084480 | 1-683 | UniProt | Leucine-rich repeat and calponin homology domain-containing protein 4 | |||
Sequence: MAAAVAAPLAAGGEEAAATTSVPGSPGLPGRRSAERALEEAVATGTLNLSNRRLKHFPRGAARSYDLSDITQADLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSLLPPYICQLPLRVLIVSNNKLGALPPDIGTLGSLRQLDVSSNELQSLPSELCGLSSLRDLNVRRNQLSTLPEELGDLPLVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQVCLKGKLHIFKYLSTEAGQRGSALGDLAPSRPPSFSPCPAEDLFPGHRYDGGLDSGFHSVDSGSKRWSGNESTDEFSELSFRISELAREPRGPRERKEDGSADGDPVQIDFIDSHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQERERRQQQQSGAWGAPRKDSLLKPGLRAVVGGAAAVSTQAMHNGSPKSSASQAGAAAGQGAPAPAPASQEPLPIAGPATAPAPRPLGSIQRPNSFLFRSSSQSGSGPSSPDSVLRPRRYPQVPDEKDLMTQLRQVLESRLQRPLPEDLAEALASGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKARKNVESFLEACRKMGVPEADLCSPSDLLQGTARGLRTALEAVKRVGGKALPPLWPPSGLGGFVVFYVVLMLLLYVTYTRLLGS | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 281 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 281 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 304 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 307 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 309 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 313 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 346 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 380 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 432 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 457 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 511 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 513 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 517 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 517 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 521 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 589 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75427 | CYB5R3 P00387 | 3 | EBI-718707, EBI-1046040 | |
BINARY | O75427 | DOCK6 Q96HP0 | 2 | EBI-718707, EBI-4401295 | |
BINARY | O75427 | DOCK7 Q96N67 | 2 | EBI-718707, EBI-2433703 | |
BINARY | O75427 | DOCK8 Q8NF50-3 | 2 | EBI-718707, EBI-25409271 | |
BINARY | O75427 | ELOVL7 A1L3X0 | 3 | EBI-718707, EBI-10285373 | |
BINARY | O75427 | HSD17B11 Q8NBQ5 | 3 | EBI-718707, EBI-1052304 | |
BINARY | O75427 | KASH5 Q8N6L0 | 3 | EBI-718707, EBI-749265 | |
BINARY | O75427 | KRT40 Q6A162 | 3 | EBI-718707, EBI-10171697 | |
BINARY | O75427 | KRTAP10-7 P60409 | 3 | EBI-718707, EBI-10172290 | |
BINARY | O75427 | KRTAP10-8 P60410 | 3 | EBI-718707, EBI-10171774 | |
BINARY | O75427 | MDFI Q99750 | 3 | EBI-718707, EBI-724076 | |
BINARY | O75427 | NOTCH2NLA Q7Z3S9 | 3 | EBI-718707, EBI-945833 | |
BINARY | O75427 | RETREG3 Q86VR2 | 3 | EBI-718707, EBI-10192441 | |
BINARY | O75427 | RNASEK Q6P5S7 | 3 | EBI-718707, EBI-18397230 | |
BINARY | O75427 | SUGT1 Q9Y2Z0 | 2 | EBI-718707, EBI-307008 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MAAAVAAPLAAGGEEAAATTSVPGSPGLPGRRSA | ||||||
Repeat | 41-64 | LRR 1 | ||||
Sequence: AVATGTLNLSNRRLKHFPRGAARS | ||||||
Repeat | 67-90 | LRR 2 | ||||
Sequence: LSDITQADLSRNRFPEVPEAACQL | ||||||
Repeat | 92-113 | LRR 3 | ||||
Sequence: SLEGLSLYHNCLRCLNPALGNL | ||||||
Repeat | 114-136 | LRR 4 | ||||
Sequence: TALTYLNLSRNQLSLLPPYICQL | ||||||
Repeat | 138-158 | LRR 5 | ||||
Sequence: LRVLIVSNNKLGALPPDIGTL | ||||||
Repeat | 159-181 | LRR 6 | ||||
Sequence: GSLRQLDVSSNELQSLPSELCGL | ||||||
Repeat | 182-204 | LRR 7 | ||||
Sequence: SSLRDLNVRRNQLSTLPEELGDL | ||||||
Repeat | 206-226 | LRR 8 | ||||
Sequence: LVRLDFSCNRVSRIPVSFCRL | ||||||
Repeat | 227-250 | LRR 9 | ||||
Sequence: RHLQVILLDSNPLQSPPAQVCLKG | ||||||
Region | 268-292 | Disordered | ||||
Sequence: ALGDLAPSRPPSFSPCPAEDLFPGH | ||||||
Compositional bias | 326-349 | Basic and acidic residues | ||||
Sequence: FRISELAREPRGPRERKEDGSADG | ||||||
Region | 326-436 | Disordered | ||||
Sequence: FRISELAREPRGPRERKEDGSADGDPVQIDFIDSHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQERERRQQQQSGAWGAPRKDSLLKP | ||||||
Compositional bias | 359-413 | Basic and acidic residues | ||||
Sequence: SHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQE | ||||||
Region | 449-539 | Disordered | ||||
Sequence: STQAMHNGSPKSSASQAGAAAGQGAPAPAPASQEPLPIAGPATAPAPRPLGSIQRPNSFLFRSSSQSGSGPSSPDSVLRPRRYPQVPDEKD | ||||||
Compositional bias | 450-467 | Polar residues | ||||
Sequence: TQAMHNGSPKSSASQAGA | ||||||
Compositional bias | 478-492 | Pro residues | ||||
Sequence: PASQEPLPIAGPATA | ||||||
Compositional bias | 504-522 | Polar residues | ||||
Sequence: PNSFLFRSSSQSGSGPSSP | ||||||
Domain | 534-647 | Calponin-homology (CH) | ||||
Sequence: VPDEKDLMTQLRQVLESRLQRPLPEDLAEALASGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKARKNVESFLEACRKMGVPEADLCSPSDLLQGTARGLRTALEAVKRVGG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length683
- Mass (Da)73,450
- Last updated2004-06-21 v2
- ChecksumAF297AA30E4DA353
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H7C5D9 | H7C5D9_HUMAN | LRCH4 | 652 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 40 | in Ref. 1; AAC78793 | ||||
Sequence: E → D | ||||||
Compositional bias | 326-349 | Basic and acidic residues | ||||
Sequence: FRISELAREPRGPRERKEDGSADG | ||||||
Compositional bias | 359-413 | Basic and acidic residues | ||||
Sequence: SHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQE | ||||||
Sequence conflict | 391 | in Ref. 1; AAC78793 | ||||
Sequence: S → N | ||||||
Compositional bias | 450-467 | Polar residues | ||||
Sequence: TQAMHNGSPKSSASQAGA | ||||||
Sequence conflict | 467-473 | in Ref. 1; AAC78793 | ||||
Sequence: AAAGQGA → GCSGAGS | ||||||
Compositional bias | 478-492 | Pro residues | ||||
Sequence: PASQEPLPIAGPATA | ||||||
Compositional bias | 504-522 | Polar residues | ||||
Sequence: PNSFLFRSSSQSGSGPSSP | ||||||
Sequence conflict | 682-683 | in Ref. 1 | ||||
Sequence: GS → DP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF053356 EMBL· GenBank· DDBJ | AAC78793.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CH236956 EMBL· GenBank· DDBJ | EAL23828.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007634 EMBL· GenBank· DDBJ | AAH07634.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018529 EMBL· GenBank· DDBJ | AAH18529.3 EMBL· GenBank· DDBJ | mRNA |