ID A0A1B0CSP3_LUTLO Unreviewed; 2876 AA.
AC A0A1B0CSP3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Multiple epidermal growth factor-like protein 8 {ECO:0008006|Google:ProtNLM};
OS Lutzomyia longipalpis (Sand fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Lutzomyia; Lutzomyia.
OX NCBI_TaxID=7200 {ECO:0000313|EnsemblMetazoa:LLOJ007892-PA, ECO:0000313|Proteomes:UP000092461};
RN [1] {ECO:0000313|Proteomes:UP000092461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jacobina {ECO:0000313|Proteomes:UP000092461};
RA Richards S., Qu C., Dillon R., Worley K., Scherer S., Batterton M.,
RA Taylor A., Hawes A., Hernandez B., Kovar C., Mandapat C., Pham C., Qu C.,
RA Jing C., Bess C., Bandaranaike D., Ngo D., Ongeri F., Arias F., Lara F.,
RA Weissenberger G., Kamau G., Han H., Shen H., Dinh H., Khalil I., Jones J.,
RA Shafer J., Jayaseelan J., Quiroz J., Blankenburg K., Nguyen L., Jackson L.,
RA Francisco L., Tang L.-Y., Pu L.-L., Perales L., Lorensuhewa L.,
RA Munidasa M., Coyle M., Taylor M., Puazo M., Firestine M., Scheel M.,
RA Javaid M., Wang M., Li M., Tabassum N., Saada N., Osuji N., Aqrawi P.,
RA Fu Q., Thornton R., Raj R., Goodspeed R., Mata R., Najjar R., Gubbala S.,
RA Lee S., Denson S., Patil S., Macmil S., Qi S., Matskevitch T.,
RA Palculict T., Mathew T., Vee V., Velamala V., Korchina V., Cai W., Liu W.,
RA Dai W., Zou X., Zhu Y., Zhang Y., Wu Y.-Q., Xin Y., Nazarath L., Kovar C.,
RA Han Y., Muzny D., Gibbs R.;
RT "Whole Genome Assembly of Lutzomyia longipalpis.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:LLOJ007892-PA}
RP IDENTIFICATION.
RC STRAIN=Jacobina {ECO:0000313|EnsemblMetazoa:LLOJ007892-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; AJWK01026351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01026352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01026353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01026354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJWK01026355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EnsemblMetazoa; LLOJ007892-RA; LLOJ007892-PA; LLOJ007892.
DR VEuPathDB; VectorBase:LLOJ007892; -.
DR OrthoDB; 5471913at2759; -.
DR Proteomes; UP000092461; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 4.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 4.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR PANTHER; PTHR46093:SF17; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF13415; Kelch_3; 2.
DR Pfam; PF13418; Kelch_4; 3.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF01437; PSI; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00423; PSI; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF117281; Kelch motif; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 3.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..2876
FT /note="Multiple epidermal growth factor-like protein 8"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008406214"
FT TRANSMEM 2712..2734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..163
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1198..1239
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1274..1320
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1321..1375
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1355..1501
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 1499..1532
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2310..2358
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 2852..2876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1292..1301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1304..1318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1343..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1522..1531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2330..2339
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2342..2356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2876 AA; 319285 MW; 4F6FAB4DA75D31DF CRC64;
MMARRVVRGC RRSWPVGVAL LLLFAILQNQ AQAEPLRVAA PPGTPPPNQP CDRTRRIFTE
PYGEISDGPS GFNYTQDSHC EWLIKAKNDS QYITLTFRSM GTECSYDYIF VYDGDSFRSP
LLGSFSGKTE PQRVVATSGS MLILLYSDTN YVLDGFKAEF SVTNCPNNCT NRGKCVNHKC
ICHGDWMGVD CSGNACPDRC GEDEGHGVCS GECKCRDEFS GQSCSLHKSH PVGNEWHWLS
NSIEGLSPRA AHTAVYVPET DSLYVFGGYD LNNVLSSLQI YRFEKSRWED EWGMKLKSSH
KFDKTHVKEA LETDSSQWGL SASASFLRNT LSTVLTDHQL AIRDKQSTNH PHINRTTDDI
LEDIIGRSRP TARYGHAACL MPDGFIIYGG KLASGGLSSN LWFYNVSNGG GEWTLRAMNS
TVKPPALTRH TLTLAGDYLY LFGGSRDNGE FSSRMFRIKV LGQTEEDGDE QWEEVTPRGG
KVLDVRVVAH TTVYHKSSNS LIVYGGVVAG VARFSKLSDR MFAFQLDKRH WTEIMYPRTP
LRDAYIPRER AFHTTTIVGN YLIVFGGYSH RHNKEEICYD NQMYLYHLGC HTWVNQDVLG
VGKRSRYPKQ QGVFAHAASL RNKNTLLIVG GYHGNVNGDL LAYTLPPMLV IKDEETFEPE
PLCYKHTSVT ECLSDPECGW CSADGVCYGR TVGANCTTNL QTTRCPGICP ALGDCHSCLL
HGAVDIVEKN HQTVAHKLGL GQCTWCVQNA RCHHKDDNYG VCGEDTPSQS PGWWGTKGTE
IVAANQCTEL DKRPGLTFIK YLHPVNWTMP DQVTIVNATM VDFNAPSSNT HTEQSFHGDM
VARLAGFIRP PSSWEKSGEM LRVCASYSDA TLRMSTNGDI TLAANISTEA TQCTMAQWPP
LKSSRIMVDL QARRSVGNGN MFHHHHHSKM GLQHNRTNEN AKAFTFEYLE PFSNGTNCDV
YRNCLHCLSD SACGWCEVTN TCLRRTDNEM DMCRMDDEWM YLTLQPSHCA NCSNYISCEQ
CVESGLCEWW AEDARCSRRG RAPLAVTDVA QCPAPCYARE TCSACLDERG RCVWCEATQQ
CFSFSVYTSE YQFGLCREWL DQTMPLAPSS VQMDGVMTDE QAMAVQQSLP AQQCKSCARF
SNCTSCLRSL SCGWCFDRDN PIEGICMQGD FNRSTEDCAA ALNTTQQEAE WAYAQCPDVD
ECGLGLHDCH PEAKCTNTHG SYNCHCRRGF IGDGRTSCVR TCFETCIHGY CEGAPNYKCR
CNLGWTGADC SINCGCNNHS TCVEEVGKCD ECQNWTEGEF CERCSPGSYG NATSFIGCQP
CNCNGHGNEA LGVCDVQTGE CFCQDNTEGF HCEVCNREFY GDPRDGGQCF FQCEARGMLT
HIGRQGIGSM QSHKSLWGGA DTRECLWIIR PRTPGGSLLN TSLIQLHINR DDLNVSCVDN
AVYVYDGLPD LTGNTQQSQL LAVFCNQDST AMTVEAHTGH LTVYYKQGPV GQGFNAMYSV
HSCSSGTCQP PHVCTDNGKC VCPQGFTGPH CSIERCPGNC SVALNQGTCD TSYGRCLCAT
GFGGPDCSVK LKLRNVVMAE LFNSQLISES LEHLRKTLPR FGHSMVADKR AYLWIFGGYS
LSHGPLNDIR QFDTKNNTWM QVTVDSTPEA KMPQGRYFQA AEIVSSKQAI FVYGGLTGQG
KGYANSILGD FWQFSLQNQR WDEVEMEDVK PPPLAGHTLT FVKDGDRECL VIIGGFSTER
GMQNELWEYD VNTGKWEKLA ATGAGPVGVY GHTTVFHANN MVLYVYGGVE FEGQRTVISN
KLYALQYNKM MWSELPVFSE LIRGVNHMPR GRFLHSAITT DGYMIVFGGQ TNPYNSTDVM
AAYVFKCNYW VRLTEEVEIV GNLPSPTYAQ AMSYEQESGS IYVIGGWDGN TRSRVTRITV
PSDLCELWSS GKYMCRNFMG CSFCSVDNTS HCFSSGRSEV CTGQNARTIF NYGALCDDTW
LSKRKCSTFH TCTTCLASWP SHAELSPACQ WCESCGGEGR CIPAGQECDK DDDCGSPQTT
IGLVNQCPSL KCAATDCESC HALSACSWAQ NGTDPWQCVA TELVEEEKWT PIAGACPPRC
NIHRNCSTCL AAHTSEGGWE HCLWSTQLNE CISPSYQPLY CAGGVCGLVL THEDPLNCPE
PCSSFTQCST CLRHAHCGWC SREGSEGDGV CTEGSIESPT EYPAASTCDI IYASRHNITN
VDPEDEFKWY YVQCPPENEC INGHHTCNPK SEQCVDLMIG YECICGVGFR EDQGECTPVC
TQGCVRGNCI EPNLCECHFG YVGANCSIQC QCNGHSNCGG PDRLDECLEC HNNTMGAQCE
KCQRFFVGDP RNNGECVPCI DYCNGHSDLC VMKSSDAHVF NLTRNELEKY LTEGPTLDAV
CLRCDNRTDG DRCEGCITGH FRGTENHRDA CRPCECHGHG NTCDPVTGDK CNCGNNTESD
ATCSATASKN SAQQCWSVQC SKCKETYSGN PIEGHQCYKH INVESKMCFD AKIIDECKIK
PSPLKPGQTV FFVIQPRFMN VDIRIIVDVT QGELDLYMSP QEDSFVVTTN QTTGYHHISL
DHHYRWVTEI DSEIITPLDI SPATRYDFDN MTITSEEKIF WTPHIHDCKS LSGSGFYVKD
KHARDLSTYI TLNQCNTLLR VFGLKNRLVL TLPQNAHNLS ATRFFMALKA SAGPAASYGL
VFFRQDQLHI DLFVFFSVFF SCFFLFLAVC VVAWKAKQAA DVRRARRRHV VEMLHMAKRP
FACVTVHVDP DTESPVQNRR TRGRVKQMIA QGQQQDVRPV AIEPTADGVA AVGTVFIRLP
GKYRSPVGLA LASALITLPR MYPTGSRAFL RRRGSGHGVQ QPQAQQPPNL QPPRNN
//
