Q92614 · MY18A_HUMAN

  • Protein
    Unconventional myosin-XVIIIa
  • Gene
    MYO18A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May link Golgi membranes to the cytoskeleton and participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus (PubMed:19837035, PubMed:23345592).
Alternatively, in concert with LURAP1 and CDC42BPA/CDC42BPB, has been involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160).
May be involved in the maintenance of the stromal cell architectures required for cell to cell contact (By similarity).
Regulates trafficking, expression, and activation of innate immune receptors on macrophages. Plays a role to suppress inflammatory responsiveness of macrophages via a mechanism that modulates CD14 trafficking (PubMed:25965346).
Acts as a receptor of surfactant-associated protein A (SFTPA1/SP-A) and plays an important role in internalization and clearance of SFTPA1-opsonized S.aureus by alveolar macrophages (PubMed:16087679, PubMed:21123169).
Strongly enhances natural killer cell cytotoxicity (PubMed:27467939).

Caution

The TIAF1 protein is coded in the 3'-UTR region of MYO18A.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site498-505ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentactomyosin
Cellular Componentcell surface
Cellular Componentcytoplasm
Cellular Componentendoplasmic reticulum-Golgi intermediate compartment
Cellular ComponentGolgi membrane
Cellular Componentmembrane
Cellular Componentmicrotubule organizing center
Cellular Componentmyosin filament
Cellular Componentmyosin II complex
Cellular Componenttrans-Golgi network
Molecular Functionactin filament binding
Molecular FunctionADP binding
Molecular FunctionATP binding
Molecular FunctionATP-dependent activity, acting on DNA
Molecular FunctionDNA binding
Molecular FunctionRNA binding
Biological Processactomyosin structure organization
Biological Processasymmetric Golgi ribbon formation
Biological Processcell migration
Biological ProcessDNA metabolic process
Biological ProcessGolgi organization
Biological ProcessGolgi ribbon formation
Biological ProcessGolgi vesicle budding
Biological Processnegative regulation of apoptotic process
Biological Processpositive regulation of opsonization
Biological Processpositive regulation of protein secretion
Biological Processregulation of macrophage activation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Unconventional myosin-XVIIIa
  • Alternative names
    • Molecule associated with JAK3 N-terminus (MAJN)
    • Myosin containing a PDZ domain
    • Surfactant protein receptor SP-R210
      (SP-R210
      )

Gene names

    • Name
      MYO18A
    • Synonyms
      CD245
      , KIAA0216, MYSPDZ, TIAF1

Organism names

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

Accessions

  • Primary accession
    Q92614
  • Secondary accessions
    • Q5H9U3
    • Q5QD01
    • Q5W9F9
    • Q5W9G1
    • Q8IXP8

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus
Golgi outpost
Note: Recruited to the Golgi apparatus by GOLPH3 (PubMed:19837035).
Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity).

Isoform 1

Note: Colocalizes with actin.

Isoform 2

Cytoplasm
Note: Lacks the PDZ domain (PubMed:12761286).
Diffusely localized in the cytoplasm (PubMed:12761286).

Isoform 5

Cell surface

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis114-115No effect on interaction with actin.
Mutagenesis117-118Abolishes interaction with actin.
Natural variantVAR_030585958in dbSNP:rs8076604

Variants

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

The viewer provides 2,159 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 chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001234761-2054UniProtUnconventional myosin-XVIIIa
Modified residue35UniProtPhosphoserine
Modified residue (large scale data)35PRIDEPhosphoserine
Modified residue (large scale data)51PRIDEPhosphoserine
Modified residue52UniProtPhosphoserine
Modified residue (large scale data)52PRIDEPhosphoserine
Modified residue72UniProtPhosphoserine
Modified residue (large scale data)72PRIDEPhosphoserine
Modified residue74UniProtPhosphoserine
Modified residue (large scale data)74PRIDEPhosphoserine
Modified residue79UniProtPhosphothreonine
Modified residue83UniProtPhosphoserine
Modified residue (large scale data)83PRIDEPhosphoserine
Modified residue (large scale data)85PRIDEPhosphoserine
Modified residue98UniProtPhosphoserine
Modified residue99UniProtPhosphothreonine
Modified residue (large scale data)99PRIDEPhosphothreonine
Modified residue (large scale data)101PRIDEPhosphoserine
Modified residue102UniProtPhosphoserine
Modified residue (large scale data)102PRIDEPhosphoserine
Modified residue103UniProtPhosphoserine
Modified residue (large scale data)112PRIDEPhosphoserine
Modified residue (large scale data)116PRIDEPhosphoserine
Modified residue (large scale data)132PRIDEPhosphoserine
Modified residue140UniProtPhosphoserine
Modified residue (large scale data)140PRIDEPhosphoserine
Modified residue (large scale data)142PRIDEPhosphoserine
Modified residue145UniProtPhosphoserine
Modified residue (large scale data)145PRIDEPhosphoserine
Modified residue (large scale data)149PRIDEPhosphoserine
Modified residue157UniProtPhosphoserine
Modified residue (large scale data)157PRIDEPhosphoserine
Modified residue160UniProtPhosphoserine
Modified residue (large scale data)160PRIDEPhosphoserine
Modified residue164UniProtPhosphoserine
Modified residue (large scale data)164PRIDEPhosphoserine
Modified residue (large scale data)228PRIDEPhosphothreonine
Modified residue234UniProtPhosphoserine
Modified residue (large scale data)234PRIDEPhosphoserine
Modified residue (large scale data)403PRIDEPhosphoserine
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue (large scale data)736PRIDEPhosphoserine
Modified residue (large scale data)806PRIDEPhosphoserine
Modified residue (large scale data)980PRIDEPhosphoserine
Modified residue (large scale data)982PRIDEPhosphothreonine
Modified residue (large scale data)985PRIDEPhosphoserine
Modified residue987UniProtPhosphoserine
Modified residue (large scale data)987PRIDEPhosphoserine
Modified residue (large scale data)1008PRIDEPhosphothreonine
Modified residue1067UniProtPhosphoserine
Modified residue (large scale data)1067PRIDEPhosphoserine
Modified residue1068UniProtPhosphoserine
Modified residue (large scale data)1068PRIDEPhosphoserine
Modified residue1070UniProtPhosphoserine
Modified residue (large scale data)1070PRIDEPhosphoserine
Modified residue (large scale data)1076PRIDEPhosphoserine
Modified residue (large scale data)1309PRIDEPhosphoserine
Modified residue1501UniProtIn isoform Q92614-5; Phosphoserine
Modified residue (large scale data)1528PRIDEPhosphoserine
Modified residue1640UniProtPhosphoserine
Modified residue (large scale data)1640PRIDEPhosphoserine
Modified residue1843UniProtPhosphoserine
Modified residue1922UniProtIn isoform Q92614-3; Phosphoserine
Modified residue1942UniProtPhosphoserine
Modified residue (large scale data)1942PRIDEPhosphoserine
Modified residue1959UniProtIn isoform Q92614-4; Phosphoserine
Modified residue1970UniProtPhosphoserine
Modified residue (large scale data)1970PRIDEPhosphoserine
Modified residue1974UniProtPhosphoserine
Modified residue (large scale data)1974PRIDEPhosphoserine
Modified residue1998UniProtPhosphoserine
Modified residue (large scale data)1998PRIDEPhosphoserine
Modified residue2002UniProtPhosphoserine
Modified residue (large scale data)2002PRIDEPhosphoserine
Modified residue (large scale data)2005PRIDEPhosphoserine
Modified residue2006UniProtPhosphoserine
Modified residue (large scale data)2006PRIDEPhosphoserine
Modified residue2007UniProtPhosphoserine
Modified residue (large scale data)2007PRIDEPhosphoserine
Modified residue2014UniProtPhosphoserine
Modified residue (large scale data)2014PRIDEPhosphoserine
Modified residue2020UniProtPhosphoserine
Modified residue (large scale data)2020PRIDEPhosphoserine
Modified residue (large scale data)2030PRIDEPhosphothreonine
Modified residue (large scale data)2031PRIDEPhosphoserine
Modified residue2035UniProtPhosphotyrosine
Modified residue (large scale data)2035PRIDEPhosphotyrosine
Modified residue2036UniProtPhosphoserine
Modified residue (large scale data)2036PRIDEPhosphoserine
Modified residue (large scale data)2038PRIDEPhosphoserine
Modified residue (large scale data)2039PRIDEPhosphotyrosine
Modified residue2041UniProtPhosphoserine
Modified residue (large scale data)2041PRIDEPhosphoserine
Modified residue2043UniProtPhosphoserine
Modified residue (large scale data)2043PRIDEPhosphoserine
Modified residue2045UniProtPhosphothreonine
Modified residue (large scale data)2045PRIDEPhosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer. Forms a tripartite complex with CDC42BPA/CDC42BPB and LURAP1 with the latter acting as an adapter connecting CDC42BPA/CDC42BPB and MYO18A. Binds F-actin; regulated by ADP and GOLPH3. Interacts with GOLPH3; the interaction is direct and may link Golgi membranes to the actin cytoskeleton. Interacts with JAK3. Interacts with MSR1 and CD14 (PubMed:25965346).
Isoform 5 interacts with CD11B (PubMed:25965346).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q92614GOLPH3 Q9H4A66EBI-949059, EBI-2465479

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-34Disordered
Region1-398Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3
Motif114-118Interaction with actin
Compositional bias140-164Polar residues
Region140-167Disordered
Domain220-311PDZ
Region318-338Disordered
Compositional bias322-338Basic and acidic residues
Domain349-401Myosin N-terminal SH3-like
Domain405-1185Myosin motor
Domain1188-1217IQ
Coiled coil1246-1971
Region1450-1480Disordered
Region1852-1901Disordered
Compositional bias1962-1985Basic and acidic residues
Region1962-2054Disordered
Compositional bias1999-2014Polar residues
Compositional bias2016-2031Basic and acidic residues
Compositional bias2032-2054Polar residues

Domain

The myosin motor domain binds ADP and ATP but has no intrinsic ATPase activity. Mediates ADP-dependent binding to actin (PubMed:23990465).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (6)
  • Sequence status
    Complete

This entry describes 6 isoforms produced by Alternative splicing.

Q92614-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    1
  • Synonyms
    Alpha, SP-R210L
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    2,054
  • Mass (Da)
    233,115
  • Last updated
    2003-07-25 v3
  • Checksum
    52BFA0AA273E18F7
MFNLMKKDKDKDGGRKEKKEKKEKKERMSAAELRSLEEMSLRRGFFNLNRSSKRESKTRLEISNPIPIKVASGSDLHLTDIDSDSNRGSVILDSGHLSTASSSDDLKGEEGSFRGSVLQRAAKFGSLAKQNSQMIVKRFSFSQRSRDESASETSTPSEHSAAPSPQVEVRTLEGQLVQHPGPGIPRPGHRSRAPELVTKKFPVDLRLPPVVPLPPPTLRELELQRRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQPIPELSELSRSWLRSGEGPRREPSDAKTEEQIAAEEAWNETEKVWLVHRDGFSLASQLKSEELNLPEGKVRVKLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRQGPEESGLGDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGEPRSASSRRVSSSSELDLPSGDHCEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDERRAVEELLECLDLEKSSCCMGLSRVFFRAGTLARLEEQRDEQTSRNLTLFQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKRKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAASDDGSLKSSSPTSYWKSLAPDRSDDEHDPLDNTSRPRYSHSYLSDSDTEAKLTETNA

Q92614-2

  • Name
    2
  • Synonyms
    Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q92614-3

Q92614-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q92614-5

  • Name
    5
  • Synonyms
    SP-R210S
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

O95411-1

The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

View isoform
  • Name
    TIAF1
  • See also
    sequence in UniParc or sequence clusters in UniRef

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
O95411TIAF1_HUMANMYO18A115
H0YEV9H0YEV9_HUMANMYO18A172
A0A1B0GV45A0A1B0GV45_HUMANMYO18A464
A0A1B0GWJ6A0A1B0GWJ6_HUMANMYO18A340
E9PN42E9PN42_HUMANMYO18A27
K7EKB3K7EKB3_HUMANMYO18A93
A0A994J771A0A994J771_HUMANMYO18A2051

Sequence caution

The sequence BAA13206.2 differs from that shown. Reason: Erroneous initiation
The sequence BAD66838.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0078691-331in isoform 2
Alternative sequenceVSP_0230581-458in isoform 5
Compositional bias140-164Polar residues
Compositional bias322-338Basic and acidic residues
Alternative sequenceVSP_007870332-333in isoform 2
Sequence conflict1014in Ref. 1; BAD66838 and 2; AAV80770
Sequence conflict1020in Ref. 4; CAI45931
Alternative sequenceVSP_0078711571-1607in isoform 3
Sequence conflict1757in Ref. 4; CAI45931
Sequence conflict1889in Ref. 4; CAI45931
Alternative sequenceVSP_0078721952-1966in isoform 3, isoform 4 and isoform 5
Compositional bias1962-1985Basic and acidic residues
Compositional bias1999-2014Polar residues
Compositional bias2016-2031Basic and acidic residues
Compositional bias2032-2054Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB177858
EMBL· GenBank· DDBJ
BAD66836.1
EMBL· GenBank· DDBJ
mRNA
AB177860
EMBL· GenBank· DDBJ
BAD66838.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AY703984
EMBL· GenBank· DDBJ
AAV80770.1
EMBL· GenBank· DDBJ
mRNA
D86970
EMBL· GenBank· DDBJ
BAA13206.2
EMBL· GenBank· DDBJ
mRNA Different initiation
CR933614
EMBL· GenBank· DDBJ
CAI45931.1
EMBL· GenBank· DDBJ
mRNA
BC039612
EMBL· GenBank· DDBJ
AAH39612.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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