ID A0A1I8EZU5_WUCBA Unreviewed; 3646 AA.
AC A0A1I8EZU5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:maker-PairedContig_740-snap-gene-0.22-mRNA-1};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_740-snap-gene-0.22-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_740-snap-gene-0.22-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_740-snap-gene-0.22-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR STRING; 6293.A0A1I8EZU5; -.
DR WBParaSite; maker-PairedContig_740-snap-gene-0.22-mRNA-1; maker-PairedContig_740-snap-gene-0.22-mRNA-1; maker-PairedContig_740-snap-gene-0.22.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd02795; CBM6-CBM35-CBM36_like; 1.
DR CDD; cd00055; EGF_Lam; 20.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 18.
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; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 19.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 21.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 4.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 16.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 68..342
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 597..647
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 776..830
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 831..883
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1501..1546
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1547..1591
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1592..1639
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1711..1898
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1932..1981
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2040..2092
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2140..2186
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2187..2234
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2799..2992
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3004..3187
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3193..3357
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3441..3640
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 2399..2426
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2543..2570
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 597..609
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 599..616
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 618..627
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 801..810
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 854..863
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1501..1513
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1503..1520
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1522..1531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1564..1573
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1615..1624
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1951..1960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2064..2073
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2076..2090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2160..2169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2187..2199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2189..2206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2208..2217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3646 AA; 406060 MW; D26EF0DEF38E81E0 CRC64;
MSSSVHGGST GLTEIIFVEH FVKDQCSLFR MYSGSYFYTP SNNNKVVGEL AMLPVLLLIA
AAKTGFIWGQ VLVPPYTNLA LDRKIEASST CGELNGQPMK EIFCQIAGSS QYTPLNQYSY
STGEDGVSVF AELKMEKQSF VQGGQMCDFC QSNSSFAHPA TNMVDGRASW WQSPPLSRGI
QYNQVNISIN LEQEFHVAYV WIQMANSPRP GSWVLERSID GGKSYMPWQY FAETPAECDR
LFGRHTLQPI LEDDTVICTH EFSGIHPMEN AEIMINLLEN RPGKHNFSHS EVLQNFTRAT
NVRLRLLRTK TLHGHLMDVN RRDPTVTRRY FYAIKEIFMG GRCVCNGHAD TCDILDVRRS
NILLCRCEHN TCGDHCEYCC PGFEQKMWQR SKEGAEFVCE PCNCHGHSEE CVYEKELDRM
HSSLDIHGNY DGGGRCLNCR DNTEGINCNK CIFGYYRPKT KWWNETDVCQ PCVCDPAKHT
GDCEDETARC VCKPQFTGVN CDRCTPGHYS PPKCKPCDCS VNGTLDDICL PINGRCPCRS
NYGGKLCQLA IVMNSARCTI TVMKAQHSVC AKPISLDLRA IVALMDTLVI LSVNVNCDCD
AIGTEDSICD KVTGACLCKS GFSGSRCDEC SLYFYGYPFC KECGCNKRGS KSAKCDRKNG
DCPCYANFTS KKCDRCAAGY YDFPKCKPCS CMAIGSKGMT CDNNGQCFDG QTNYVETVLR
PVYAFVLLYI IKCYCKKNFQ GERCDQCKTN FYNFPICEDV FFLFPIVVVL LNVAECNCNP
KGVVAGFPGC DKVEPGELCT CKTHVTGRIC DRCKPTYWDL QYYHEDGCVQ CDCNLAGTLS
GLNECSIEGG QCNCKRHVVG RRCDKCADGF FQLEMHNQFG CQACNCDIGG ALGIGCDMQT
GECRCRPRIT GQKCDRPIEN HYFPTLWHNK YEAEDGISME QNAVRFTTDK NKFPNYSWRG
YAVFSPIQED ILLDVAVNKA SLYRLLFHYI NPTDVQINTR IAIMPLFTHT QDVEQKTRLN
LPSTSEPTTI AINPQQPFVL SPGKWRIKIS TKQRLFLDYI VLLPSEYYEG TVLKERIFEP
CQATDSQNTT CLELLYPPLP TTSRADIIEG PITEQNNSST QRVEESDKIL RVLTPNTNKA
GWEPALLILI ENLFTITDEA AIVQTNNESR KIRISLKVLV PENNYYIFLM EYYNANSKTV
SLSLEVRQYG HLLMKENIIF KHCPYSTFCR DIVSSDAGIA LMYLKDEGDV EITLIIGSKH
KFGLAAANLI KMEDWDITYL QQVPVCIRKN GHCVSQWFPL VANGILNEAE SQINANNSII
GEKLPFIIAN PKEVQVIALD GNMGTVEVSG VVPSHGDYVF IVQYFNPDNT LLTVDVTLQN
GHLYHAEISF SYCPSVIGCR AVIRDKERRD VIQFFVDDKY TASFYFNENQ KGPLYIDSIT
SLPFHSYSDT LLTPLPVDIS AQYIQKCSLN NFKNDPSNVS EYCRQKVFSL TSEHNMAALP
CECNSQGSIS FACEEYGGEC SCRPNIIGRR CDRCASGYYS FPDCIKCKCP DNHLCDENTG
QCFCPPHVEG KHCDSCVPYA FGYDPLIGCQ LCGCQQNGSE ARQLQCDPDN GQCLCKVNVG
GRKCDKCLPG FYGFPHCYEC ACEIKGTTEE ICESTSAACK CKIYLTTALF QKNVIGENCD
ICRPGTFDLR ASNSDGCSEC FCFGATDRCR SSFLPITFVN FDEEAWKVYP NESVLHSHGK
IVYEAKIDGK DDVYFLAPVR SGHDYSTSYG LQHFGKHILS FVILSNPRDG ETKMSSAPDV
QLVGNNTVLD FWAREQPANP RIPFYVDIIL LPENFMESTG EPTTRDTLMM VLHDLDELRI
KACYYTNCEL ASISELQLEI AKDDQTTSDS YTASSVEICQ CPPPYTGLSC QQCSPGYYRV
SNGRYLGSCV SCNCNGHSGS CDPTTGICFD CEHDTFGDHC EFCRVGFYGD ATKGGPYSCM
PCACPYATDS NNFATSCQVS ETGLLESCFC KEGYTSDHCE RCSIGYYGQP TAIDGSCHKC
NCNNNNDLAI DGSCHPVTGD CYLCLNNTDG AHCEHCKPWF YGDAVEAKNC TNCACNQCGS
SLCDNSSGKC ECLTNVEGEK CDRCVTNAWG FIRCHGCEMC NCALASSSPQ CDAETGQCSC
MPGAAGQMCE ICEYGYWNYG PTGCSKCDCE ADLSMGTVCD VNTGQCHCQE GATGPRCDQC
ALHYVRIPNF GCRLCDECVH SVMHDLDKLT DAVALVNGTV NNISTTALTG ARLKRIHKKI
NDLKPIVVNH MNSSSDVDIK SLSSNGILDS ASNVVSVIVR ANRSLDTLST MGSTLNGIIN
RTNIFLSGVF DRVELAASVV DSLKNLVFSL GKDSGAVYRQ KWLTDSTLLL QKIRNAADDE
ETRERMKDAE DETQKLLSRI RELKDEDNVM HAKYFTVRDQ VDRLMNNITD YHSFLYRAAN
SVENTLQRVN NSNIRHINSV QAGVKAGEAK IRETHAFINS LKETSEISIE SLSNLNKTLR
EVISKVQVVF GQLNIMNGTY RHRRTRNINK NEYRSKLKEL ESEALFLSSL FGRTRTEAKN
AVAAANGYKE LIEHLKKARD IANRTSLNAE QARRFHEEGV AASARTFREK SADLLRSAVD
LKQSSVNNVD VLKDIFLGKA LELQFFIENQ KRILDSLHPK FDDLEVNAKL EHSLTASEEA
RTRTDSTISL FDRVKPDLEK MVSRSKKLVE SISVSANNVD TAREQIWKLV NESSPIMEEL
KMRQHAALNT STTIEHCREK LNLLKEKITL SRDLANRIKL GAHFEKGSIL ELPLPPRITR
FAAYTDIEFF FRTTNTSGLI LFFGNELGVA GTRAVPTDDY IAVEVERGHL RIVINLGETP
TQLVSDSFVT DGNWRKVAVD RVGKTIKLRL SSPNSVNYEE EKTRTVGGFK SVLNLHQKKS
RLFIGGVVPG VNISPEIHNR EFTGDIEDLR IHGETLGLWN AKKGGNYNVK GAMKKFFATS
LTNEIALSFN GDGYAVHKLG IWNPRKQTIF SLTFQTYSPD GLFIYLGKEV RIMQLLLSAA
LNNRGFLSLE LQDGRVKLSF DFGSGVGRLT STGNNYNDGK PHCVYVHRLE RHARMQVDDS
DVSEGDSPGT MFELSLSDVF YLGGVPSDVS TRTAVVSMNG CIERVKLDNR LVDLSKSRTA
RGVQLGCSAR NVRVVSMVSE RSSATFSGFN AKEDYLELTF RFKTKRSSGI LASVISDEQE
VLLQLRYLDG FIFAEYGSDN KDVAQIEFRS IADGHWHYFA AIVKPETIRL DLDDLYSNEI
RRTVANNEVV GVPIIVQFGQ SLDSNLYFEG CIGDATYNGQ LLDFVEASTN EVGLTDCSFL
EDISTTSMSS GQTTTNQPMN VSIPATNSMQ PFVTETDNEF TAESRISSGT LFLSTLRGIA
RKSDECALLK RSFGGRPDSS GTRFGLSPSS RLEFDKPPAS FDKNSLFSIQ LRATASNGII
MFTTNNRHTD YLALYLVNGI VHFAYNSGSG QAVLKSNRSV MDYEWHSIRA EREGLAGTLY
IDNVMEANGQ SPPGTDAVDT QPPIYIGGLP TDLVPFASRI LQGAKSVFGG CLRDFKLNEM
KFDVLPVEIG TVPCSHYTEE GLYFGPNGGY AVLNKNLKVC DLDESS
//
