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Database: UniProt
Entry: R0LGD6_ANAPL
LinkDB: R0LGD6_ANAPL
Original site: R0LGD6_ANAPL 
ID   R0LGD6_ANAPL            Unreviewed;      1827 AA.
AC   R0LGD6;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Vitellogenin-2 {ECO:0000313|EMBL:EOA99312.1};
DE   Flags: Fragment;
GN   ORFNames=Anapl_07192 {ECO:0000313|EMBL:EOA99312.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA99312.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|Proteomes:UP000296049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23749191; DOI=10.1038/ng.2657;
RA   Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA   Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA   Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA   Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA   Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA   Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA   Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA   Rao M., Pitel F., Wang J., Li N.;
RT   "The duck genome and transcriptome provide insight into an avian influenza
RT   virus reservoir species.";
RL   Nat. Genet. 45:776-783(2013).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR   EMBL; KB743342; EOA99312.1; -; Genomic_DNA.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
DR   GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 1.
DR   Gene3D; 2.20.50.20; Lipovitellin. Chain A, domain 3; 2.
DR   Gene3D; 2.20.90.10; Vitellinogen, beta-sheet shell domain; 1.
DR   Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR   InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR   InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR   InterPro; IPR015816; Vitellinogen_b-sht_N.
DR   InterPro; IPR015258; Vitellinogen_b-sht_shell.
DR   InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR   InterPro; IPR015255; Vitellinogen_open_b-sht.
DR   InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR   InterPro; IPR001747; Vitellogenin_N.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR23345:SF15; VITELLOGENIN-1-RELATED; 1.
DR   PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR   Pfam; PF09175; Vit_b-sht_shell; 1.
DR   Pfam; PF09172; Vit_open_b-sht; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM01169; DUF1943; 1.
DR   SMART; SM01170; DUF1944; 1.
DR   SMART; SM00638; LPD_N; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR   PROSITE; PS51211; VITELLOGENIN; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00557}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..1827
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012045394"
FT   DOMAIN          24..662
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000259|PROSITE:PS51211"
FT   DOMAIN          1556..1733
FT                   /note="VWFD"
FT                   /evidence="ECO:0000259|PROSITE:PS51233"
FT   REGION          936..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1319..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..959
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..980
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1166..1241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        162..188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
FT   NON_TER         1827
FT                   /evidence="ECO:0000313|EMBL:EOA99312.1"
SQ   SEQUENCE   1827 AA;  202598 MW;  8184CEBAEE78140D CRC64;
     MRGIILALVL TLVGSQKFDI DPGFSSRKSY LYSYEGFMLN GLQERSLAKA GVRLSSKLEI
     SGLSENTYLL KVRSPQVEEY NGVWPRDPFT RSSKITQMVS SCFSRPFKFE YSTGRIGNIY
     APEDCPDTCV NIVRGILNMM QITIKKSQNV YELQESGIGG VCHTRYVIQE DRKNSRVSVT
     KTVDQNNCQE KVKKSVGMAY IYPCPVDTMK ERLVKGTAAF SYKLKQLDSG TLITEVASQQ
     VYQISPFSEP TGVAVMEARQ QLTLLEVRSE RGSAPDIPMQ SYGSLRYQFP DALPQMPLQL
     VKTKNPEQRI VETLQHIVLN NQQDFHDDVP QRFLELVQLC RIASADTLES IWRQVSDKPR
     YRRWLLSAVS ASGTTEALQF IKTRIRNDEL NYIQTLLTVS LAFHLMKVDE HTLPIAADLM
     TSSRIQRSPM LQQVACLGYS SVVNRYCSQT SACPKEALQP VHDLADEAIS KGREDKMKLA
     LKCIGNMGEP ASLKRILKFL PISSSSASDI PTHIQIDAIM ALRKIAWKDP RTVQGYLIQI
     LADQSLLPEV RMMACAVIFE TRPALPLITT IANVVMKESN LQVASFVYSH MKALSKSRLP
     YMYNISSACN IALKLLAPKL DRLSYRYSKV IRVGGYFDNY RVGVAGDVFV MNSPGTMFPS
     AIISKLMANS AGSVADLVEV GVRVEGLTDV ITKRNIPFAE YPTYKKIKEL GKTLLGWKEL
     PTETPLISAY LKIFGQEVAY VNINKEVLQQ AMKTIVEPAD RNTAMKRIAN QIRNGISGQW
     TQPVWMGELR YIVPSCLGLP LEYGSYTTAL ARAAANVDGK MTPPLTGDFR PSQLLESTMQ
     IRSDINPSLY VHTVATMGVN TEYFQHAVEI QGKVQMRVPM KFDAKIDMKL KNIKIETNPC
     REETEILVGR HKAFAVSRNI GELGVEKKTS ILPGDSSSNI VEEPFNPTEG ASRESFTMQG
     PDSIPRKHSH DSQEDLLHGT RRKTHKRDIC IKLHRLGCQL CFFRRSRDAS FIKNTYLHRL
     IGEHEAKIVL MPVQTDADID KIQLEIQAGS RAASKIIHEV NSESEEEDET SPYEDIQAKL
     KKILGIDNVF KVANKTRHQK KRPSKKENTM LTELGTDPNA KTPSSSSSAS SALSSSSSSA
     SSPDHRKPMD EDDNDQVKQT RNRDTSRKSS SSSGSGRNSK SSSSSSKHSS SSSSSSKSSS
     SSSSSSRSSS SSKSSSSSSS KSSSSSSKGS SSSTSSSSSK SVNHHSHRHH SRYLNGSSSS
     SSSSSSSKSV SHHSHGHHSG HLEDGGSSSS SSVYSKIWGG HEIYQYRFRS AHRQEFPKRK
     LPADQYSSTY SSTRSSRDTS RAASWPKFLG DVKTPVLAVF LNGVSNNKKT GGLQLVVYAD
     IDSIRPRMQV FVSNLTDSSK WKLCADASVL NAHKAVGYLK WGRNCQDYKV STELVTGRFA
     GHPAVQVKLE WPKVPSSVRS MAEWFYNFVP GAAFMLGFSE RMDKNPSRQA RLVVALTSPR
     TCDVVIKLPD MILYEKAMRL PLPLPVGPRI PASELQPPIW NVFAEAPSAV LENLKARCSV
     SHNKITTFNE VRFNYTMPAN CYHILAQDCS PDLKFLVMMR NAEEAMNLKA INIKLGSHEI
     DMHPANGQLK LLVDGVESPS TNVSLISAGA SLGIHSEKQG LVLVAPAYGI DRLYFDGHTF
     MIQVALWMAG KTCGMCGKYD AECEQEYRMP NGYLAKDAVT FGHSWILEET PCKGACKLHR
     SFVKLEKTVQ LAGIESKCYS TEPVLRCRKG CSVTQTTPVT VGFHCLPADS ATSMTDKQMK
     FDQKSEDMQD TVDAHTACSC ENEECST
//
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