VIT3_SOLIN
ID VIT3_SOLIN Reviewed; 1761 AA.
AC Q2VQM5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Vitellogenin-3 {ECO:0000312|EMBL:AAY22961.1};
DE Flags: Precursor;
OS Solenopsis invicta (Red imported fire ant) (Solenopsis wagneri).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Solenopsis.
OX NCBI_TaxID=13686;
RN [1] {ECO:0000312|EMBL:AAY22961.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tian H., Vinson S.B., Coates C.J.;
RT "The vitellogenin genes of the red imported fire ant, Solenopsis invicta:
RT cDNA cloning, protein expression and promoter analysis.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q7Z1M0}.
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DR EMBL; AY941796; AAY22961.1; -; mRNA.
DR RefSeq; NP_001291514.1; NM_001304585.1.
DR AlphaFoldDB; Q2VQM5; -.
DR SMR; Q2VQM5; -.
DR PRIDE; Q2VQM5; -.
DR EnsemblMetazoa; NM_001304585.1; NP_001291514.1; LOC105205783.
DR GeneID; 105205783; -.
DR KEGG; soc:105205783; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Secreted; Signal; Storage protein.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..1761
FT /note="Vitellogenin-3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378061"
FT DOMAIN 24..796
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1402..1591
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 336..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1404..1554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1426..1590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1761 AA; 201053 MW; 7325132973BCE294 CRC64;
MWFPVVLLLL VGVAVAVPDH EHAWEPQNEY QYSVFVRTLT GVDTLKQQYT GIQLKGVLVI
QVKSEELLQA KYINPRYAHI HQELSNGPYS KIPEENLEYR DIPMSGKPFE IKLKHGVIRD
LLFDRNVPTW EVNMLKGIVG QLQIDTQGEN AIDSQSTQIP SNSEPSSATF KAMEDSVGGK
CEVLYEITPL PQHVAQTRPD RVPMSSVPSK GHHYEVKKLK NYEKCQERQL YHYGMDVKMT
KENMMKRNKV VSELSTTHIV ITGTLKSFTI QSTEMKNEIT VQPESSDSPI GTVYSITKLT
LAKINKISNS WFGPLELSNV ESTGNLVYIF NNPFSDSEQR KVGQPSISRN SEQENSLETK
KRSFHSHSSS SSSSSSSSSE EENESVMQSK ASLRNIFMAP NVPLLPYFIG FKGKTIMKSD
EHNVMQLAKD LLLQIAKEIQ NPSEGYENTL EKYVNLKNLI RTMDRKQYTE LEQYVSQFNK
ATVEGENAWY TLRDAVVHAG TGPAFVTIEN WLKSGQVKGE EAAELLSKIP KSVHQPTPDY
IKEFFKLIKS SVVTQQEYVN VSAPLAFAEL LRNNYVVPSY YPVHSFGRMT LKGNEEIDNY
ISYLANQLQQ GYLENNTQKI QTFIFALGVT AHPKIISVFE PYLEGKLPTT KYQRMLMVAA
LYDLSRDIPK LVGPIFYKLY MNENEAHEVR CMAVQQFILT DPPMITLQRV AKYTNYDQSD
QVNSAVKSTL NSIINTKRPE WRNLANKARS VRYLVNPKNY DTWYSKGYYI DFENWVFKGL
NVKMVASNDA VLPRYVYVGL DSIFNFLRKP TFEVGYAVSS YRQVYDLINE LWNSYQFEEM
REKSQGSRVE KLAQELKIKS GQKNNLEGHV LFNSVYGSMV YPYDKHRIRE AVAALKKLLT
SDSKLKTTAF NNFEKIVSFP MEMGVPFVYS FELPVFVKSE INFKKGEPIT SRSGVYETLF
CNRVQKRFGF IAPFEYQNYI AGIDKNGIMR VPLKYETNID IKQKNFALKI HPNIPQSGTS
TGLTHYSVVP FTTRQNIFNL QPVSNEGNTR PVITSEIHKM TKEKGPFSIK IESDTTKKES
VLEDIVTGIS KSSNSNNERY MKIDTTFESK QVAKCEIQID MTFDAVTIHG KNQQPSHKEM
QHHSKLDWKP NSKERREEIV NVLSAGLKSG TVFVADVSFS LPRLQDNTYV FTVGSVRSNI
DQKLRHYFYV NTNAAQEVKY ELCYSQEVQY AYPTPLNFEY AINNEPKDKL KGVLRYGRTC
NTGNEIVITG SSSQSPQLRD MIENSSITKQ CMEEIQKGKK SVRTCNKATD VAQVRDQLNF
HIDASQLSEI RQKYDQVIGL LNYTNLSQYN VQQNSETNTI VVQNPWVMVP TVQEPWYRWA
IKPSESQRQS EIDVLLDEVS QPSCTLDNDK ILTFDNQLYN VQLGKCKHVL LTTYPQDSHN
RRNYIPESSK VAVLAKDTDN DSRNVYVWLG NLEIELKKVG NDLKVAINGQ NVEIPEKGHQ
ESNGNEIIFE IVQLPDGSLS VISEKYGITV IFDGKHVRLY ANGATYRNAI RGLCGNYDSR
RDNDFLTPKN CLLTKPEEFA ATYAMTNENC QGPAPENKRK AEGAMCIEVP EQQQMNVISD
REAGRMMTEG GNWGYHQSNR KKEHGQDSKR GHGHKKYNQK DSQEGGSNES QYRKKHNIVY
RTRVVEMDDK ICFTTTPVPG CLQDTRPVER VPKKYDLYCL SKNNESMDLK RRVEEGAKPD
FTQKPVNKIQ NFQIPVSCSA A