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Database: UniProt
Entry: A0A0N1III6_PAPMA
LinkDB: A0A0N1III6_PAPMA
Original site: A0A0N1III6_PAPMA 
ID   A0A0N1III6_PAPMA        Unreviewed;       904 AA.
AC   A0A0N1III6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Atrial natriuretic peptide-converting enzyme {ECO:0000313|EMBL:KPJ16423.1};
GN   ORFNames=RR48_05502 {ECO:0000313|EMBL:KPJ16423.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ16423.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ16423.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ16423.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ16423.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
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; KQ460226; KPJ16423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1III6; -.
DR   STRING; 76193.A0A0N1III6; -.
DR   InParanoid; A0A0N1III6; -.
DR   Proteomes; UP000053240; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd07066; CRD_FZ; 1.
DR   CDD; cd00112; LDLa; 2.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF67; PROLOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 1-LIKE PROTEIN; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        213..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          520..650
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   REGION          17..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..847
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..816
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        568..606
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        635..647
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        642..660
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        654..669
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        672..684
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        679..697
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   904 AA;  100832 MW;  17745F08E050F677 CRC64;
     MVNGNYVLYG DRPSSESEIV EDHVHTRAAE KKTKRKPNRT ANELQYSLNL AQLDNETDSV
     KYEKKVKEPR LLRYVPTTDV EEHFVSEKFE TYDLKATDEP PRRYAFTKKP KNPADGSINY
     AYSRSSSSCS SPNGNLPTIS EHGEQFSTYR IRSIRTPTDE EVSHAYETKL DKYFSRPREV
     KTFVAKGSHP DSLYRVPVGS GVASSKVVRV LRILRWPVAL FSVCIALAIF VYFLMPDNLS
     SEYSTVNATS WQEDTASAQS RIQPGKPNRK PPEQGQHGPQ KGNIRTKPQE IDFYDAENVK
     TIDLKSLMET VTENSEKRTP VPPVFPTHIA PEVQYGNERA DKEKMRSPKL IDTVMNSDES
     TLKPHITQSP ERPLAIYFDE GKVATSTETI TRAESNNDIL HYDEKELPKT TEETTSKPYS
     PVYKDTSLYI RKEHSKSKQR PTEPDLTQAL HEYYRLTPIN HDNRFTSGHS KLFGISMEDA
     QSMKSTTQST LYNTRVSPTL PTWRDNADST TKKYPLNTNL DVSQCRSTHL GLCRGVLPYD
     LAGPAATLDG VDVTDLLPQM EYLVSSNCSE RTAHFLCSLL EPECSPTPYL HKMPCYSLCR
     AVAEHCDGSI PRDLLGVFGC TRYPTGGCAA ARAPCGAREL PCGDGSCVPS HWACDGAADC
     PAAEDEAHCT ACASNEFRCP SGGCVHTRWL CDGYADCPRG EDEAEQQCAA RREHDDEQVA
     DADPEPGEEP AGSAPALAVR RPFQTSKGYA DDSVHRNGET ESSKEILMTS DSKNGLKRNF
     TRRPSPARLS PYSRPIIHDT KTQSKGKLDP RVKTKTNQRK ASRTTLRTTT TSQHMAETAQ
     PPRYQPLQQP GACARLALPQ RRTALRRRQG AWFIAKWAGC HRPVLVAGRK RSESFGDGDA
     AAPG
//
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