ID A0A836XN13_VESVU Unreviewed; 781 AA.
AC A0A836XN13;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF7405309.1};
GN ORFNames=HZH66_004215 {ECO:0000313|EMBL:KAF7405309.1};
OS Vespula vulgaris (Yellow jacket) (Wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Vespoidea;
OC Vespidae; Vespinae; Vespula.
OX NCBI_TaxID=7454 {ECO:0000313|EMBL:KAF7405309.1, ECO:0000313|Proteomes:UP000614350};
RN [1] {ECO:0000313|EMBL:KAF7405309.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Marl-1 {ECO:0000313|EMBL:KAF7405309.1};
RX PubMed=32859687; DOI=10.1534/g3.120.401579;
RA Harrop T.W.R., Guhlin J., McLaughlin G.M., Permina E., Stockwell P.,
RA Gilligan J., Le Lec M.F., Gruber M.A.M., Quinn O., Lovegrove M.,
RA Duncan E.J., Remnant E.J., Van Eeckhoven J., Graham B., Knapp R.A.,
RA Langford K.W., Kronenberg Z., Press M.O., Eacker S.M., Wilson-Rankin E.E.,
RA Purcell J., Lester P.J., Dearden P.K.;
RT "High-Quality Assemblies for Three Invasive Social Wasps from the
RT <i>Vespula</i> Genus.";
RL G3 (Bethesda) 10:3479-3488(2020).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KAF7405309.1}.
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DR EMBL; JACSEA010000003; KAF7405309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A836XN13; -.
DR Proteomes; UP000614350; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR FunFam; 2.10.25.10:FF:000014; Latent-transforming growth factor beta-binding protein 3; 1.
DR FunFam; 2.10.25.10:FF:000037; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR050751; ECM_structural_protein.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR PANTHER; PTHR24034:SF89; COMPLEMENT COMPONENT C1Q RECEPTOR; 1.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF14670; FXa_inhibition; 2.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000614350};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..781
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032823564"
FT DOMAIN 536..569
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 570..610
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 573..610
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 611..655
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 614..655
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 656..696
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 659..696
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 697..744
FT /note="EGF-like calcium-binding"
FT /evidence="ECO:0000259|SMART:SM00179"
FT DOMAIN 700..744
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT REGION 76..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 87828 MW; 11BCE83D4A672363 CRC64;
MCDRRSFRLK RILCVLFFVN GIVLPIGSCQ NAEPRGSFGS KSIARRMDLL RDTERLDERR
FNWDVSLDGE KMLEENTRSF SSERKSKDEN EEDKDAVSRS NGENKNVALH PSEDRTRASF
LRQTLNTTAT TSLGEQRRST GINEGNKTRK KNRRTKDSRN NPSYNIDGTT DVRENEIKIG
GRSSLQENKE NVNTDSTSKK SRYSQTRKYR GERRRRRKNR DRKRGRKRSR QNDDRRMDDE
RRRTSKFKKR TENEGSEQSF GNSSNIGLTY GGKNVSIFRQ DSTNFDGLDS STGGAPSNLR
APSITTTTTT NADDRKSLPQ VSPRRDVYVE NVERELSKQL EKEIARSGMI NLSNRVLTGS
TTHRDVTSYD NDRNKLSNEI IIDDRARFGN SRYDAEKMLG YSRTEEDLPI LDLENEDRPK
FSSPSRLHDQ PIVSLITSTT TTTTMTTTTN ADTYDEDNPK GDLSCINGTF LPAPLARHAL
IKYVKSSIPG HEYLEADYEC APGFYMVSTG SRLLCRNRQW IGQVPKCKLK QGSDGVCSEV
SCEHVCKEID GRAVCSCYNG FRLDAYKCID VNECEENNGG CEYKCVNTPG SFRCECPKGM
KQGEDRFTCI DINECLLNNG HGPCQDTCRN LVGGYECSCE GIQDTVLSAD NHTCQNAGPC
SVNNAGCSHT CLSTMGRVFC LCPDGFMLED DWKTCQDVDE CAVPDLQTEV CRYGCINTQG
SYRCAEPTEL KDQPIADSLS ITCLPGYEVS ADGSCVGLYS LMIIDTPREV KLCPHGHSQP
I
//
