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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
 
 
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