ID A0A1B0A4X1_GLOPL Unreviewed; 3580 AA.
AC A0A1B0A4X1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GPAI034544-PA};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI034544-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI034544-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI034544-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; 7398.A0A1B0A4X1; -.
DR EnsemblMetazoa; GPAI034544-RA; GPAI034544-PA; GPAI034544.
DR VEuPathDB; VectorBase:GPAI034544; -.
DR Proteomes; UP000092445; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR CDD; cd00033; CCP; 3.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00041; CUB; 3.
DR CDD; cd00054; EGF_CA; 13.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 6.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 17.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 6.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR12916; CYTOCHROME C OXIDASE POLYPEPTIDE VIC-2; 1.
DR PANTHER; PTHR12916:SF4; NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1-RELATED; 1.
DR Pfam; PF00431; CUB; 3.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 7.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02494; HYR; 3.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00084; Sushi; 4.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00032; CCP; 10.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 3.
DR SMART; SM00181; EGF; 19.
DR SMART; SM00179; EGF_CA; 15.
DR SMART; SM01411; Ephrin_rec_like; 7.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 11.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 3.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 12.
DR PROSITE; PS50026; EGF_3; 17.
DR PROSITE; PS01187; EGF_CA; 6.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS50825; HYR; 3.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 5.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..3580
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008403480"
FT TRANSMEM 3445..3471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..167
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 209..321
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 325..437
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 438..550
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 549..610
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 611..671
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 672..732
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 733..791
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 791..829
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 828..976
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1048..1107
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1297..1443
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1462..1548
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1549..1632
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 2020..2056
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2058..2094
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2096..2134
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2136..2175
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2177..2213
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2215..2250
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2252..2288
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2290..2326
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2328..2366
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2368..2404
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2406..2443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2445..2481
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2483..2519
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2521..2557
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2798..2880
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 3366..3403
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 3405..3440
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 171..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 178..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 438..465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 551..594
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 674..717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 703..730
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1078..1105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2046..2055
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2084..2093
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2105..2122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2124..2133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2165..2174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2203..2212
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2219..2229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2240..2249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2278..2287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2316..2325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2337..2354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2356..2365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2394..2403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2433..2442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2471..2480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2509..2518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2547..2556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3374..3391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3408..3418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 3430..3439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 3580 AA; 390780 MW; 33FE4EF74A504921 CRC64;
MGRVTAVSGF WLSGLISLIS LCCALVKAGE DVFSCPNGWE LHGLHCYKYF NIKHSWEKSA
ELCRRYGAEL VAIDSFSENN NTLSIARSND PNHRASDKYW LGLASLDDLR TNTLESASGA
LISQYSGFWS LHQPDPASGE CVAASFLSNS QSWDLGTCES LLPFMCRAPA CPQSSIHCAN
SKCVNQAFRC DGTDDCGDGS DELDCPTQCH YHMQSGGDVI ETPSYPHKYA PLSKCKWTLE
GPLGSNIILQ FQDFETEKTF DTVQILVGGR TEDKSVSLAT LSGKQDLTAH PFVSASNFMI
VKFITDGSVE RKGFRATWKT EAKNCGGVLK ASLQRQTLTS PNYPKQYPGG LECLYIIKAQ
VGRIISIEVD DLDISEGRDF LLIRDGESPM SRPIARLTGK TNDNEKIIIS TGHALYLYFK
SSLGDSGKGF SLRYIQGCKA TITARNGTVT SPAFGLADYP KNQECYFTIR NSMGSPLSLK
FNKFMVHQSD NVQVYDGSST SGLRLHSGNG FTGATVPKLT LTASSGEMLI KFTSDALHNA
VGWSATFSAD CPELKPGIGA LASSRDTAFG TVVTFTCPIG QEFATGKNKI VTECLKGGNW
SVSYIPKCQE VYCGPVPQID NGFSIGSSNV TYRGVAMYQC YAGFAFSSGT PIEKISCLPD
GRWERKPTCM ASQCAPLPDV PHANITLLNG GGRSYGTIVK YECDPGYERT GHPVLICMSN
GTWSGEVPRC VRKRCFEFPQ IDNGFVVDAA RPYYYGDDAR VQCFKGYKLI GSNIIRCNTD
QVFENPPTCE DINECTSTQC DLATTECVNT NGSFHCQCRS GFTATTECRP VGDLGLSNGG
IPDESITTSQ TEEGYTKGMV RLTSAGWCGA SVEPGANWLM IDLKAPTVLR GFRTMSVQRF
DGNIAFTSAV RLQYSDDLTD VFKDYTNPDG TAVEFRILEP TLSILNLPMP IEARYIRFRV
QDYVGAPCIR LEAMGCTRLD CVDINECSKN NGGCDQKCVN SPGSFACSCN TGYQLYTANG
TAGFAIERFE TGERDGDTYQ RNKSCVPVMC PTLLAPENGK LLTTKYDQHF GDIIKFQCNF
GYIMSGSSSL LCLSSGQWNG TVPECNYAKC VSLPDDKLEG LSVIRPDIES VLVPFRDNVT
VTCTSPGRNL RGTASAGFRQ CVYDPKPGLP DYWLSGSQPS CPRIDCYAPT ATPGAEYGQY
VDTRYQSNFF FGCQNTFKLA GQTSHHDNVV RCQADGIWDF GDLRCEGPVC EDPGRPSDGR
QIARSYEQAA EIYFGCNRPG YILINPRPIT CIREPECKVI RPLGLTSGKI PDSAINATSE
RPNYEARNIR INSATGWCGK QEAFTYVSVD LGEIYRVKAI LVKGVVTNDI VGRPTEIRFF
YKQAENENYV VYFPNFNLTM RDPGNYGELA MITLPKYVQA RFVILGIVSY MDNACLKFEL
MGCEEPKKEP LLGYDYGYSP CVDNEPPIFQ NCPQQPILVK RDENGAILAV NFTEPTAVDN
SGSIARLEVK PQNFKTPSYI FRDTVVKYVA FDYDGNVAIC EINITVPDVT PPLLQCPQSY
VIELIDRQDS YTANFNDTRK RIKTSDNSGE VRLTFSPEHA TIAIGTFENV TVTATDKFNN
RAYCNFQVSV QASPCVDWEL QPPANGAINC LPGDRGIECI ATCKSGFRFT DGEPIKNFSC
ETSRLWKPTS VVPDCVSENT EQADYQVTAT VTYRANGAVA HSCLGQYQNL LAQHYTGLNQ
LLSQRCSAVN VNMNVTFLKS VPSLLEENVV KMDFILSILP AIRQPQLYDL CGSTLNLIFD
LSVPYASAVI DSLLNISHIG NQCPPLRALR SNISRGFTCS IGEVLNMDTS DVPRCLHCPA
GTYVASGQNI CTYCPRGYYQ NRDRQGICLH CPAGTYTREE GSKSLNDCVP VCGYGTYSPT
GLVPCLECPR NSYTGEPPTG GFKDCQACPQ NTFTYQTAAF TKDLCRQKCP PGTYSSTGLA
PCSPCPANFF QSVTGSHTCI ECPTNMRTEG AGSKGHEECK LIVCGDGACQ HGGLCVPMGH
GIQCFCPAGF SGRRCEIDID ECSSQPCYNG GSCSDLPQGY RCECPPGYSG INCQDEASDC
GENICPARAM CKNEPGYKNY TCLCRSGYTG ENCDVTIDPC TANGNPCSNG ASCNALLQGR
YKCECLPGWE GIHCESNIDD CAENPCLLDA NCTDLINDFQ CNCPSGFTGK RCEEKIDLCL
SEPCKHGTCV DRLFSHECVC YPGWTGFACD VNIDDCADTP CFNDGICVDL VNGYSCTCES
GYTGKNCQHT VDDCESNPCQ NGATCVDQLD GFLCKCRPGF VGLSCEAEID ECLSDPCNPV
GTERCLDLDN KFQCACRDGF NGVLCETDID DCASNPCLNG AKCRDRVGGF ECICEQGWSG
MHCETQITTC NVLSPCQNDA SCIDLFQDYF CVCPSGTDGK NCETAPERCI GNPCMYGGKC
QDFGSGLNCT CPIDYSGIGC QYEFDACEAN ICQNGATCID NGAGYTCLCP KGFTGKNCEK
DIVDCKDNSC PPGATCVDLT NTFYCQCPFN MTGDDCRKVI QVDYDLYFSD ASRSTAAQVV
PFYTGESPSL TIAMWVQFAQ KDDTGIFFNL YGVESAHTAN NRHLLLQAHS SGVQVSLFAD
LPDAFLSFGE YTSVNDGQWH HVAIVWDGIS GQLQLITEGL IASKLEYAQG RIMPKFLWTV
LGRPQPSTFK HDLAYSETGF QGTITKAQVW ARALDVTSDI QKQVRDCRSE PVLYNGLVLN
WSGYEITSGG VERTVPSTCG QRKCPNGYSG PNCQQLVVDK EPPIVEHCPG DLWVIAKNGS
AVVTWDEPHF SDNIGVTKII ERNGHRSGST LLWGSYDITY LASDAAGNTA SCNFKVSLLT
EFCPPLSDPV GGIQVCKDWG AGGQFKVCEI ACNLGLRFSE EVPEFYTCGA EGFWRPTNDP
SMPLIYPSCS PSKPAQRVFR IRMLFPSDVL CNKAGQGVLR QKVTSSVNAL NRDWNFCSNT
VEGTRECKDI KIDVKCDHYR AAQHNRVRRQ AKDGGVYVLE AELPVLTEEE ETETRARHGR
QQTGGDTYTL EISFPAVNDP VLHTSSGERS SVKALLEKLI LEDDQFAVQD ILPNTVPDPG
SLELGSEYAC PVGQVVMIPD CVPCAIGTYY DSSNMSCVPC EHGTYQSEAG QLQCSKCPLI
AGRPGVTAGP GARSAADCKE RCPAGKYFDS ETGLCRPCGH GFYQSNEGSF GCKLCGLGQT
TRTAEATSRK ECRDECISGL QLGIDGHCEP CPRGTYRSQG VQPSCTACPL GRTTPKVGAK
SVEECTLPVC SPGSYLNGTL NMCVECPKGY YQSESQQTTC IICPPNHSTK NTGATAKSEC
TNPCEQIPEG SAHCDPNAYC ILVQETSDFK CECKPGFNGT GMECIDVCEG FCENAGTCVK
DLKGTPSCRC VGSFTGPYCA ERSEFAYIAG GIAGAVIFII VIVLLIWMIC VRSTRRRDPK
KMLTPAIDQT GSQVNFYYGA HTPYAESIAP SHHSTYAHYY DDEEDGWEMP NFYNEAYIKD
GLHVGGKMST LARSNASLYG TKEDLYDRLK RHAYTGKKGM
//
