ID A0A194R369_PAPMA Unreviewed; 3724 AA.
AC A0A194R369;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein {ECO:0000313|EMBL:KPJ10291.1};
GN ORFNames=RR48_08951 {ECO:0000313|EMBL:KPJ10291.1};
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:KPJ10291.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ10291.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ10291.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ10291.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KQ460953; KPJ10291.1; -; Genomic_DNA.
DR STRING; 76193.A0A194R369; -.
DR InParanoid; A0A194R369; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00055; EGF_Lam; 4.
DR CDD; cd00110; LamG; 3.
DR CDD; cd00112; LDLa; 12.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 14.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR PANTHER; PTHR12231:SF262; DPR-INTERACTING PROTEIN KAPPA, ISOFORM A; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 9.
DR Pfam; PF00052; Laminin_B; 3.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF00057; Ldl_recept_a; 11.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 7.
DR SMART; SM00409; IG; 13.
DR SMART; SM00408; IGc2; 13.
DR SMART; SM00281; LamB; 3.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 13.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 13.
DR SUPFAM; SSF57424; LDL receptor-like module; 11.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS50835; IG_LIKE; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 3.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 12.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240}.
FT DOMAIN 441..533
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 669..759
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 808..997
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1190..1369
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1457..1505
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1532..1708
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1885..1979
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1988..2070
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2078..2149
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2160..2253
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2267..2353
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2395..2473
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2503..2587
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2592..2676
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2696..2763
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2827..2899
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2930..3008
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 3011..3188
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3186..3222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3224..3259
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3266..3441
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3452..3485
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3494..3533
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3539..3718
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1870..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1871..1889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 24..36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 31..49
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 43..58
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 60..72
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 67..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 79..94
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 151..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 177..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 189..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 214..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 221..239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 233..248
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 262..274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 269..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 281..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 301..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 308..326
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 320..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 405..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 412..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 550..562
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 557..575
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 569..584
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 590..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 597..615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 609..624
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 652..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1476..1485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2791..2806
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 3193..3210
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3212..3221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3228..3238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3249..3258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3475..3484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3523..3532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3724 AA; 408535 MW; 5B8A8C75C6423CE2 CRC64;
MRCNRKYDCD PGDYSDEQNC RTICMAYEYK CSSGQCVKAD SWCNGTKECN DGSDERNCPC
RRDEIECRDG TCINIALRCN GRKDCPNGED EYNCGEPRCP ADSFACTVDS RMGCARRCDG
RQECDNGEDE LECTECSHEC DGRCLEDHLI CNGVPDCSDS SDELSCPTCD SLDDFRCANG
ECINIAHRCN GLNDCSDFSD EKNCNNTLPS TDDCNDNQFR CQDGTCIDIQ FSCDGNYDCF
DNSDEDNCPW VVEPPTLPPP PCHESEFTCY DGRCIPHILR CDNIYDCSDF SDEQKCYHSA
CKENEWQCTT GQCVPFQARC DGSVDCTDTS DEQDCVTTTW IPPIQPQSTT RSPIITIPPI
IYAPTTGNPN RDPYEPSTRL PNLYPSTFRP EEFPGGGGSS GSDGCASNQW RCENGPCIDS
RRRCDGRVDC PRDSSDELDC PSDRQDYTAL NLKTYPKTQT VRNGGDVVFQ CRDEGPLRAP
VRWIKEGGRP FKPGTVDRRG RLEMTKVSVS DSGVYICQAP AYAGYPGSEA RVTLMVESAS
QVPKLPFTPC NFSEATCGNG QCIPKYAVCD GKPDCDDRSD EDSCNLNGQC EPNQFVCDNK
KCVLKTWLCD SEDDCGDGSD ERDCRAEPGQ ACSAVEFACA SNQQCIPKSY HCDGHFDCQD
NTDEIGCAPV HVKRPPAPAN VRLNPGESLV LVCEAVGVPM PLISWRLNWG HVPPKCTSTS
IDGVGTLTCN NMQPEDSGAY SCEAINRSGT TFAAPDSIVY VNKTDVCPTG FFNSEARSQN
ECIRCFCFGE SNVCRSADLF TYNMPTPLGE GGTRLIGVTQ TYTGEVQIAS QPITEQFYYQ
SMRNGATVTK LDLASWYKSP DVQPFLTLPE TYNGNQLTSY GGHIRYNLSP HSTRYSTDST
PDIIIKGKYQ SLIYKYGGEI SRGSYIEARL TPGNWMKPTS RGPERASRED IMMALDNVEM
ILLRAGINNA GVNITDFAME SAQHINVGLG AASLVEECTC PPGYEGLSCQ KCAANYVRVK
NGPWLGDCVP KRTCPEGTYG DPNSGYECKP CPCPLTNTGN RFATSCSIGS NGDVTCDCFP
GYEGPHCEHC AAGYIGNPLV PGDSCKPKPT DNCHPEGTSV VRPPDECICK DNVEGRFCDQ
CKNGSFYLSQ DFRQGCALCF CSAVSQQCTS STNLRRRAIT VSFNVPNVVN QVKVYSSVPS
SSAGAIRYNA PVETKLQPTL LRGEVNLPSV DRSRPAIYYW SLPSSYAGDK VTSYGGYLNY
TINNVSPYGT RNNAADIQLI SDVTFHYFGN FEPNSDGTLT ASVQLLEKGW QRPDGKEVSR
EYFLLALSHL KTILIKATYN TNDVSPISTA SLEIAESNGN GPLALHVEQC VCPDGYIGTS
CENCAPGYTR SMERGFYLKL CEPCECNGHS TMCHPETREC YDCADNTDGP SCENCKPGYV
KDAYGNCVYE SSTSPSCYCD PRGAEGPCDN SGYCRCKQNV EGQSCDRCRP GTFGLDSDNP
LGCHSCYCSG ATTECHEATH YSRIQLAAPV FGDKVGYTLM DLQGSVVIND QFVSVPIESE
LRYVFTRPPN QDLYWSLPVF PGNRVLSYGG TLMLTQSFET GGIPDQGNAV VILVGNARSI
SWTSPNPIPS GTAVSYQVPM QESGWYLLNT PTPASREDFM YILQDLKRVL VKATLSPNVA
SSAIADVSLD TASEIYSTGS RPAKGVEICM CPKGYSGTSC ETCRSGYYKE PTGLCKQCNC
NGHDCQLGAY REVVCNCRPP YTGPNCSTVG LIMELHPKIR DSSDLNPFMR RVTFTCKYRA
PEPLTIKFYF KGREMLPVKY YNESELFDDG WRGEHSWQTV WDTRRQGEIY ECHTVTEKGF
TLGVLTTSLP EKGGENKNDT SLPPPSQSTV SIKIANPQIR IQEVGSSVRF ICEAQSLYTH
NALRVNWTKV DGYLPLERTY VDARTGELLI TNLQVTDSGQ YICQTSDGIS TGQAKATLKV
PGNPMTLPIV AIRPSSTDYY EGDRIELECQ VSGNPAPSIT WQRAANKPVY RASQYDTFFI
IDNALEEDSG EYRCIASNSM GSSDKSVVIT VRARPSRPVR EKLTVSASAA NLTEGQSTRI
VCTGTANVPA GTIEWIRQDG AQLLENVRSD NGVLYIDRAT TENQGIYVCH SISTEIGPVP
IVVTIIPLNP PSPGEASNIT VSEKSLRLHA GASGSVECNP TGNPLPLIKW TKYQDKFGAG
VSQRYNSLLV SNAQPSDEGY YVCEGSVNDE TIGIIYVYVA VEKREAPRVS VWPQGEQAVA
LGSPFMLMCR LLAGDPEPVV TWERAGGRSL APHAHLEPNH VLNFEKVDVN DEGEYICTAT
NDAGSDRSST VIKVRYIYTI FEKVDVNDEG EYICTATNDA GSDRSSTVIK VRSPPEIFIT
PSDYVEAVRG DSVTIECRAR GYPEPMVSIK TSPEMREVVP PSRGMAVLRI PSVSERDDGM
YVCTASSAAA TIDQQIIIRV DRGDGGLGDF EGSGEVDINV DQPSIYENRP SNSIAIEGRD
ARLSCNGSSD FDVAWRKDNG RLKYDVEARG TELIIKNAKK SDSGVYECLL RSRQTGELQQ
VTAIRLSVMA APRISLRPAT QTVQPGQSPT VECVVTGDDI RDIAWIPVNR QPSSRIEIRG
STLIFRQIEV EDAGQYECFA QNPIANASAV AEVIVSEESE GRATESHDNE QTAYVGAAVQ
LSCNVTRPSQ RIRWSKDGMA LPRSARQNDD GSLFIRLAQK SDSGRYICII YDQYGRKTSN
YINLHIEGVE CLRSQFRCHD DSGCIEKMLL CDGFSDCQDS SDEENCLSSD DSNPVILSDS
DMNSAGPRNN AELVSIEQPK RQYIVGENVE VMCKAISRDI RVYWERYGTN QYVVSRTYGD
GALLILQGVQ EADAGLYRCI GSDPYGVTSY DDFNLDVVPV ANNQLIPAEP QPQAYTARLW
DSVRLPCNHN LEQPVNIEWT KEYSHLPTNV RINEPVLDLD SVSETDAGTY ICRVSNNRAA
VEARAILRVT GIVPRFNGDS WLALPMIKDA YMQFDIEISF KPSDNNGLVL YNGQNLDRSG
DYLALQLIDG VPTFVFETGS GPVSVSGDRP LLLNTWHTIR ISRTNSKVSM DVDNKGPFTS
ESSQQWDVLD LKQPLYIGGV PDPNQLPADL AGASGFIGCV SMLILGREEI NMMADTTSQN
NLQECDSCLP NVCLHGGVCQ EARNERGYVC LCPAGYAGLR CDRTGEACRP GLCGPGRCTD
TADGYKCACP VTFTGKNCEQ KQNIEYPAFT GSAFLAIRLP RTSRRYFRMS MKIKATPPVI
DGIIMYCKAR GGGYTALSVH NGKLEFRFDL GDGRPVVLTS NKTLDVNEWT DVHVARVGAD
VSMKINMIDT YEQKLASNKT DVILDSPMYV GGVDESITLD NSTGVIGGFS GCIKEKLVRL
NQGDQLDIVN ASIQSANIQE CPNDVRGDIP EVYSVCSLCR NGGRCTSLDA TACTCPPGFS
GTYCENRSSY RTPYTDPCAA RPCRNGGICK LDRSSKMNYT CDCTLGFAGA NCQMPLELLE
SVGFNGNGYL ELPGSMLSYE NLDMDPAVMA LAINTNYDGV LLYHHEAQAP PNSGDYVLIR
IENGVVVMEW DMGSGLNEVR IENVHVTDGE RHEIIAKLMT ENQAYLSVDG TTKIAQSNGF
ANVMSADSNV YIGGIPDRLN YNRYPGLVGC IEQVELMDMD RGIKLGRTAV AGRNTQRCRE
SVTF
//
