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FLP11_CAEEL
ID   FLP11_CAEEL             Reviewed;         110 AA.
AC   Q21156; O61467; Q7Z140;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=FMRFamide-like neuropeptides 11;
DE   Contains:
DE     RecName: Full=AMRNALVRF-amide;
DE   Contains:
DE     RecName: Full=ASGGMRNALVRF-amide;
DE   Contains:
DE     RecName: Full=SPLDEEDFAPESPLQ-amide;
DE   Contains:
DE     RecName: Full=NGAPQPFVRF-amide;
DE   Flags: Precursor;
GN   Name=flp-11 {ECO:0000312|WormBase:K02G10.4a};
GN   ORFNames=K02G10.4 {ECO:0000312|WormBase:K02G10.4a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC08948.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), ALTERNATIVE SPLICING, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC08948.1};
RX   PubMed=9685599; DOI=10.1016/s0169-328x(98)00106-5;
RA   Nelson L.S., Kim K., Memmott J.E., Li C.;
RT   "FMRFamide-related gene family in the nematode, Caenorhabditis elegans.";
RL   Brain Res. Mol. Brain Res. 58:103-111(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 43-54; 58-72 AND 76-85, AND AMIDATION AT PHE-54; GLN-72
RP   AND PHE-85.
RC   STRAIN=Bristol N2 {ECO:0000269|PubMed:16061202};
RX   PubMed=16061202; DOI=10.1016/j.bbrc.2005.07.044;
RA   Husson S.J., Clynen E., Baggerman G., De Loof A., Schoofs L.;
RT   "Discovering neuropeptides in Caenorhabditis elegans by two dimensional
RT   liquid chromatography and mass spectrometry.";
RL   Biochem. Biophys. Res. Commun. 335:76-86(2005).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15236235; DOI=10.1002/cne.20189;
RA   Kim K., Li C.;
RT   "Expression and regulation of an FMRFamide-related neuropeptide gene family
RT   in Caenorhabditis elegans.";
RL   J. Comp. Neurol. 475:540-550(2004).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=16187307; DOI=10.1002/neu.20201;
RA   Papaioannou S., Marsden D., Franks C.J., Walker R.J., Holden-Dye L.;
RT   "Role of a FMRFamide-like family of neuropeptides in the pharyngeal nervous
RT   system of Caenorhabditis elegans.";
RL   J. Neurobiol. 65:304-319(2005).
RN   [6]
RP   FUNCTION (AMRNALVRF-AMIDE; ASGGMRNALVRF-AMIDE AND NGAPQPFVRF-AMIDE).
RX   PubMed=16377032; DOI=10.1016/j.peptides.2005.11.017;
RA   Mertens I., Clinckspoor I., Janssen T., Nachman R., Schoofs L.;
RT   "FMRFamide related peptide ligands activate the Caenorhabditis elegans
RT   orphan GPCR Y59H11AL.1.";
RL   Peptides 27:1291-1296(2006).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=28065609; DOI=10.1016/j.cub.2016.11.045;
RA   Serrano-Saiz E., Oren-Suissa M., Bayer E.A., Hobert O.;
RT   "Sexually Dimorphic Differentiation of a C. elegans Hub Neuron Is Cell
RT   Autonomously Controlled by a Conserved Transcription Factor.";
RL   Curr. Biol. 27:199-209(2017).
CC   -!- FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides.
CC       {ECO:0000305}.
CC   -!- FUNCTION: [AMRNALVRF-amide]: Potent inhibitor of the activity of the
CC       dissected pharyngeal myogenic muscle system (PubMed:16187307). Acts as
CC       a ligand for the npr-22 receptor in vitro (PubMed:16377032).
CC       {ECO:0000269|PubMed:16187307, ECO:0000269|PubMed:16377032}.
CC   -!- FUNCTION: [ASGGMRNALVRF-amide]: Acts as a ligand for the npr-22
CC       receptor in vitro. {ECO:0000269|PubMed:16377032}.
CC   -!- FUNCTION: [NGAPQPFVRF-amide]: Acts as a ligand for the npr-22 receptor
CC       in vitro. {ECO:0000269|PubMed:16377032}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000312|WormBase:K02G10.4a};
CC         IsoId=Q21156-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:K02G10.4b};
CC         IsoId=Q21156-2; Sequence=VSP_052619;
CC       Name=c {ECO:0000312|WormBase:K02G10.4c};
CC         IsoId=Q21156-3; Sequence=VSP_052620, VSP_052621;
CC   -!- TISSUE SPECIFICITY: Each flp gene is expressed in a distinct set of
CC       neurons (PubMed:15236235). Flp-11 is expressed in the DD, VD and DVB
CC       motor neurons, the PVC and URX interneurons, and the AUA, BAG, DA, LUA,
CC       and SAB neurons (PubMed:15236235). Also expressed in head muscle,
CC       socket or sheath cells and uterine cells (PubMed:15236235). Expressed
CC       exclusively in PHC sensory neurons in males (PubMed:15236235,
CC       PubMed:28065609). {ECO:0000269|PubMed:15236235,
CC       ECO:0000269|PubMed:28065609}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from the comma stage of embryogenesis,
CC       during all larval stages, and in adults (PubMed:9685599). In males,
CC       highly expressed in PHC sensory neurons during the L4 larval stage
CC       (PubMed:28065609). {ECO:0000269|PubMed:28065609,
CC       ECO:0000269|PubMed:9685599}.
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC       {ECO:0000255}.
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DR   EMBL; AF042397; AAC08948.1; -; mRNA.
DR   EMBL; AF042398; AAC08949.1; -; mRNA.
DR   EMBL; BX284606; CCD68560.1; -; Genomic_DNA.
DR   EMBL; BX284606; CCD68561.1; -; Genomic_DNA.
DR   EMBL; BX284606; CCD68562.1; -; Genomic_DNA.
DR   PIR; T16537; T16537.
DR   RefSeq; NP_001024752.1; NM_001029581.5. [Q21156-1]
DR   RefSeq; NP_001024753.1; NM_001029582.1. [Q21156-2]
DR   RefSeq; NP_001024754.1; NM_001029583.2. [Q21156-3]
DR   AlphaFoldDB; Q21156; -.
DR   BioGRID; 45676; 3.
DR   DIP; DIP-25649N; -.
DR   STRING; 6239.K02G10.4a; -.
DR   EPD; Q21156; -.
DR   PaxDb; Q21156; -.
DR   EnsemblMetazoa; K02G10.4a.1; K02G10.4a.1; WBGene00001454. [Q21156-1]
DR   EnsemblMetazoa; K02G10.4b.1; K02G10.4b.1; WBGene00001454. [Q21156-2]
DR   EnsemblMetazoa; K02G10.4c.1; K02G10.4c.1; WBGene00001454. [Q21156-3]
DR   GeneID; 180741; -.
DR   KEGG; cel:CELE_K02G10.4; -.
DR   UCSC; K02G10.4c; c. elegans. [Q21156-1]
DR   CTD; 180741; -.
DR   WormBase; K02G10.4a; CE04704; WBGene00001454; flp-11. [Q21156-1]
DR   WormBase; K02G10.4b; CE31030; WBGene00001454; flp-11. [Q21156-2]
DR   WormBase; K02G10.4c; CE34328; WBGene00001454; flp-11. [Q21156-3]
DR   eggNOG; ENOG502SXW2; Eukaryota.
DR   HOGENOM; CLU_173525_0_0_1; -.
DR   InParanoid; Q21156; -.
DR   OMA; LDHMHDI; -.
DR   OrthoDB; 1549263at2759; -.
DR   PRO; PR:Q21156; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001454; Expressed in larva and 3 other tissues.
DR   GO; GO:0005576; C:extracellular region; IC:WormBase.
DR   GO; GO:0071855; F:neuropeptide receptor binding; IDA:WormBase.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IDA:WormBase.
DR   GO; GO:0030431; P:sleep; IMP:WormBase.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Neuropeptide; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..29
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000312064"
FT   PEPTIDE         32..40
FT                   /note="AMRNALVRF-amide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000312065"
FT   PEPTIDE         43..54
FT                   /note="ASGGMRNALVRF-amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT                   /id="PRO_0000312066"
FT   PEPTIDE         58..72
FT                   /note="SPLDEEDFAPESPLQ-amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT                   /id="PRO_0000312067"
FT   PEPTIDE         76..85
FT                   /note="NGAPQPFVRF-amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT                   /id="PRO_0000312068"
FT   PROPEP          88..110
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000312069"
FT   REGION          60..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         40
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         54
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT   MOD_RES         72
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT   MOD_RES         85
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:16061202"
FT   VAR_SEQ         83..110
FT                   /note="VRFGRSGQLDHMHDLLSTLQKLKFANNK -> EAQVRQQQVMTEDDRLLLEQ
FT                   LLRRIHH (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052619"
FT   VAR_SEQ         83..86
FT                   /note="VRFG -> GKLS (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052620"
FT   VAR_SEQ         87..110
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_052621"
SQ   SEQUENCE   110 AA;  12213 MW;  7C3B42E42F8DDEA7 CRC64;
     MTQFSALALL LIVFVAASFA QSYDDVSAEK RAMRNALVRF GRASGGMRNA LVRFGKRSPL
     DEEDFAPESP LQGKRNGAPQ PFVRFGRSGQ LDHMHDLLST LQKLKFANNK
 
 
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