ID A0A016TXE0_9BILA Unreviewed; 2555 AA.
AC A0A016TXE0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Basement membrane proteoglycan {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0070.g452 {ECO:0000313|EMBL:EYC07470.1};
GN Synonyms=Acey-unc-52 {ECO:0000313|EMBL:EYC07470.1};
GN ORFNames=Y032_0070g452 {ECO:0000313|EMBL:EYC07470.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC07470.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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:EYC07470.1}.
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; JARK01001406; EYC07470.1; -; Genomic_DNA.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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; cd00112; LDLa; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 16.
DR Gene3D; 2.10.25.10; Laminin; 4.
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; 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; PTHR45080; CONTACTIN 5; 1.
DR PANTHER; PTHR45080:SF32; MYOTILIN; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 8.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00409; IG; 16.
DR SMART; SM00408; IGc2; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 16.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS50835; IG_LIKE; 16.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2555
FT /note="Basement membrane proteoglycan"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001488088"
FT DOMAIN 40..125
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 265..349
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 375..423
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 449..624
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 739..913
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 947..996
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1003..1052
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1120..1214
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1224..1309
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1317..1399
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1409..1498
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1502..1587
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1599..1682
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1699..1780
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1791..1876
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1884..1968
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1971..2064
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2068..2158
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2168..2248
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2336..2399
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2409..2496
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT REGION 1383..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1502..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2498..2555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2498..2538
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 144..156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 151..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 163..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 184..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 191..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 203..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 247..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 394..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 966..975
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1022..1031
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2555 AA; 280689 MW; C8080A15A42C2651 CRC64;
MLGKQFRLLW WLAILATASA AKRKHRQTYQ DIDEEGASDV QITVYPVEAQ VREGRDVVFD
CRARTADNSF YPPTRWTRVG GPLPPHAHDS SGRLTINPVS LSDSGQYVCT ASHNGRTVEA
RATLHVQSYG PQELQSQLPS SGQCMADERA CGNNECVKAD YVCDGEPDCR DRSDEMNCPA
LRQCEPNEFK CHNQRCVQKM WLCDGDDDCG DNSDELNCGA QEAGEMCKKT EFQCRDQRQC
VPSSFHCDGT NDCRDGSDEV GCVQPTVVEP PETNKQVAQG STFQLTCKAV AVPEAYINWR
LNWGPVCEPP RCIQTSEGGY GTLTVNNAQA IDQGAYTCEA INVKGRVLAT PDCIVRIVNI
PAPEPPRPPP QPQVRCDPRG AASQYADQSG ACPCKPLVTG PTCTECRPGS FHLNEKSPQG
CLKCFCFGVT DQCRSSTWYR TEDRLMFAGS SEGVMLSDIE ERDIERDSRF DFSKPGFLTY
PSQIRGPKYW RMPQRFLGDK VTSYGGRMEI QLEYSGSGSM SREPMVVLKG NQIVLVHHVR
NQEQVLAPDR PNTITVETYE TNFVQMNGAP ATREDLMMVL ADLDAFLIRA SHVDQQYSSS
LGHVSWQIAV DRPTPDGLAL EVEQCSCPPG YIGTSCEDCA PGYERSGHGP YLGTCVPVQQ
RQPQCTGPGA VSPYAGHGGR CQCKTYAQGP NCDQCPPNSF YMAATNPQGC IPCFCSGVTQ
QCQSSSFRRQ IVEINYPRGD RDQLILTTSD IRQPYHPPTP AYVSGRAIEF VNFQEANGQT
LYWKLPAKFL GNKVTAYGGT LKYTFRFSGE GRTNQEPDVI IRGNDITLQY THRQPIHAER
ENSIELKFFE DGWQRVDGQQ GTREHLLMAL ADLDDILIKA TYMEECSQSG LISVSMEFAE
PQGRGQVAYE VEQCSCPPGY IGTSCEDCAP GYSRTGGGLY LGLCERCECH GHATQCDKEY
GYCVDCQHNT EGDQCERCKP GFVGDARRGT PHDCQPAATR PPCHCNNHSP RGCDSFGRCL
LCEHNTEGTH CERCKKGFYG DATKGTPYDC TPCPCPGAAD CYLDAQGQVA CRNCPAGLSG
RLCDECAPGY TRSHKIAGRP CEPIGQVGDN ERTYVPPPPP HEALRVRILE PKRQVVSEGA
HVQWICQIVG PMRSYVRLEW TRVGYPSLPA SANFTVYDDT TTLYLKDISE DDVGQYRCMA
TTINSIATDD ATLTVSAYAS GRPPQPVVDP PHLTVNEDEP ASFRCWVPGI PDCQITWHKE
RVGGALPHGV YQTGNALKIP KAQLHDAGNY VCTAVNDYGI GQSPYARLDV VRPTQRPRVD
PVEQTVNEGE PARFRCWVPG NQNVDLKWHR EGHQPLPSSV QEHQGILHIP RAMQHEAGRY
VCTATDPRDN RPQDSDPVTL NVRRPEPEPQ LMRPQVDPPE QTVNEGDPAQ FRCWVPGNPH
AVLRWNKQDG QPLPEGTLER DGFLRINSAK MSDAGAYICS ASDPRGGPPT DAPPARLNVR
PPALAPQVDP PSQTVDEGQP SRIRCWVPGN PRAQLRWSKH GRQPLPGHAQ ERDGVLTIPQ
TRKSDEGHYV CTATDPQTGA TAEAPPAHIG VRQPSRLAPQ VDPIEQSIPE GSPFRIRCWV
PGNPHVHLTW RRALGDINDD SEQNQGILTV NRAELTDAGE YICSAEDPRT GEEAEAPPAT
VHVTQPTKVP DVGDVEHGPE VSPPEQTVPE GDPASIRCWV EGQPQADLSW KRADGAPLPF
GATDEDGVLA ISSTLKSDEG DYVCTYHPPD GGRPKDSTPS RLNVKTPGGP PRPVATPPVL
TVKHGEPARF HCDAHSPTPA QISWGHGDAD TALPDGVTHA VDDIIIDAAD ESHEGEYVCS
ATNEYGTGVA EPVKLVVTDE EQPPTARVEP RVWNGKPGDR HQFKCIVTGI PTPKVQWSGP
NNSPLPHDVT ELDGNVLDFS NGRTELNGDY TCTATNPVGE ASDYGSVNIG PSLTVKTTPA
GPRLILTVGE PLHVKCEAFG EPEPEVEWLH DPGPERGDLP DDYKPVTISE QFIRHPAIGL
GNAGAYTCKG SNSHATATKN IYIEVVEPSR VATVSILGGS SQWFQQGEPS QLICTATGSS
LVDRLEWVKV DDQLPTDVEE HNEPGLLHFP NFKNSYAGEY ECRGYRNNEL IASSSVMVYS
TTDDTEDAKV EIEPPRVRVV SQGESIVLKC SVEDPKTRVL WFHTVNHTDA QMVGSERFLH
LPYVDVCDRG IYYCTDEHTN YDYAHSVNTL VVLQDSEFGA KNGENYEWAL LRGGNIVRKL
GTEATLHIKS ADPTNDFGVY RCNVEDDNGV VIGSAYTAVS VGYSGSDHAQ VVKFDEKSDA
SFTCPIYSVP GSKVEWSRVD GELPANAVPN GNKLEIKDFD DTAAGTYKCQ VTFNDNVVEG
FVDAQIFVPD TIIQVLLDVS SESVNVGDRA WFDCKVTGDP SAVIMWSKEG SEELPENSQV
TGGRLLFNAV TEDNAGVYKC RAKTKAGPLE TRTVLNIGSA KRKRKHTRGR HARRSHRRRA
ANASAAAKHH HHHHHQQQQQ QSLTHSTFGS WFSTH
//
