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CUE_DROPE
ID   CUE_DROPE               Reviewed;         647 AA.
AC   B4H1F5;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE   Flags: Precursor;
GN   Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GL22490;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1] {ECO:0000312|EMBL:EDW30132.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Has a role in spermatogenesis and oogenesis.
CC       {ECO:0000250|UniProtKB:Q95RU0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cueball family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW30132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH479202; EDW30132.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002024684.1; XM_002024648.1.
DR   AlphaFoldDB; B4H1F5; -.
DR   SMR; B4H1F5; -.
DR   STRING; 7234.FBpp0186597; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:EnsemblMetazoa.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00135; LY; 4.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS51120; LDLRB; 3.
PE   3: Inferred from homology;
KW   Cell membrane; Differentiation; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Oogenesis; Reference proteome; Repeat; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..647
FT                   /note="Protein cueball"
FT                   /id="PRO_0000386574"
FT   TOPO_DOM        23..534
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        556..647
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          119..166
FT                   /note="LDL-receptor class B 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          167..211
FT                   /note="LDL-receptor class B 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          212..257
FT                   /note="LDL-receptor class B 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          365..401
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          436..473
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        376..389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        391..400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        440..450
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        444..461
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        463..472
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   647 AA;  72914 MW;  4607D0D5484CBFE5 CRC64;
     MLWCPSVLVP LIAVAACLPV LAIGTPLEWE FAITLKSKIL FVDEFWRTLA SAAHEFDELS
     ALTFDETEEL IYFNDQQHRN GSIFSLRRDA LMASHIAEQA IQRTGNESVG GLAYDPLNRN
     LFWSDTLQKK IFFASIDSKV TETPKVLVDL SQEGARPDGV AVDVCRRKLY WTNSNITHPT
     VESIDLAGTN RQVIIDTDID MPRGIVVDQL SDRIFWIDDL KGVFFALKSA RLDGSDRQLV
     LHDKHHEPLN LAVTNDAIYW TDKTTKAVWS HPKVPIVKAT TTTSPVKAEE EDATETIPDI
     EPEPVAEVSA LLRVANLSEE ARGIVARTGF YQRLQKDEHC ANIVRKVKER LDLMTKKKQM
     RSLVDEKTAQ LERDHCLNGG TYIADRVLCI CPTGFKGSRC EIRECHNFCV HGTCEISDRA
     YPKCYCQPGF SGERCEISKC SGLCLNGGHC KLEDISEKPS CECPHNFAGE RCEQNSTEIC
     ALFCRLLKHE ADIYVPFGCH DICEELAKDA SDKIAIPQYH HLEVCMTPSP WTSNVIIVLV
     LGIVSCFFLV AVIVHGFRRL YKPKRPRIRK TFVVRKQART NSSGDTPLTN RPLATEQCEI
     TIENCCNMNI CETPCFDPKL VEQTLAKSSN CKEDKKILIH NMDDDLY
 
 
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