ID G1NNC9_MELGA Unreviewed; 297 AA.
AC G1NNC9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Neuromodulin {ECO:0000256|ARBA:ARBA00021591, ECO:0000256|RuleBase:RU368113};
DE AltName: Full=Axonal membrane protein GAP-43 {ECO:0000256|ARBA:ARBA00030597, ECO:0000256|RuleBase:RU368113};
DE AltName: Full=Growth-associated protein 43 {ECO:0000256|ARBA:ARBA00033250, ECO:0000256|RuleBase:RU368113};
GN Name=GAP43 {ECO:0000313|Ensembl:ENSMGAP00000015149.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000015149.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000015149.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000015149.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: This protein is associated with nerve growth. It is a major
CC component of the motile 'growth cones' that form the tips of elongating
CC axons. Plays a role in axonal and dendritic filopodia induction.
CC {ECO:0000256|ARBA:ARBA00025215, ECO:0000256|RuleBase:RU368113}.
CC -!- SUBUNIT: Binds calmodulin with a greater affinity in the absence of
CC Ca(2+) than in its presence. {ECO:0000256|RuleBase:RU368113}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368113};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU368113};
CC Cytoplasmic side {ECO:0000256|RuleBase:RU368113}. Cell projection,
CC growth cone membrane {ECO:0000256|ARBA:ARBA00004503,
CC ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004503, ECO:0000256|RuleBase:RU368113};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004503,
CC ECO:0000256|RuleBase:RU368113}. Synapse {ECO:0000256|ARBA:ARBA00034103,
CC ECO:0000256|RuleBase:RU368113}. Cell projection, filopodium membrane
CC {ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU368113}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- PTM: Palmitoylated. Palmitoylation is essential for plasma membrane
CC association. {ECO:0000256|RuleBase:RU368113}.
CC -!- SIMILARITY: Belongs to the neuromodulin family.
CC {ECO:0000256|ARBA:ARBA00005890, ECO:0000256|RuleBase:RU368113}.
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DR AlphaFoldDB; G1NNC9; -.
DR Ensembl; ENSMGAT00000016098.3; ENSMGAP00000015149.3; ENSMGAG00000014319.3.
DR GeneTree; ENSGT00730000111265; -.
DR HOGENOM; CLU_102989_0_0_1; -.
DR InParanoid; G1NNC9; -.
DR Proteomes; UP000001645; Chromosome 1.
DR Bgee; ENSMGAG00000014319; Expressed in brain and 11 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0016198; P:axon choice point recognition; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:0060019; P:radial glial cell differentiation; IEA:Ensembl.
DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.190; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001422; Neuromodulin.
DR InterPro; IPR017454; Neuromodulin_C.
DR InterPro; IPR018947; Neuromodulin_gap-junction_N.
DR InterPro; IPR033137; Neuromodulin_P_site.
DR PANTHER; PTHR10699; NEUROMODULIN; 1.
DR PANTHER; PTHR10699:SF15; NEUROMODULIN; 1.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF06614; Neuromodulin; 1.
DR Pfam; PF10580; Neuromodulin_N; 1.
DR PRINTS; PR00215; NEUROMODULIN.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00413; NEUROMODULIN_2; 1.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW ECO:0000256|RuleBase:RU368113};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU368113};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|RuleBase:RU368113};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU368113};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782,
KW ECO:0000256|RuleBase:RU368113};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604,
KW ECO:0000256|RuleBase:RU368113};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU368113};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW ECO:0000256|RuleBase:RU368113}; Palmitate {ECO:0000256|RuleBase:RU368113};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU368113};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Signal {ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU368113}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..297
FT /note="Neuromodulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032575643"
FT DOMAIN 73..103
FT /note="Neuromodulin gap junction N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10580"
FT DOMAIN 140..282
FT /note="Neuromodulin (GAP-43) C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06614"
FT REGION 35..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 31755 MW; E2DB0B5FFA2A0E23 CRC64;
MCDERWLWTF QSLLAALVCV RVCVCACARE EREGGREGRG AERVGGRDKR EKRKRREEKE
GRRRKEGDNT IMLCCMRRTK QVEKNEDGDQ KIEQDGIKPE DKAHKAATKI QASFRGHITR
KKLKGEKKAD APASESEAAD KKDEGPAGGA AENKESEASA ATEASAADSA QLDEGSKDSS
APAEEKKGNG AADTGSEQPA PQAATPAASS EEKSAAAAET ESATKASTDN SPSLKADEAQ
DKEEPKQADV PAADTTATTT PAAEDATAKA TAATPNGDSG EQPNRREDRC CRRNQTY
//
