VIT1_SOLIN
ID VIT1_SOLIN Reviewed; 1641 AA.
AC Q7Z1M0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Vitellogenin-1 {ECO:0000303|PubMed:11249942};
DE AltName: Full=Vitellogenin {ECO:0000312|EMBL:AAP47155.1};
DE Short=VG {ECO:0000303|PubMed:11249942};
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:AAP47155.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body {ECO:0000312|EMBL:AAP47155.1};
RA Lewis D.K., Chen M.-E., Vinson S.B., Keeley L.L.;
RT "Cloning and characterization of the vitellogenin cDNA from the imported
RT fire ant Solenopsis invicta (Formicidae: Apocrita).";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11249942; DOI=10.1016/s0022-1910(00)00155-4;
RA Lewis D.K., Campbell J.Q., Sowa S.M., Chen M.-E., Vinson S.B., Keeley L.L.;
RT "Characterization of vitellogenin in the red imported fire ant, Solenopsis
RT invicta (Hymenoptera: Apocrita: Formicidae).";
RL J. Insect Physiol. 47:543-551(2001).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11249942}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:11249942}.
CC -!- DEVELOPMENTAL STAGE: Abundantly present in reproductive females but is
CC present to a lesser degree in other female caste members (alate, virgin
CC queens; and workers). Not expressed in males.
CC {ECO:0000269|PubMed:11249942}.
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DR EMBL; AF512520; AAP47155.1; -; mRNA.
DR AlphaFoldDB; Q7Z1M0; -.
DR SMR; Q7Z1M0; -.
DR PRIDE; Q7Z1M0; -.
DR GO; GO:0005576; C:extracellular region; IDA: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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1641
FT /note="Vitellogenin-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378059"
FT DOMAIN 19..790
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1410..1597
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 322..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 172..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1435..1596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1641 AA; 186288 MW; 0A557609857DEEB3 CRC64;
MWYLAFLLII GAYAADHAWE TGNEYHYLIE SRTLTVLDKL SQQFSGIVIK GGLTIQVKSP
DTLQAVVSKT QYAPVHKTLE NWNDEIADLK FDELSMSGKS FEIKLKHGVI RDVLIDQDVL
TWEVNLIKSI VSQLQVDLQG ENVIASSDNQ IPDDSQPFGV YKAMEDSVGG KCEVLYSITP
VPENFDSIPF PNLRKDGLNF FVTKTKNYNK CEQQMAYHSG ITDKMNWKLG SNDGVLSRSS
TSSIIISGNV KHFTIQSSLT TSEIFVRSKL HDTYSSAVYD SVKLTLDRMN QISNPMSASN
NLVSTGNLVY IYNNPFSNQR KLRQPSVSLN SMEARSSENS NEENRSDDDR SNFLSNSGEE
REYLQSKPTL NEAPESPLLP YFIGYKGESI QKSEDITSVA ARFIAQIAWN LETSPVNAFN
FSPSTEYIEP CIILIRLIRT MNVEQIAELE NKLSDPIYHL QGNKLPTEYK KSYDKTTWDI
FFNAVVSAGT GPALISIKNM IKNGQLKDTQ AAMIISKIPK TALTPTSEYV NKFFELITDE
QVTKQRFLNT SALLAFAELV RYTQSNRSIH YPVHSFGHMV SKQDNALLET YIPYMANQLT
EAIKDGDSRR IQTYIMALGN FGHPKVLSVF EPYLEGTLPA STFQRLMMVV SLNRLSENFP
RLARSVAFKI YMNIMEAYEL RCAAVYVVMK TNPPLVMLQR MAEFTNQDQD RHVNSVIKTN
IDALANLEQP EFQDLAAKAR IARELLNPHI DTESYSQGFL FKKIIPSLNM AEITILQIIG
SQDTTVPKSS YLNIYQSYGG FNLPPSRMSY EISSFRALLD MWYEMPWMIE NETQKKLIIE
ETIEKLGIKG EDPVQFEGNI FVNTLYSSQF SPLDNNTIEE TINAFKRIIS SWQRSSKNFT
SENINYLHYY DMTVAFPTES GLPFIYTLTV PKLLRINIGG GHKGSKTEHF KELTAAGYIM
VHEKVQSRIG FVTPFEHRHY VAGIDTNTRL VTPLGLSISV NTTEENKKFK LTLQPSKYIR
YGTGHSTVHF SVVPYTARNN ILDLEHDFSK QDNDTLPVHT KEPHEIHFYI SNWMFVAKSD
LIDSKASEKQ GMEAIKETVN LFCNSRGAYY RRFDGLMYFG EVRIRASYDF AKLDSDSSEA
TIPTIVNKEP DSEERKKQFL KEVGKNMNSA YGYVFDMSID QGFDVQVFTL AYSYSQIDHK
SQALFYWNVQ SVDDPKIYAE LGAIGYVKSK SISLNPEKAL EQIPNDEFKA EIRLGNNFNE
EMIKLEGNWT RTDDVKDMAM KSEIVKKCRQ DMKQGNILLP ACQKANKLIN QKDLLMMSID
TTSDILYASA NRGILWIQSL ISENYVETMN LRSSSKNTID MEIKMLPDND DAKISLRTSQ
ADVSFSLKDI IGNDSNVSMK DTFKEQLDDE SVCVLDKTHA VTFDGKVYPL KLGKCWHVMM
TIYPKRDPNN FEKTLSIPSD MRAIVMAQEM DDGSKQIKMI LGDQEVHLQK SGDCLEASVD
GETANFSDHK SHQEKDFEIY GSNETITVFS PTYEITVEYD GEHILLMISD NYLNAVRGLC
GNYDTQPNND FIIPENCILT KAEEFAATYA MTQESCQGPA PENKRKAEQS TCMSRSYRPS
DVISDREAGR SSTKNRGWGY H