Q9C0C4 · SEM4C_HUMAN

  • Protein
    Semaphorin-4C
  • Gene
    SEMA4C
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cell surface receptor for PLXNB2 that plays an important role in cell-cell signaling. PLXNB2 binding promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248'. Required for normal brain development, axon guidance and cell migration (By similarity).
Probable signaling receptor which may play a role in myogenic differentiation through activation of the stress-activated MAPK cascade

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular space
Cellular Componentplasma membrane
Cellular Componentpostsynaptic density
Cellular Componentpostsynaptic density membrane
Cellular Componentsynaptic vesicle membrane
Molecular Functionchemorepellent activity
Molecular Functionsemaphorin receptor binding
Biological Processaxon guidance
Biological Processcell migration in hindbrain
Biological Processcerebellum development
Biological Processmuscle cell differentiation
Biological Processnegative chemotaxis
Biological Processneural crest cell migration
Biological Processneural tube closure
Biological Processpositive regulation of cell migration
Biological Processpositive regulation of stress-activated MAPK cascade
Biological Processsemaphorin-plexin signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Semaphorin-4C

Gene names

    • Name
      SEMA4C
    • Synonyms
      KIAA1739, SEMAI
    • ORF names
      UNQ5855/PRO34487

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9C0C4
  • Secondary accessions
    • Q32MJ3
    • Q7Z5X0

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain21-663Extracellular
Transmembrane664-684Helical
Topological domain685-833Cytoplasmic

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 780 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
Signal1-20UniProt
ChainPRO_000003232521-833UniProtSemaphorin-4C
Disulfide bond99↔110UniProt
Glycosylation106UniProtN-linked (GlcNAc...) asparagine
Glycosylation121UniProtN-linked (GlcNAc...) asparagine
Disulfide bond128↔137UniProt
Disulfide bond261↔370UniProt
Disulfide bond285↔330UniProt
Glycosylation310UniProtN-linked (GlcNAc...) asparagine
Glycosylation419UniProtN-linked (GlcNAc...) asparagine
Disulfide bond500↔517UniProt
Disulfide bond509↔526UniProt
Glycosylation522UniProtN-linked (GlcNAc...) asparagine
Glycosylation564UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)716PRIDEPhosphothreonine
Modified residue (large scale data)717PRIDEPhosphoserine
Modified residue742UniProtPhosphoserine
Modified residue (large scale data)742PRIDEPhosphoserine
Modified residue (large scale data)760PRIDEPhosphoserine
Modified residue (large scale data)772PRIDEPhosphoserine
Modified residue (large scale data)774PRIDEPhosphothreonine
Modified residue (large scale data)832PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Family & Domains

Features

Showing features for domain, region, compositional bias, motif.

TypeIDPosition(s)Description
Domain30-497Sema
Region46-489Dominant negative effect on myogenic differentiation
Domain499-551PSI
Domain556-644Ig-like C2-type
Region748-807Disordered
Compositional bias754-770Pro residues
Region814-833Disordered
Motif830-833PDZ-binding

Sequence similarities

Belongs to the semaphorin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    833
  • Mass (Da)
    92,623
  • Last updated
    2004-05-24 v2
  • Checksum
    075FDC0A392F0CE3
MAPHWAVWLLAARLWGLGIGAEVWWNLVPRKTVSSGELATVVRRFSQTGIQDFLTLTLTEPTGLLYVGAREALFAFSMEALELQGAISWEAPVEKKTECIQKGKNNQTECFNFIRFLQPYNASHLYVCGTYAFQPKCTYVNMLTFTLEHGEFEDGKGKCPYDPAKGHAGLLVDGELYSATLNNFLGTEPIILRNMGPHHSMKTEYLAFWLNEPHFVGSAYVPESVGSFTGDDDKVYFFFRERAVESDCYAEQVVARVARVCKGDMGGARTLQRKWTTFLKARLACSAPNWQLYFNQLQAMHTLQDTSWHNTTFFGVFQAQWGDMYLSAICEYQLEEIQRVFEGPYKEYHEEAQKWDRYTDPVPSPRPGSCINNWHRRHGYTSSLELPDNILNFVKKHPLMEEQVGPRWSRPLLVKKGTNFTHLVADRVTGLDGATYTVLFIGTGDGWLLKAVSLGPWVHLIEELQLFDQEPMRSLVLSQSKKLLFAGSRSQLVQLPVADCMKYRSCADCVLARDPYCAWSVNTSRCVAVGGHSGSLLIQHVMTSDTSGICNLRGSKKVRPTPKNITVVAGTDLVLPCHLSSNLAHARWTFGGRDLPAEQPGSFLYDARLQALVVMAAQPRHAGAYHCFSEEQGARLAAEGYLVAVVAGPSVTLEARAPLENLGLVWLAVVALGAVCLVLLLLVLSLRRRLREELEKGAKATERTLVYPLELPKEPTSPPFRPCPEPDEKLWDPVGYYYSDGSLKIVPGHARCQPGGGPPSPPPGIPGQPLPSPTRLHLGGGRNSNANGYVRLQLGGEDRGGLGHPLPELADELRRKLQQRQPLPDSNPEESSV

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J4M7C9J4M7_HUMANSEMA4C139
C9JV89C9JV89_HUMANSEMA4C201

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict602in Ref. 1; AAQ89201
Compositional bias754-770Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY358842
EMBL· GenBank· DDBJ
AAQ89201.1
EMBL· GenBank· DDBJ
mRNA
BC017476
EMBL· GenBank· DDBJ
AAH17476.2
EMBL· GenBank· DDBJ
mRNA
BC109103
EMBL· GenBank· DDBJ
AAI09104.1
EMBL· GenBank· DDBJ
mRNA
BC109104
EMBL· GenBank· DDBJ
AAI09105.1
EMBL· GenBank· DDBJ
mRNA
AB051526
EMBL· GenBank· DDBJ
BAB21830.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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