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Database: UniProt
Entry: A0A183GYA6_9BILA
LinkDB: A0A183GYA6_9BILA
Original site: A0A183GYA6_9BILA 
ID   A0A183GYA6_9BILA        Unreviewed;      2667 AA.
AC   A0A183GYA6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Ig-like domain-containing protein {ECO:0000313|WBParaSite:OFLC_0000021501-mRNA-1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0000021501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0000021501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   STRING; 387005.A0A183GYA6; -.
DR   WBParaSite; OFLC_0000021501-mRNA-1; OFLC_0000021501-mRNA-1; OFLC_0000021501.
DR   Proteomes; UP000050787; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 3.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   PANTHER; PTHR45836:SF4; PROTEIN SLIT; 1.
DR   PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 6.
DR   SMART; SM00181; EGF; 13.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM01411; Ephrin_rec_like; 7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   PROSITE; PS00022; EGF_1; 9.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 7.
DR   PROSITE; PS50835; IG_LIKE; 1.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2416..2434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1378..1417
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1457..1492
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1494..1534
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1536..1577
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1579..1616
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1617..1653
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1655..1695
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          2646..2667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1382..1392
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1407..1416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1461..1471
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1482..1491
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1524..1533
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1567..1576
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1606..1615
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1643..1652
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1685..1694
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2667 AA;  301692 MW;  FADB44E3AB99FB77 CRC64;
     MTVFYHLEDS KRNQSDESNA MMNRYSKNCI INTVNDVHVN VNTSAMLWCF LSANCTNITS
     ISDSFQIKWY RNNYQNISGI SLKGKNGSWG LFFESVKNSI VLILQLNDNG RYYCALLDKK
     RGVLEKHPAD LYVYQTFETG RSWPEIVQNS EPVKEILFTT DNNDWSIISE NISMEDISIV
     NGTKPTNKYV FIAMHLISKK ERKKMLYAKN KFFNSMRIAY CRSWLFQQVV LLPGGCYVME
     IKYQSENCST CSLELISHSV ENTDLANYSL AYSNETNIVL IDHGFNFFQK EICLQQSNLF
     VGIRGDVNSM VLDSVKIYTI KCPEHLNLWH YLFFLRLQLN KKKVETLFYK ANIDSLRCWL
     LGTSELYTVP TNNCHGTIVF GQCLHGARTI VQGQTPELFC TQHGKWIYNM QNANLCFCST
     NYTSEYDACV ERGPVCYVCS GNVGTDCNDS SAVFCDKRQY CFTQITKFLG GNIVRKGCIN
     ECFANPVGCT TKEEACEMCC QEDYCNSWLN MSKIHNEYLR PYPMFRAICP RNITVLRYSK
     GLFAAAAIVP PLIYNYEPFY HLTVDQNIFN GTVQLIKEIN AIVWTVTNRM SQFRNCSTYV
     SYKDYWAPVL DCPSLYIDFL ANTTSLKFRS RFPNIDYRDL GSRISLHYAP SNGTIAEIGE
     PVKVTVTATD ESNNSAQCVF WYIGQVADCP LWPINETEYE CKGSMNQRIC KRRQKCSGIQ
     FPHHITALHC VAGQGWSYMS PQSIAVVPMN LFRLPVCLRN SANDVHLSMN LATNSSLNQS
     CKAALIHKIQ QLPKMHEAEN CRQLNWTFTG LLVVHNNIFV NYTMRHENTS TTFKCAAQFV
     RQIIKGKLAF NALKSTCKNI QFNALSANYS NGCFKDECAP GFYAAANGCY PCPLHTYSET
     IGAKNCTRCP KNTFTSKTGS FSSQLCQKKC PPGFFSPTGL EPCQACAVGF YQPFFGSQSC
     NNCISPRKTS AVGSVSASDC CKPGWFSRTG FEPCMKCPIG FYQDRAGQTT CIACIINANN
     KQISVNHCKG FFCTESGCKN NGKCSNGRCI CPFFHIGLDC TVALNLCLAN FCPRSEECHF
     DGVITSCIYN GDPSSEVSRM IWWESLWKLK QQKQQKQLLD EETQKVVNKS SLLASKRLAN
     ILAKLNTDSG LIDKEFSVWS KNARIRREAN KETIISTGSH SSISDPTQPF MQFISDHLTS
     SEIATTGEWK SDLSHTTKLI KTFSSSLIKM SNHGRDNVES TTPISTVLTV INATSSIPQI
     RCSDRLNFCK NGNCATSSNG SISCICQKGY KINGSNYCVL LQSCDYNPCG QNICKNINNE
     YFCQCSVAHN IFHQQKWCPI GKECDQKNLC KNNGISICDY KSRCICPTSY YGEFRSEKTE
     PCKNLPCDHG ICISQFDQLL PYYFCRCDPG YYGERCTAHA VCTDRNINCK HGYCHKNDDT
     ANCKCYPGFT GSDCSEEINH CNSSPCVHGT CKPKFLGYTC ICDEGYKGNR CENLIDPCDE
     KPCNINSECR ALSYGYRGKF LCNCAAGWTG KYCTELIDLC IHSQCISGST CITRPGVNGE
     VSYVCICPPN KAGIFCNESV DYCKPMNPCL NKGICQGRDD GYTCHCKPGY QGDHCQYNLC
     SPNPCQNNGN CTILSLTTYN CSCPQYYEGV NCTVVTDACA ASNFDDYCLN GGKCISNNFE
     PVCRCTYQYE GRRCENKKDL DFNVIFNKQT RNLRSTPFDS SVLKQFTLCF WIRMISIDNS
     SFVSFLNFDQ QGFGQKVLSI TKKVVKFGKY IGLTNMAENE WQQFCLRKKK DGTTEWIRNG
     EIVWKRKWDM PPINGSLRIL LGALGSFHGE MSMVQLYRVA LSSKQINNSI HHCKQWLQSI
     ITSNETPLID WNHFIGVKRG NRNFPAICTI SECVLNPNSC NSTIDKVPPK IINCPADIKI
     TSKDRLTVVN WFPSKSNEIF ADNDIINMGK YHIVYIAEDR AGNIETCQFN LIIATMNCSN
     PEKTVGINFT IRNVHSENVQ KVACVECEAN YMPIHPITDF YFCDLMGQWT RWPHGVNFYF
     PSCLKYQAPL QQLSGLVTVT ANCNELEMYE KNLTTVILNA NKQFNHFCTT LNCTNELKIW
     SNSSCNSRIL RWFNKSNENI DLYYSIAVNI TRKSIKSIVI ENLNKIFGNN TGNTRMSWQC
     PSKNYPAQIF GHDTRSCVKC PPGMYCVNDK CMPCPENTYK KDSGCKQCIP CPNNTITGPI
     IEDIGYQTNC SAGFHYSIQE GSCVECPKGM YQDQPGQLRC NACPEFRSTL KRGSVHVSNC
     TVTCGAGMSM NAQSTCVKCA KGKYRLENSS EVRCTPCPDY FTTPDNGSVD QSNCTVLDCP
     PGTYINLSSP SECFFCPRNY YQEKSNQTEC RKCMKSLITL GTGSVHPRQC MKPLFWNPVV
     SDVDISKHFT SSRRPIFGFI CFICAIAFLA LLYFQRQRIR TLFCKIRKTR LKHVATQNYY
     RDSSFTYPIV TITPADISAT HDFIEDIVPK NPEPQEMVEI YQEIYDGLHS MAEGTSRMSN
     NELASNQCFR SISRVRLEVD TTLKAEFCGD PKARGMDSSG FPIDSADYEY ADQCKSMDPE
     NYGQNLQASA FEENQTSRFQ QRFDAYRNWN LRIPLCEMYA EPTEYKLFLP GTSNISIKET
     NGILRDENKN EENKDEESDD EVYIVKT
//
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