ID W8AJ92_CERCA Unreviewed; 2645 AA.
AC W8AJ92;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Basement membrane-specific heparan sulfate proteoglycan core protein {ECO:0000313|EMBL:JAB85807.1};
DE Flags: Fragment;
GN Name=PGBM {ECO:0000313|EMBL:JAB85807.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB85807.1};
RN [1] {ECO:0000313|EMBL:JAB85807.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB85807.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; GAMC01020748; JAB85807.1; -; mRNA.
DR GO; GO:0005886; C:plasma membrane; 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; cd00055; EGF_Lam; 4.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR000742; EGF-like_dom.
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; 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; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 4.
DR Pfam; PF00052; Laminin_B; 3.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00180; EGF_Lam; 8.
DR SMART; SM00409; IG; 11.
DR SMART; SM00408; IGc2; 11.
DR SMART; SM00281; LamB; 3.
DR SMART; SM00192; LDLa; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 11.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS50835; IG_LIKE; 11.
DR PROSITE; PS51115; LAMININ_IVA; 3.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT DOMAIN 421..501
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 645..734
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 794..968
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1157..1331
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1366..1415
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1428..1475
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1499..1674
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1756..1848
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1860..1942
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1954..2042
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2060..2142
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2149..2234
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2239..2327
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2345..2414
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2435..2521
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2530..2614
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2624..2645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 202..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 272..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 295..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 302..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 332..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 339..357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 351..366
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 384..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 396..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 525..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 532..550
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 544..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 565..577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 572..590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 584..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 608..620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 615..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 627..642
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1385..1394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1446..1455
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB85807.1"
SQ SEQUENCE 2645 AA; 294520 MW; 721CB23542635DE2 CRC64;
EEERRAEEER RAEEERRAEE ERRAEEERRL EEERRAQEEE EAGYAGGEDE SVDPVTQEPN
ENEIVDEYDE EEERRRTEEA ERAEQDRLRA EQDRLRAEYI EQERRRAQEI ERARAEYEKR
QREEASERDE IPELPIMPDE SEATEEPERA YNGLDLDEGS GADTNFGIST DRSTLFTDAG
CRGDASYTCS RSGYQICDEQ RCDGREDCPD GEDEVDCEYE NGAGGDANGG AVDGNEEEII
DEDLAGKGER DEVCSDSEFK CDGNCIARYY VCNGIVECED GTDEANCPSS ETEECRPDQY
RCRSGNCIDS ARRCDRTPDC PDGDDEDASC RCAANQFRCR NGDCVSRNAQ CNGYPDCRDG
SDEDDCSEAP LPFVPSCSAA QFRCNNGQCI NAAARCNGYT DCADSSDELS CTATDVSPAN
PQLNLKTYPD SQIIKESREV IFRCRDEGPQ RARVKWTRPG GRPLPIGSRD NGDGRLEIPN
IRVEDSGQYI CEAVGYPRHV SGQQVLVHLT VEKSNPNYDR PPTACRANQA TCRNNDCIDK
ALICDGTPHC SDGSDEESCS HGLKCQPNQF MCRNSRCIDR IWRCDGEDDC FDNSDEDSCD
PEPSGAPCRY DEFQCRSGHC IPKNFQCDDT NDCLDGSDEI GCVAPAPIRP PPPYVRLQQG
DALNISCVGV GVPVPLIVWR LNWGHVPEKC VSRNYAGSAT LYCPGMDSVD QGAYSCEIIN
SKGRIFVTPD THVSVESSRP DLDVCPAGFF NMLARHPDEC INCFCFGISK TCKSANLFNF
ALQPPITSHK VKNVELNPYG DVIINEAPQP NILSRLHGVQ FRVSDVGYNS REQPYLALPI
DYMGNQLKSY GGYLRYEVNY MGNGRLNKVP DVIITGNGYT LTHRVRNQPE PNVNNKISVQ
FHAGNWYKTD GRRATRQEIM MVLANVDNIL IRLSYIDATE REVELTNIFM DSAGLTDQGL
GSASLVEKCT CPPGYVGDSC ESCAPGYVRE KYDWLGRCVP FVPEQCTAGT YGDPARGIPC
RPCPCPQTGA GNFASTCQLG PDGDVICNCF EGYTGRRCES CAPGYQGNPL VPGGSCYPIP
ESTCNAEGTY YPHPNGTCEC KTLVVGPRCD TCAPESFHLN SFTYTGCIEC FCSGLTKQCS
SSSWYRDQIS TSFGRSRAPH GFKLIRDYET PEPIVFQQSN SALQFSSTTG SEPLYWSLPA
TFLGNKITAY GGKLAYNLSY NALPGGIMSR NSAPDVVIKG EDVTMVHYRK ASVSPSQPSS
YSVPIIESAW QRSDGQVVNR EHLLMALSDI YAIYIKATYT TGTKDGQLTH VSLDIATQNN
IGTPRAYEVE ECRCPIGYIG LSCERCAPGY KRESEEGLYL GVCIPCECNG HSTQCDAETG
VCVNCDHNTA GDYCDRCAAG YTGNASGGTP YDCTPDYAPP PPSNQSSCSY CNRAGTVSCD
GGYCACKPNV DGAYCDRCRP GTFGLSERNP DGCEECYCSG KSTQCNSALL YRQLIPVDFI
LNAPLITDIK GEVIDNSNQN FDFPTNSYTY NYTSYTEKYW SIRGSVLGNQ LYSYGGHLSY
NLDVETYGDY VPGKDVVLIG NGMELHWSRP DEEQDSNEYR VRLHEDEEWQ RTEYGSTIRA
TRLDFMNVLA NLEHILIRAT TKIPTTRTSI RDVILESAVE HRTPDATQAV EIELCTCPAG
YSGASCEKCE PLHYKDNYGS CVACPCREDT TDSCFLQRNE VVCQCKPGYS GQQCQVNDVY
PPRPEPTRPT PPPALPEYQT QITVSIAPPQ YEIIPIGGSL TLTCTGRMAW NGLPVFVNWF
KLGGRLPNAA EEEDGILRLY NLQIYDSGVY VCRAVNNDTK RVFEDKVSIT ISEDSLRTGP
RIENLPQVVE FEEYQTNEIN CEVSGNPTPT VTWTRVDGRM SMEAHTDGTR LIFDAPRKSD
EGRYRCKATN PLDTVEKYTQ VYVRTSPPVP PPPPRELIYI EPPSYTGESG DSVRLTCQPT
TSIVLVYEWN KDGYPLYRQS NVIVSGNTLE IREATARDSG YYTCIGIDLR NRRNYTNDAQ
VVIEESNYPA PGPLPGTIAP VVKRLPEENR IAQGQDFSIT CEASGSPYPS IKWTKFHAAL
ADNVQQTGNV LRIINARPEN GGMYLCIAEN VAGSHESSTI IDVDPRESPT IDIHPPEPQR
VNVGTEAMLY CSGNGSPEPT VQWRRVDGKP LSSRCEIVRE GYIMIRNIQV EDDGDYECIA
KNDVGRTTAV QEIRVLVPPS ITLEPNEEYL SLTEGDELKL ICSASGVPSP IVQWVDDSTE
FNRELSVGRQ FNQAFLEKYR VDRNDAKIYK CIASNEAGTD ESYVTVDVRP RRGDAPVDSD
VIRYPVADTP PPQNIYRARE GDAVKLTCDL NQALLTRWER VDGDPLPENS YLDRNSLIIS
GVEQKNIGRY RCNAIDNLGN IETFIVAELV LVPIPHITFH PQIPVVLTEN DNIDIFCEVS
GEQPIAVTWH TTNNRPLPDS VRIEGPYLRF FSITPADAGR YLCSASNRYG NTTKTAEVVV
NRRGPYLPTP RAQVHEIREG DDVTLTCNVG DGRETIRGGI RYNWRREDQR PLPPGALIHD
QRLILRGVQK QDEGRYVCDS YTTAGYSSAP SYVDLIVKRE YNSSLPDNYG RERHRRRRYN
TRRGY
//
