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BURS_CULPP
ID   BURS_CULPP              Reviewed;         171 AA.
AC   P85315;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Bursicon;
DE   AltName: Full=Bursicon subunit alpha;
DE   Flags: Precursor;
GN   Name=burs124 {ECO:0000250|UniProtKB:Q66Q82};
GN   and
GN   Name=burs3 {ECO:0000250|UniProtKB:Q66Q82};
OS   Culex pipiens pipiens (Northern house mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=38569;
RN   [1] {ECO:0000305}
RP   CONCEPTUAL TRANSLATION, AND TRANS-SPLICING.
RX   PubMed=17435221; DOI=10.1534/genetics.107.070938;
RA   Robertson H.M., Navik J.A., Walden K.K.O., Honegger H.-W.;
RT   "The bursicon gene in mosquitoes: an unusual example of mRNA trans-
RT   splicing.";
RL   Genetics 176:1351-1353(2007).
CC   -!- FUNCTION: Final heterodimeric neurohormone released at the end of the
CC       molting cycle, involved in the sclerotization (tanning) of the insect
CC       cuticle, melanization and wing spreading.
CC       {ECO:0000250|UniProtKB:Q9VD83}.
CC   -!- SUBUNIT: Heterodimer of burs and pburs. {ECO:0000250|UniProtKB:Q9VD83}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VD83}.
CC   -!- MISCELLANEOUS: The bursicon gene is encoded by two loci: burs124
CC       contains exons 1, 2 and 4, and burs3 contains exon 3. Exon 3 is trans-
CC       spliced into position in the mature transcript. This unusual gene
CC       arrangement has existed for at least the 150 million years (MY) of
CC       mosquito evolution since the split of the culicid and anophelid family
CC       lineages, but is younger than the 250 MY split of the dipteran
CC       suborders Nematocera and Brachycera (containing the Culicidea and
CC       Drosophilidae, respectively). {ECO:0000269|PubMed:17435221}.
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DR   AlphaFoldDB; P85315; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005179; F:hormone activity; ISS:UniProtKB.
DR   GO; GO:0007593; P:chitin-based cuticle sclerotization; ISS:UniProtKB.
DR   GO; GO:0048067; P:cuticle pigmentation; ISS:UniProtKB.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR004133; DAN.
DR   Pfam; PF03045; DAN; 1.
DR   SMART; SM00041; CT; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hormone; Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..171
FT                   /note="Bursicon"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000312828"
FT   DOMAIN          47..137
FT                   /note="CTCK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        47..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        61..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        71..131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        75..133
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        93..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT   DISULFID        95
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
SQ   SEQUENCE   171 AA;  18431 MW;  A164C873F5D2B197 CRC64;
     MISSPSTPAT FAAGSLVLLC LVLGGGHFAL AQKEGNDDIQ HYTADDCQVT PVIHVLQYPG
     CVPKPIPSFA CVGRCASYIQ VSGSKIWQME RSCMCCQESG EREASVSLFC PKAKNGEKKF
     KKVSTKAPLE CMCRPCTGIE DANVIPQELA AFADDGTLTS YFQKGQLRNS E
 
 
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