VIT2_SOLIN
ID VIT2_SOLIN Reviewed; 1807 AA.
AC Q2VQM6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Vitellogenin-2 {ECO:0000312|EMBL:AAY22960.1};
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:AAY22960.1}
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; AY941795; AAY22960.1; -; mRNA.
DR RefSeq; NP_001291513.1; NM_001304584.1.
DR AlphaFoldDB; Q2VQM6; -.
DR EnsemblMetazoa; NM_001304584.1; NP_001291513.1; LOC105205782.
DR GeneID; 105205782; -.
DR KEGG; soc:105205782; -.
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; 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..1807
FT /note="Vitellogenin-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378060"
FT DOMAIN 24..819
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1448..1636
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 334..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 180..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1450..1599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1472..1635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1807 AA; 204975 MW; EEEAFDAF920730C0 CRC64;
MWFPVTLLFL AGVAVATNNH EHAWETGNEY QYSVFGRTLA GVDKLKRQYT GIQYNGILTI
QVKSPELLQA KFDNQHYAHI HQELSNGPDD FDDPKNVNYK RMPMSEKPFE IKLKHGIIRD
LLFDRDVPTW EVNMMKAIVG QLQVDTQGEN AINSKSIQVP SDESFAATFK AMEDSVSGKC
EVLYEITPLT VNEIQAKQDR IPMPSLHSDG NHYEVKKLKN YERCQERQLY HYGFDIKSAG
KKWAGQDKVI SQLSVTEMVI SGDLKRFTIQ STEMKNEIAV QPETSDSPIG NVYTITRLTL
KKKNSISNSW FGPHEISNLE STGNLVYTFN NPFSDSDNRR VRHHSVSQNS EQENSSESSK
SSSQSSSSSS SASSSSSSSS SSSSSSSSSS SSSSSSSSEE ENENVVQTKA ALQNIFLAPN
IPLLPYFIGY KGKTILKSDK QNVMQFAKNL ISEIAEEVQI TSEGYEATME KYTILKKLLR
TMNRKQYAEL EQYVLQFNKG SDSRANAWTT FRDAVLHAGT GPAYVTIENW IKSGQVKGAE
AARLLSQLPK NVYLPTPNYV QAFFELIKSP MVTQQEYVNV SAPIALAELL RNSYIGQNYY
PIYSFGFITL KKNDEVVGKY INYLANQLQQ GYQENNSRKI QTYIFALGVT AHPKIISVFE
PYLEHSLPAS TYQRTLMVAA LSDLAKVQPK LVGPIFYKLY LNENEAHEVR AMAVHEFILT
DPPMITLQRI AKNTNYDTSK QVNAVVKSTL ESLVHTKRSE WRHLANKARN VRYLVTSNNY
GNWHSSGYHL DFQDWLVNGL SLQTIAGDDL IPKYVYVGVN SVFDFLDQPS VEAGYGLSSH
RQFFNEISKQ WYSHQADDER RRSRVEKLAQ ALQIKAKEQN NLEGHFLFNS VYDSAFYPYD
RHRIREAVAA LKQFLNGNNK LEGSAFNNYE NIMSFANEDG LPFVYTLDAP TFTKAKVNFK
QGGRTANSGT FQALIANNVQ QQFGFVALFE HQKYIAGINN NRVLRVPVEY DVEFNSNNAK
NFALKIRPQN LPRMGNELKL LHYSVVPFTT QQDLLDLKPT SNDKNTRPVF TSPVYKTTVQ
KDTFSIKVES DSIGKESDTE SFVADVLRLT NANDDHYTKI STILTSDQIQ KSEGHITMTY
DTVTIGGNND NSGQSSEEME SLHSISWKSN SKERRKQIAN NLSKGIKSGE VYIFDVSYSV
PMLHENEYVF TFGGMKSNSN QKLRGYFYWN SHAPQEVNYE VCFSHEMQYA PRATPLNFKY
ALKNSPRDEY KAVLKYGKTC ATGNKVVITG SSSQSQQLRD IIENSSLPNN VWKRFQTGNK
AVENCMKAND IAQMRDQIDV QFDLSNIVPE SVRRYAKKII EYLEKYVYKV CDNVSREEES
EENTIKNTLL FASPVNRMWP NWLPQSVSDI TSGWSPSFNS FGPSSESQWQ TMRLNVADYP
DEFESEKQSC TLDKDKVYTF DNQLYNVHLG KCKHVLLTTY PQDFHNRRNY IPENSKVAIL
AEDADNDSRN VYIWLGKQEI KLKKAGNNVQ AVVNGQNVEI SDKGYQKING NEITFEILSL
PDDSLSVVSE KYGINAVYDG KRVVISASDA YRNAVRGLCG NFDSRPNTDF VTPKNCLLTK
PEEFAATYAM TQENCQGPAP ENKRRAEQST CHEFPENEQM NVISDREAGR MMTEGVNWGY
HQANRNKEHG RGNKSHQNNK KQYQANSQES GSSESRNDKK KHNIVYRTRV VEEGDEICFT
TTPLPACRQG ARPTERYPKK ADLYCMPRND QSLDLKRRVE DGANPDFTRK SVSRMQVFQV
PVSCSAA
