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Database: UniProt
Entry: E2ALX5_CAMFO
LinkDB: E2ALX5_CAMFO
Original site: E2ALX5_CAMFO 
ID   E2ALX5_CAMFO            Unreviewed;      1019 AA.
AC   E2ALX5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Very low-density lipoprotein receptor {ECO:0000313|EMBL:EFN65567.1};
GN   ORFNames=EAG_00992 {ECO:0000313|EMBL:EFN65567.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN65567.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; GL440682; EFN65567.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2ALX5; -.
DR   STRING; 104421.E2ALX5; -.
DR   InParanoid; E2ALX5; -.
DR   OMA; DEYACKN; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 9.
DR   Gene3D; 4.10.1220.10; EGF-type module; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 9.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 9.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 9.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 5.
DR   PROSITE; PS50068; LDLRA_2; 9.
DR   PROSITE; PS51120; LDLRB; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|EMBL:EFN65567.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EFN65567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        938..962
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          514..528
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS01186"
FT   REPEAT          616..659
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          660..702
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          703..746
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          747..791
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          1000..1019
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        162..174
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        169..187
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        203..215
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        210..228
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        222..237
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        264..279
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        283..295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        290..308
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        302..317
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        330..348
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        342..357
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        369..381
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        430..445
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        460..478
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1019 AA;  113485 MW;  1B78219CCADD5060 CRC64;
     MLHTGWWWCA LTQWWNEGRK DTTVRRKRVV MGQDSRGVLL LVALAALAAA DAFSIDSKVA
     CPLRQFRCAN GRCIPISWVC DKSDDCTDNS DESPEECKYT NCCLIISNSI EINQLICVTE
     TVPAKSRDIG RNSVSSQLAC ATIIPIGAVA HSSMNISDAQ ECKDSDFKCT NGRCIPNIWH
     CDGDRDCPDG VDEDPAVCRA IPCSETEFQC SPGECIPKTW LCDHQADCTD GLDEKNCHRS
     KSCTPEQFTC HSGNGECVAL TWMCDDNPDC SDGSDEAECN DTCRSDEFTC ANKHCIQQLW
     VCDNDNDCGD NSDEKACEPT ACHPNTDFAC SEHYCITSRW RCDGDYDCPD RSDEIGCKEP
     PNKERISHCD KEFDCDDGVT CIHQTWVCDG EKDCPNGADE SSQRCHNVTC RPDQFQCEDR
     RSCISGYLYC NGKAECADES DEKNCTSKGI SCDRRIQFEC SEGSCISLEY VCNQKPDCIG
     WEDESADLCG VNECAKNNGG CSQICVDMPI GYRCDCHAGY RLIDNRTCDD IDECLEPGSC
     SQFCQNEKGS FKCSCAAGYL KDPRNSTRCK AAEGHASLLF ARRHDIRKVA LDRQEMTAIV
     NNTKMATALD FVFRTGMIFW SDISEKKIYK APIDEGNERT VVIEKDLTTS DGLAVDWIYS
     HIYWTDSGKD TIELANFEGN MRKTLIQDHI QEPRAIALNP LEGWMFWTDW SDEARIERAG
     MDGTHRSVIV GNDVKWPNGL TLDLIGKRVY WVDAKLNIIG SCNYDGTGRR TVLYSPSNLR
     HPFSITTFED YVYWTDWDKE TIFKANKFTG KEVEAVTSIK TLQHPMVVHV YHPYRQPDGM
     NQCQAVNGHC SHLCLPAPKI NSRSPLLSCA CPDGLRLLPD GLMCVENVTT TVAPSTEAAM
     LPFQRLKPLN VTTTLNPLSA ADADGKRNLA TESTDPGLVA GIVIGVVSLG LLLLALVAVL
     CYRHYLHRNV TSMNFDNPVY RKTTEDQFSL EKNRFPLPAA TVGEEAQEPL TSPGTNDYV
//
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