NEUM_PANTR
ID NEUM_PANTR Reviewed; 238 AA.
AC Q5IS67;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Neuromodulin;
DE AltName: Full=Axonal membrane protein GAP-43;
DE AltName: Full=Growth-associated protein 43;
GN Name=GAP43;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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; AY665261; AAV74299.1; -; mRNA.
DR RefSeq; NP_001009816.1; NM_001009816.1.
DR AlphaFoldDB; Q5IS67; -.
DR SMR; Q5IS67; -.
DR STRING; 9598.ENSPTRP00000026293; -.
DR PaxDb; Q5IS67; -.
DR Ensembl; ENSPTRT00000085660; ENSPTRP00000082104; ENSPTRG00000015246.
DR GeneID; 460599; -.
DR KEGG; ptr:460599; -.
DR CTD; 2596; -.
DR VGNC; VGNC:11399; GAP43.
DR eggNOG; ENOG502RXWF; Eukaryota.
DR GeneTree; ENSGT00730000111265; -.
DR HOGENOM; CLU_102989_0_0_1; -.
DR InParanoid; Q5IS67; -.
DR OMA; GTPNKPE; -.
DR TreeFam; TF333213; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000015246; Expressed in Brodmann (1909) area 10 and 13 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0035727; F:lysophosphatidic acid binding; IBA:GO_Central.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0016198; P:axon choice point recognition; IBA:GO_Central.
DR GO; GO:0031103; P:axon regeneration; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0042246; P:tissue regeneration; IBA:GO_Central.
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_0000159598"
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:P06836"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P06836"
SQ SEQUENCE 238 AA; 24803 MW; B3536D012A127CC8 CRC64;
MLCCMRRTKQ VEKNDDDQKI EQDGIKPEDK AHKAATKIQA SFRGHITRKK LKGEKKDDVQ
AAEAEANKKD EAPVADGVEK KGEGTTTAEA APATGSKPDE PGKAGETPSE EKKGEGDAAT
EQAAPQAPAS SEEKAGSAET ESATKASTDN SPSSKAEDAP AKEEPKQADV PAAVTAAAAT
TPAAEDAAAK ATAQPPTETG ESSQAEENIE AVDETKPKES ARQDEGKEEE PEADQEHA
