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CBPE_CAEEL
ID   CBPE_CAEEL              Reviewed;         472 AA.
AC   O17754;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Carboxypeptidase E {ECO:0000303|PubMed:12657671};
DE            Short=CPE {ECO:0000303|PubMed:12657671};
DE            EC=3.4.17.10 {ECO:0000303|PubMed:12657671, ECO:0000303|PubMed:17564681};
DE   AltName: Full=Egg-laying defective protein 21 {ECO:0000303|PubMed:11813735};
DE   Flags: Precursor;
GN   Name=egl-21 {ECO:0000303|PubMed:11813735, ECO:0000312|WormBase:F01D4.4};
GN   ORFNames=F01D4.4 {ECO:0000312|WormBase:F01D4.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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   [2] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=11813735; DOI=10.1093/genetics/104.4.619;
RA   Trent C., Tsuing N., Horvitz H.R.;
RT   "Egg-laying defective mutants of the nematode Caenorhabditis elegans.";
RL   Genetics 104:619-647(1983).
RN   [3] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12657671; DOI=10.1523/jneurosci.23-06-02122.2003;
RA   Jacob T.C., Kaplan J.M.;
RT   "The EGL-21 carboxypeptidase E facilitates acetylcholine release at
RT   Caenorhabditis elegans neuromuscular junctions.";
RL   J. Neurosci. 23:2122-2130(2003).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17564681; DOI=10.1111/j.1471-4159.2007.04474.x;
RA   Husson S.J., Janssen T., Baggerman G., Bogert B., Kahn-Kirby A.H.,
RA   Ashrafi K., Schoofs L.;
RT   "Impaired processing of FLP and NLP peptides in carboxypeptidase E (EGL-
RT   21)-deficient Caenorhabditis elegans as analyzed by mass spectrometry.";
RL   J. Neurochem. 102:246-260(2007).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA   Liu T., Kim K., Li C., Barr M.M.;
RT   "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT   regulate male sexual turning behavior in Caenorhabditis elegans.";
RL   J. Neurosci. 27:7174-7182(2007).
RN   [6] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=22275875; DOI=10.1371/journal.pgen.1002464;
RA   Hao Y., Hu Z., Sieburth D., Kaplan J.M.;
RT   "RIC-7 promotes neuropeptide secretion.";
RL   PLoS Genet. 8:E1002464-E1002464(2012).
RN   [7] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=25101962; DOI=10.1371/journal.pgen.1004529;
RA   Sharabi K., Charar C., Friedman N., Mizrahi I., Zaslaver A., Sznajder J.I.,
RA   Gruenbaum Y.;
RT   "The response to high CO2 levels requires the neuropeptide secretion
RT   component HID-1 to promote pumping inhibition.";
RL   PLoS Genet. 10:E1004529-E1004529(2014).
CC   -!- FUNCTION: During FMRFamide-like peptide (FaRPs or FLP) and
CC       neuropeptide-like protein (NLP) precursor processing, catalyzes the
CC       removal of Arg or Lys residues from the C-terminus following the
CC       initial endoprotease cleavage (PubMed:17564681, PubMed:12657671). By
CC       processing neuropeptides, modulates basal acetylcholine release at the
CC       ventral cord neuromuscular junctions (PubMed:12657671,
CC       PubMed:22275875). Involved in egg-laying, defecation and locomotion
CC       (PubMed:11813735, PubMed:17564681, PubMed:22275875). By processing FLP
CC       neuropeptides, regulates the turning step of male mating behavior
CC       (PubMed:17611271). Involved in reducing pharyngeal pumping in response
CC       to high CO(2) levels (PubMed:25101962). {ECO:0000269|PubMed:11813735,
CC       ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:17564681,
CC       ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:22275875,
CC       ECO:0000269|PubMed:25101962}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of C-terminal arginine or lysine residues from
CC         polypeptides.; EC=3.4.17.10; Evidence={ECO:0000303|PubMed:12657671,
CC         ECO:0000303|PubMed:17564681};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P00730};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon
CC       {ECO:0000269|PubMed:12657671}. Perikaryon
CC       {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle
CC       lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to
CC       axons in the nerve ring. {ECO:0000269|PubMed:12657671}.
CC   -!- TISSUE SPECIFICITY: Expression is restricted to the nervous system.
CC       {ECO:0000269|PubMed:12657671}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
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DR   EMBL; BX284604; CAB02881.1; -; Genomic_DNA.
DR   PIR; T20454; T20454.
DR   RefSeq; NP_501935.1; NM_069534.6.
DR   AlphaFoldDB; O17754; -.
DR   SMR; O17754; -.
DR   DIP; DIP-26452N; -.
DR   IntAct; O17754; 1.
DR   STRING; 6239.F01D4.4.1; -.
DR   MEROPS; M14.033; -.
DR   EPD; O17754; -.
DR   PaxDb; O17754; -.
DR   PeptideAtlas; O17754; -.
DR   EnsemblMetazoa; F01D4.4.1; F01D4.4.1; WBGene00001189.
DR   GeneID; 177940; -.
DR   KEGG; cel:CELE_F01D4.4; -.
DR   UCSC; F01D4.4.1; c. elegans.
DR   CTD; 177940; -.
DR   WormBase; F01D4.4; CE09156; WBGene00001189; egl-21.
DR   eggNOG; KOG2649; Eukaryota.
DR   HOGENOM; CLU_006722_1_3_1; -.
DR   InParanoid; O17754; -.
DR   OMA; KHPVTTW; -.
DR   OrthoDB; 101221at2759; -.
DR   PhylomeDB; O17754; -.
DR   Reactome; R-CEL-977606; Regulation of Complement cascade.
DR   PRO; PR:O17754; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00001189; Expressed in larva and 3 other tissues.
DR   GO; GO:0030424; C:axon; IDA:WormBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0004180; F:carboxypeptidase activity; IMP:WormBase.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0014055; P:acetylcholine secretion, neurotransmission; IMP:WormBase.
DR   GO; GO:0071244; P:cellular response to carbon dioxide; IMP:UniProtKB.
DR   GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR   GO; GO:1903745; P:negative regulation of pharyngeal pumping; IMP:UniProtKB.
DR   GO; GO:0061837; P:neuropeptide processing; IMP:UniProtKB.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:UniProtKB.
DR   GO; GO:2000294; P:positive regulation of defecation; IMP:UniProtKB.
DR   GO; GO:0060456; P:positive regulation of digestive system process; IMP:UniProtKB.
DR   GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IMP:WormBase.
DR   GO; GO:1903998; P:regulation of eating behavior; IMP:UniProtKB.
DR   GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF73; PTHR11532:SF73; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Cell projection; Cytoplasmic vesicle; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..472
FT                   /note="Carboxypeptidase E"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004157411"
FT   ACT_SITE        329
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P14384"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00730"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   472 AA;  52279 MW;  E3B1AFF682075A8B CRC64;
     MLHAMRPVLL VAALLAVTAH AFLGFGSGST HKDDAEWGHY HNQAQLEAKL GEINEKCPEI
     TTLYEIGQSV EGRPLVVIQF STTPGEHIPT KPEVKLIGNM HGNEPIGREL LLRFAETLCN
     GAINNDKEIV QLLNSTSIHI LPSMNPDGFE LALGTEPAQR QWLTGRSNIN GVDLNRDFPD
     LDSIFYELQK IGVPKFDHLL SLFEDNVDRQ PETIAVGQWT LSLPFVLSAN FHEGDLVANY
     PFDAAIDENS QKTAYSASPD DGTFRWLAKS YADNHAHMSK NDHAPCDGTS QDAFARQGGI
     TNGAKWYSVA GGMQDFNYLA TNAMEITLEL SCEKMPEGSQ LPRFWEDNQK SIFEYVWKSH
     SGVKGMVVDA MTGEPIKRAV VWIRNGTETV PVKHPVTTWS EGDFYRVLPA GKYEIIVAAE
     GYDIAAKNVT VENKVRDSAL VVNFALSPAA DEPSENEQEQ IAELVNEIAR RR
 
 
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