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NEUM_CHICK
ID   NEUM_CHICK              Reviewed;         246 AA.
AC   P35001;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Neuromodulin;
DE   AltName: Full=Axonal membrane protein GAP-43;
DE   AltName: Full=Growth-associated protein 43;
GN   Name=GAP43;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=2153895; DOI=10.1016/0169-328x(90)90074-n;
RA   Baizer L., Alkan S., Stocker K., Ciment G.;
RT   "Chicken growth-associated protein (GAP)-43: primary structure and
RT   regulated expression of mRNA during embryogenesis.";
RL   Brain Res. Mol. Brain Res. 7:61-68(1990).
RN   [2]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PALMITOYLATION.
RX   PubMed=9813098; DOI=10.1083/jcb.143.3.795;
RA   Kutzleb C., Sanders G., Yamamoto R., Wang X., Lichte B.,
RA   Petrasch-Parwez E., Kilimann M.W.;
RT   "Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in neurons
RT   and implicated in plasma membrane dynamics and cell process formation.";
RL   J. Cell Biol. 143:795-813(1998).
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: Binds calmodulin with a greater affinity in the absence of
CC       Ca(2+) than in its presence. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9813098};
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:0000269|PubMed:9813098}.
CC       Cell projection, filopodium membrane {ECO:0000269|PubMed:9813098};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}.
CC   -!- TISSUE SPECIFICITY: Expressed in neurons. {ECO:0000269|PubMed:9813098}.
CC   -!- DEVELOPMENTAL STAGE: First expressed in the body and head at embryonic
CC       stage E3 (PubMed:2153895). Expressed in the mid-thoracic region of
CC       embryos and also in the spinal cord, dorsal root and sympathetic
CC       ganglia at embryonic stage E10 (PubMed:2153895). Highly expressed in
CC       the brain at embryonic stage E13 (PubMed:2153895). Expressed at low
CC       levels in the gut at embryonic stage E16 (PubMed:2153895). Not
CC       expressed in heart, skeletal muscle or liver at embryonic stage E16
CC       (PubMed:2153895). {ECO:0000269|PubMed:2153895}.
CC   -!- PTM: Palmitoylated (PubMed:9813098). Palmitoylation is essential for
CC       plasma membrane association (PubMed:9813098).
CC       {ECO:0000269|PubMed:9813098}.
CC   -!- SIMILARITY: Belongs to the neuromodulin family. {ECO:0000305}.
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DR   PIR; A60049; A60049.
DR   AlphaFoldDB; P35001; -.
DR   VEuPathDB; HostDB:geneid_427955; -.
DR   eggNOG; ENOG502RXWF; Eukaryota.
DR   InParanoid; P35001; -.
DR   PhylomeDB; P35001; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR   GO; GO:0097060; C:synaptic membrane; IDA:AgBase.
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   1: Evidence at protein level;
KW   Calmodulin-binding; Cell membrane; Cell projection; Developmental protein;
KW   Differentiation; Growth regulation; Lipoprotein; Membrane; Neurogenesis;
KW   Palmitate; Phosphoprotein; Reference proteome; Synapse.
FT   CHAIN           1..246
FT                   /note="Neuromodulin"
FT                   /id="PRO_0000159600"
FT   DOMAIN          32..61
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   246 AA;  25631 MW;  6F9330F121126F01 CRC64;
     MLCCMRRTKQ VEKNEDGDQK IEQDGIKPED KAHKAATKIQ ASFRGHITRK KLKGEKKADA
     PASESEAADK KDEGPAGGAA ENKESEASAA TEASAADSAQ LDEGSKDSSV PAEEKKGNGA
     ADTGSEQPAP QAATPAASSE EKPAAAAETE SATKASTDNS PSLKADEAQD KEEPKQADVP
     AADTTATTTP AAEDATAKAT AQPQMETVES SQTEEKTDAV EETKPTESAQ QEEVKEEESK
     ADQENA
 
 
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