ID A0A194PGG9_PAPXU Unreviewed; 2211 AA. AC A0A194PGG9; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 19-JAN-2022, entry version 27. DE RecName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats {ECO:0000256|ARBA:ARBA00014669}; DE AltName: Full=Sortilin-related receptor {ECO:0000256|ARBA:ARBA00013467}; DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats {ECO:0000256|ARBA:ARBA00013956}; GN ORFNames=RR46_13707 {ECO:0000313|EMBL:KPI92486.1}; OS Papilio xuthus (Asian swallowtail butterfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC Papilionidae; Papilioninae; Papilio. OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI92486.1, ECO:0000313|Proteomes:UP000053268}; RN [1] {ECO:0000313|EMBL:KPI92486.1, ECO:0000313|Proteomes:UP000053268} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI92486.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:KPI92486.1}; 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:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Cytoplasmic vesicle, secretory vesicle membrane CC {ECO:0000256|ARBA:ARBA00004212}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004212}. Early endosome membrane CC {ECO:0000256|ARBA:ARBA00004158}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004158}. Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004115}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004530}. Endosome, multivesicular body membrane CC {ECO:0000256|ARBA:ARBA00004545}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004545}. Golgi apparatus membrane CC {ECO:0000256|ARBA:ARBA00004614}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004614}. Golgi apparatus, trans-Golgi network CC membrane {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane CC protein {ECO:0000256|ARBA:ARBA00004393}. Recycling endosome membrane CC {ECO:0000256|ARBA:ARBA00004480}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004480}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1 CC subfamily. {ECO:0000256|ARBA:ARBA00007041}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KQ459604; KPI92486.1; -; Genomic_DNA. DR STRING; 66420.A0A194PGG9; -. DR Proteomes; UP000053268; Unassembled WGS sequence. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR CDD; cd00063; FN3; 3. DR CDD; cd00112; LDLa; 9. DR Gene3D; 2.120.10.30; -; 1. DR Gene3D; 2.60.40.10; -; 3. DR Gene3D; 4.10.400.10; -; 9. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. 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 InterPro; IPR031777; Sortilin_C. DR InterPro; IPR031778; Sortilin_N. DR InterPro; IPR006581; VPS10. DR Pfam; PF00041; fn3; 1. DR Pfam; PF00057; Ldl_recept_a; 9. DR Pfam; PF00058; Ldl_recept_b; 2. DR Pfam; PF15902; Sortilin-Vps10; 2. DR Pfam; PF15901; Sortilin_C; 1. DR PRINTS; PR00261; LDLRECEPTOR. DR SMART; SM00181; EGF; 3. DR SMART; SM00060; FN3; 5. DR SMART; SM00192; LDLa; 9. DR SMART; SM00135; LY; 5. DR SMART; SM00602; VPS10; 1. DR SUPFAM; SSF49265; SSF49265; 2. DR SUPFAM; SSF57424; SSF57424; 9. DR PROSITE; PS50853; FN3; 4. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 9. DR PROSITE; PS51120; LDLRB; 2. PE 3: Inferred from homology; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Endosome {ECO:0000256|ARBA:ARBA00022753}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KPI92486.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000053268}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..2211 FT /note="Low-density lipoprotein receptor relative with 11 FT ligand-binding repeats" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5008263225" FT TRANSMEM 2137..2161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REPEAT 931..976 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT REPEAT 977..1021 FT /note="LDL-receptor class B" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461" FT DOMAIN 1638..1735 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 1740..1827 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 1829..1928 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT DOMAIN 2027..2128 FT /note="Fibronectin type-III" FT /evidence="ECO:0000259|PROSITE:PS50853" FT REGION 2182..2211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2182..2198 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 1126..1138 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1133..1151 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1145..1160 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1162..1174 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1169..1187 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1181..1196 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1201..1213 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1208..1226 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1220..1235 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1291..1303 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1298..1316 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1353..1365 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1360..1378 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1372..1387 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1407..1419 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1414..1432 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1426..1441 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1455..1467 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1462..1480 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1474..1489 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" FT DISULFID 1520..1535 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124" SQ SEQUENCE 2211 AA; 248390 MW; 3620AF0AA8C2A8F1 CRC64; MFTVIRRRIS FVALLYFIPC VVSSHEYETW EKSLYVAQEP FEGSGKLFII NKFDTVGDGS HFERKKREAP TTPAPALEKN ISTWTTHLND SHQQLMVHWV GEGSKVIICL ARDSSPRSNG TLSPSALFIS YNYGQTIVNK TESFRLDDTP NSGYAQLDRF YNHPKHPEFC VFVDSINKRL YYTDDNGQNI HRSELTFHPS ELLFDEDNPK RFVVLDKVGR NRMLYMTFNG GKTFTLIQSY VKTFYWSSGP GFPKMFYLER WEPNRSSTVL SVSDPEDMIN AKVLFADAKE FQIKGDYMFA MRQKDNNTFD LYISHQRGPF YKAEFQTELD RRKFHIADVT DKRIFISVMH TENLTNLYVS EISNNFTQYN FVLSLEQVLC YFPQGNWKDS WLEDVTDDAF TDLYRVEGLK GIYIASKVNS KSLIADIEPE HLVSLITFDH GVTWSPIKPP AEDENGKPLS CIDSNDSEKS CSLHLCQKFS QLYPVTSPPG NVISNAMRLL CIAALAAVKR VGGLRVKHVT WNLQVVGSNP AISASIMSSK SAPGIIMATG VVGRSLKGIP GVYLSRVAGL TWKRILKDFY FFNYGDHGGV LVAVKYFKML SETREILYST NEGIEWNSYQ FNANDLRIYG LMTEPGENTT VFTMFGSANE QHQWIIITID LQKAFPRNCT ADDYKDWSPS PPDTTATCVL GTRDVFQRRL AHTNCYNGID YDGPIRKEVC ECGRRDFECD FGFVLSRNVC VHNKSSKYDP YSIPPSCRPG DYYERTKGYR KIDGDVCTTS GYLPYNPDVI PCPLDEPTEF LLVALRDKIA RIDLSDNTTI FPIKDQQNIV AIEFDMKNNC IYWADIEVDK ISRQCFETGF VQEVVVDTDL ASIEGMALDW ISNVLFFVDG MRKKIEAVRT DLSSEGRMRV TILGPDVLSK PRGIVVHPKA GYLFWTDWDR NNPSVSRSNL DGSHIVRLFE KPIVQWPNGI TIDQMSERIY WVDAMEDYIA SADLNGQYFK KILVNDEKVS HPFAVAVLKD KMYWDDWKAK SIFIADKDNG QNVITINGSF SGLMGLKVFA HFIQHGSNAC SYKNTSCDAL CLGGPGNSFS CLCPDGFVKS HGKCLCPNLV EPYANLTCPK KPGATCASDQ FSCKNDMCIA QSWRCDGNDD CGDGSDEAGC VCAPPRVACD NGSCYLPQWR CDGDIDCSDM TDEKDCGKHN CSENEFQCGN GNCVDKRWVC DGDNDCKDDS DERNCTSQVK RPNTQVNCSV HSFACNDSSG MCIPNSWVCD NETDCPGGED ERDERCRNST CAPYMFRCPS GKCIYKSWVC DGENDCSDVE SSDEKNCTHI GHSKLLPRPT TESPFSFPAN SSCLDWMIQC DNGNCLPYWW RCDGINDCGD NSDEVACGVH FVEPKTINRA DSVRQKCGKT RFTCSPGVCI PLSWVCDSQE DCVDGSDEHS CRAWATATPL PLPSCGALET TCRDGGCVLT AKICDGVPDC VDHSDETHCT MKASKPSGAC PGDQFECDEG TRCVWRGALC DGRQDCYDGS DETNCSSHEH NYHYVSLGVD QSSINSTSFL VSCWLAQQQR VLYSFLPSIA KVSDGIWRNM TWTTDSVYRF TGLEPYTNYN VTFYIRDSKS NKTYPSMKYV NTTTGEGVPS PPLRVSVRQM IGSRVNVIWD PPASPRGRLR RYTLYYAPPL PPAQKVVFVT HHEPVSLTVR GYFKPNTNYS FWVTATNNAY TSNSSEVMYL TFDEVGDVDD LKNISVTRLA NNSVSVKWDK IRSVDGYIVS TQLPLLYSRL QPIRTKENNV TLKNLPPGVK IFIHVMAYKG SMIGEPVTEV IITEGERDEM LNMTAILLKE KRTAVLLSWS PPLADRYNGK ELKYQVIYTD AAHWRIPTDL KEDHEKKIIT TNTSVVIDGL HACETYVFTV SLLGGPVTKY KEIVTRENPK APIKDLDYEY NKEKSELKIK WHINCNALSE AVPYRLEITE LTHNKVSRYA LNATRNSSLE HIIENVPVGG RFNICVAAHV EGASKRCIDV RTGALPAPRG LVAWLAPNGH LVLNWQHVEG PDTPKHKYQV IVSEKEIPDD LVQPSADMRV EEAERSPLLL AVTAPAAARP LYVSVRAVTH DGYYSELSEV NTLTMEDSVE EMGTASAVWW GCGAAVVGVA ALGAALLYSV VRQRRLARSF LRLSAHTPRY DSRRGQATIE HDDDDVPPIQ GFSDDEPLVI A //