ID A0A0V1HC46_9BILA Unreviewed; 2719 AA.
AC A0A0V1HC46;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Basement membrane proteoglycan {ECO:0000313|EMBL:KRZ07807.1};
GN Name=unc-52 {ECO:0000313|EMBL:KRZ07807.1};
GN ORFNames=T11_926 {ECO:0000313|EMBL:KRZ07807.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ07807.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ07807.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ07807.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ07807.1}.
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DR EMBL; JYDP01000096; KRZ07807.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 6.
DR CDD; cd00110; LamG; 3.
DR CDD; cd00112; LDLa; 2.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 13.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 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:SF253; NEURAL CELL ADHESION MOLECULE; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 7.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00409; IG; 13.
DR SMART; SM00408; IGc2; 13.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 13.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 4.
DR PROSITE; PS50835; IG_LIKE; 13.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..2719
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006879030"
FT DOMAIN 55..138
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 278..369
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 380..427
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 437..625
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 670..719
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 750..920
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 954..1003
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1010..1059
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1109..1183
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1209..1291
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1299..1375
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1387..1469
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1479..1564
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1575..1660
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1667..1753
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1761..1836
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1855..1937
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1959..2027
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2031..2119
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2130..2303
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2299..2337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2338..2375
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2382..2542
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2533..2713
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 157..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 164..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 176..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 197..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 204..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 216..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 260..275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 398..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 671..688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 690..699
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 973..982
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1029..1038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2308..2325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2327..2336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2365..2374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2719 AA; 300356 MW; 405D52FB82771EFE CRC64;
MLPTMRPICR FRTTLIFLSF LYTSLLAYDD HASTNENRQD IYFVGTADND DATDPLEFIE
VAPHQQTVSE GEEVTFECQP RNIRHRVHIE WRRLHGRLPS KAIIRRGRLT IPNVHMEDAG
VYICKVSSIF IPKEAEVHLN VHGRNGGLRE QTGPSRCLEG EATCQNGECV KREYICDGQR
DCRDGSDEFN CPAPQACEPN EYQCANKNCI QKMWICDGDD DCGDGSDEQN CGTRLPGQPC
APYEFQCKSG SQCVPASFQC DGQNDCMDGS DEIGCAAPVC VQLPQRELTV DCGSTIVITC
RAVGVPTPYI NWRLNWGPTC GQPRCVQTSD QGFGKLVIKG AREEDQGAYT CEAINSKGRI
LATPDAIVTV RCQQPSVISR CDAAGTLAQD PVTGSCQCKH YTVGPTCAQC SPGSFYLSPR
NPYGCVQCFC SGVTKSCQSS SWHRTQERLT FTSSTNGVTI SDFMEKQIET APRLDLRPYG
YITYGGPFFD VVYWRLPARM LGNKITAYGG SLKFKLQFEC TGQMYTQPLV VMKGNEITLI
AHAKTELQPG KENEISIDIY ETSFEREDGQ PSTREHLLMT LANLDSLLIR ATHCANQKES
RLGEISLDIA VDRDTQQEVA FEVEQCHCPP GYKGLSCEEC APGYERSGGG LYLGLCEPVE
AVTPVVPYTR CDPGGALSPT PDARTGQCAC KSLTTGPQCN QCKQGSFFLN PRNPEGCVKC
FCSGVTTQCD SSNLYRSQIF LRVGQQPELI EQLGVRTADT VGTFRPSSRP MVDSSRSISF
SGFFEAPYMK ALYLELPHYF LGNKITSYGG HLTISLRYRG SGRDNTEPEG NDIMLTHRVR
MPLTPDQDHT ISVPLTENHW NREDGRMATR EHFMMALAEV SSLMIKLSFK ENMDHIAIRD
IAMTVTTDRD GRERAWEVEQ CSCPREYLGT SCEECAPGYT RSEGGFYLGT CVPCDCHGHA
DRCDPKTGIC FNCRHNTEGD HCERCQKGFE GDATRGTPND CFTRATPPPC ECHNHSPRGC
DPYGRCLRCE HNTEGIHCER CKPGYFGDAR SGTPFDCRPC PCPGARECFL DSDGQVTCRG
CPAGFTGRLC QECAPGYQKD PVDPQRCKPI GELRVVIQPP KRVEVEEGTT AVFRCHAEGE
AGEPVTLKWT RPTHPSLPVN SIERNGILTL YSVTTADSGI YQCSGVVGPH YASDDAELVV
VKRMRGQRPT PTVQPQQQTI QIGQPFQIRC SAPGSPPPTI TWQKEGDALP HDVELFDGIL
VIRNTQKHHA GVYYCVATNP YGTERAPARI IVEEGVSRPQ ALVNPNELRV SSGERAQFQC
YSPADVTYEW RAATGPLREG IEVSGGNLVF RAAQPQDSGY YYCTVRNPYG EDSITARLIV
EDGIQKPRPF VEPSVLTVKV GDPAEFYCTA DATPPPVITW GWSIPAGPLR PGIEQDRGRI
YITNARKTDE GTYFCTASNQ YGTESVPVTL YVEDGARGPS VHIEPTARWE GRAGETFEFR
CVASGTPQPH VSWSRENQMP FDRNVQDHGY GILRIVSFEE SNVGNYVCTA TNLMGTAKAV
ASVQSAGGLS VKIIPSLPRI EILEGQPLTL ECIAEGTPKP KIEWIYDIGP SRGDVPDGYK
PAKIEGRFIR HEAVSPANEG IYKCRASNEF QVKEAEIYVN VVSRLKRQVV ITGGSERQAE
FGDDVTLTCI LPNPREKDMI WWTRIDGNLT ERHEEQIAGI LVIVDFQPQD VGIYECQSYD
MNINEKSSSS QIKLYEARAE PSINLLRVDG PEIRVLSIGD TLNLMCQETA GNSVKSELKW
FYLKSGYEEE LPRGSIQDGS LLMRNVNLSD GGTYKCVRFL DGKRDGEYQV IVLVTNTEEE
PFDVYAKQGT EVQLHCPIYV LSGMLMVWSR KGELIPDTAV AEADELIIPD FQKHKSGTYI
CEAEFGSLRA KTYVRLMVSE SDSTIEAHIN VQPPEVKIGQ NVSFQCTVKG DPDANIRWEK
RGGHLPQSAT TRDNMLTLQN VVHTDSGIYR CIASTRVGIL TTDAVLHIGT PTALKLPKRK
DDKIEYGVIG LQKRIVCPGR PSKSTTGTVL WMKEGAAVPS QFRQEDDVLV IPKFTGGDGG
QYSCTVKTTN GYSVQFNITV IAEGCLQLRD LVPRFSSDSY IQLPGLPPSA YRAFDVQMSL
KPTKQNAKED GDEKGDFFAF GLQEGRLVLR FDLGDGVTEL ASTNPLSLNK WHKIFVKREF
NKGLISLLGE QQWQRYSEGI ETGLGLGESV FIGGLPNFDE IVSGVGFKTG FSGVVSSVVI
NDVPMNLGEN LLNSNDIEQA DTCSVNSCLN EAKCVPSDGD FGYKCQCKLN SVGTYCERRF
KCNGDVCENG GFCSSASGSR KSCLCPANKT GDHCEQDYHV HGAAQFGTKE SFIVLPKPEN
MARNFQLGMS IKPVSLHDSV LFYSANDLRG TGDYIGLVIS EKNVELRYDS GLGSFRGHSP
TELVANEWYD IKVERKGSTF MLSVNGVATT LDVFYENGGL SLFTDVFIGG VYPDMYVAAG
YGIKKSFIGC IEDTHAYFNG HSYLEFPRSL LPHMSTEDVE TIEMKFSTSE KEGLLLWHGR
YPKSFGSGSD YMSVSITDGF LEFSYELGGG PLQIVSSIMV ADGKEHRIQL VRKGRHGQMF
LDDMEPEVGM SEGILAILNA EGNVFLGGVP DVSAITNGRF RKNFVGCISD VQFDGHQVKF
LEDSLGGLDV VPCTNRFFQ
//
