GenomeNet

Database: UniProt
Entry: B4HVU2
LinkDB: B4HVU2
Original site: B4HVU2 
ID   CUE_DROSE               Reviewed;         644 AA.
AC   B4HVU2;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   10-APR-2019, entry version 52.
DE   RecName: Full=Protein cueball {ECO:0000250|UniProtKB:Q95RU0};
DE   Flags: Precursor;
GN   Name=cue {ECO:0000250|UniProtKB:Q95RU0}; ORFNames=GM14208;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1] {ECO:0000312|EMBL:EDW50057.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW50057.1};
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
CC       type I membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cueball family. {ECO:0000305}.
DR   EMBL; CH480817; EDW50057.1; -; Genomic_DNA.
DR   RefSeq; XP_002034921.1; XM_002034885.1.
DR   SMR; B4HVU2; -.
DR   PRIDE; B4HVU2; -.
DR   EnsemblMetazoa; FBtr0197193; FBpp0195685; FBgn0169134.
DR   GeneID; 6610335; -.
DR   KEGG; dse:Dsec_GM14208; -.
DR   OMA; ETPCFDP; -.
DR   PhylomeDB; B4HVU2; -.
DR   Proteomes; UP000001292; 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:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; SM00179; EGF_CA; 1.
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; Complete proteome; Differentiation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Oogenesis;
KW   Reference proteome; Repeat; Signal; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    644       Protein cueball. {ECO:0000255}.
FT                                /FTId=PRO_0000386576.
FT   TOPO_DOM     27    531       Extracellular. {ECO:0000255}.
FT   TRANSMEM    532    552       Helical. {ECO:0000255}.
FT   TOPO_DOM    553    644       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      121    166       LDL-receptor class B 1. {ECO:0000255}.
FT   REPEAT      167    211       LDL-receptor class B 2. {ECO:0000255}.
FT   REPEAT      212    257       LDL-receptor class B 3. {ECO:0000255}.
FT   DOMAIN      398    430       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      433    471       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     82     82       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    108    108       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    175    175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    190    190       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    313    313       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    473    473       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    508    508       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    402    411       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    406    421       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    437    447       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    441    459       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    461    470       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   644 AA;  72715 MW;  92C3C29A9B8AA059 CRC64;
     MIRIRFGMDV LLVLLLATCL LTPAHGTPLE WDFAVTLRTK IQFMDSSWQT IATAAHEFDE
     LSALTFDESE ELIYFNDLKH RNGSIFSLKR DLVAANHVAE QTIARTGNES VGGLAYDPLN
     MNLFWSDTEQ RKIFFAPIYG SATPKVLVDL SAEGGRPDGV AVDVCRRKLY WTNSNVTHPT
     VERINLDGSN RTVIINSDID MPRGIVVDQL SDRLFWIDDL KGVFFSVESC KLDGSDRQVV
     LKDKHHEPLN LAVTNDAIYW TDRTTRAVWS HPKVPVIKVT TTSKPEEEDS TDSTDFTDPE
     PMAEDCPLVR VANLSEEARG IVVRTGFYQR LQKDHHCASI VRKVKERVVE QNRKFEIRSM
     LDQKIKVLED ERCMNGGEYR AATDLCICPT GFKGSRCEIR ECHNYCVHGT CQMSELAYPK
     CYCQPGFTGE RCELSVCSGL CLNGGHCRVS KDENEAPSCE CPAKFGGARC EQNSTEICSL
     FCRLLKHEPE MYVPFGCHSI CEELAQDNST YIAVPQYEHL EVCLTPRVWT SSVIIILVVG
     IVSSLLLVAV IVHGIRRLYK PKRPRIRKTF VVRKQARTNS AGDTPLTNRP LATEQCEITI
     ENCCNMNICE TPCFDPKLVE QTLSKSSCKE DKKILIHNME DDLY
//
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