NEUM_MACFA
ID NEUM_MACFA Reviewed; 238 AA.
AC Q95K78;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Neuromodulin;
DE AltName: Full=Axonal membrane protein GAP-43;
DE AltName: Full=Growth-associated protein 43;
GN Name=GAP43; ORFNames=QtrA-11580, QtrA-13071;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P17677}.
CC -!- SUBUNIT: Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1,
CC FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts (via IQ
CC domain) with calmodulin (By similarity). Binds calmodulin with a
CC greater affinity in the absence of Ca(2+) than in its presence (By
CC similarity). {ECO:0000250|UniProtKB:P06836,
CC ECO:0000250|UniProtKB:P06837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone
CC membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P17677}. Synapse {ECO:0000250|UniProtKB:P17677}.
CC Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P17677};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}. Perikaryon
CC {ECO:0000250|UniProtKB:P07936}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P07936}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P07936}. Cytoplasm
CC {ECO:0000250|UniProtKB:P07936}. Note=Cytoplasmic surface of growth cone
CC and synaptic plasma membranes. {ECO:0000250|UniProtKB:P17677}.
CC -!- PTM: Phosphorylated (By similarity). Phosphorylation of this protein by
CC a protein kinase C is specifically correlated with certain forms of
CC synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P07936}.
CC -!- PTM: Palmitoylated by ZDHHC3 (By similarity). Palmitoylation is
CC regulated by ARF6 and is essential for plasma membrane association and
CC axonal and dendritic filopodia induction. Deacylated by LYPLA2 (By
CC similarity). {ECO:0000250|UniProtKB:P06837,
CC ECO:0000250|UniProtKB:P17677}.
CC -!- SIMILARITY: Belongs to the neuromodulin family. {ECO:0000305}.
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DR EMBL; AB063093; BAB60799.1; -; mRNA.
DR EMBL; AB169784; BAE01865.1; -; mRNA.
DR RefSeq; NP_001270699.1; NM_001283770.1.
DR RefSeq; XP_015300827.1; XM_015445341.1.
DR AlphaFoldDB; Q95K78; -.
DR SMR; Q95K78; -.
DR STRING; 9541.XP_005548147.1; -.
DR Ensembl; ENSMFAT00000026937; ENSMFAP00000003160; ENSMFAG00000041003.
DR GeneID; 102117213; -.
DR KEGG; mcf:102117213; -.
DR CTD; 2596; -.
DR VEuPathDB; HostDB:ENSMFAG00000041003; -.
DR eggNOG; ENOG502RXWF; Eukaryota.
DR GeneTree; ENSGT00730000111265; -.
DR OMA; GTPNKPE; -.
DR OrthoDB; 1531103at2759; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000041003; Expressed in temporal lobe and 5 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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 InterPro; IPR018243; Neuromodulin_palmitoyl_site.
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; PS00412; NEUROMODULIN_1; 1.
DR PROSITE; PS00413; NEUROMODULIN_2; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Developmental protein; Differentiation; Growth regulation; Lipoprotein;
KW Membrane; Neurogenesis; Palmitate; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..238
FT /note="Neuromodulin"
FT /id="PRO_0000250206"
FT DOMAIN 31..60
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine; by PHK and PKC"
FT /evidence="ECO:0000250|UniProtKB:P06836"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT MOD_RES 202
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P06836"
FT MOD_RES 203
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P06836"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
SQ SEQUENCE 238 AA; 24789 MW; 18BCA051E2519483 CRC64;
MLCCMRRTKQ VEKNDEDQKI EQDGIKPEDK AHKAATKIQA SFRGHITRKK LKGEKKDDAQ
AAEAEANKKD EAPVADGVEK KGEGTTATEA APATGSKPDE PGKAGETPSE EKKGEGDAAT
EQAAPQAPAS SEEKAGSAET ESATKASTDN SPSSKAEDAP AKEEPKQADV PAAVTAAAAT
TPAAEDAAAK ATAQPPTETG ESSQAEENIE AVDETKPKES ARQDEGKEEE PEADQEHA
