VIT1_PERAM
ID VIT1_PERAM Reviewed; 1896 AA.
AC Q9U8M0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Vitellogenin-1;
DE Short=Vg-1;
DE Flags: Precursor;
GN Name=VG2; Synonyms=VG;
OS Periplaneta americana (American cockroach) (Blatta americana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Blattidae;
OC Blattinae; Periplaneta.
OX NCBI_TaxID=6978;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body;
RX PubMed=11015122;
RX DOI=10.1002/1520-6327(200009)45:1<37::aid-arch4>3.0.co;2-8;
RA Tufail M., Lee J.M., Hatakeyama M., Oishi K., Takeda M.;
RT "Cloning of vitellogenin cDNA of the American cockroach, Periplaneta
RT americana (Dictyoptera), and its structural and expression analyses.";
RL Arch. Insect Biochem. Physiol. 45:37-46(2000).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; AB034804; BAA86656.1; -; mRNA.
DR AlphaFoldDB; Q9U8M0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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..1896
FT /note="Vitellogenin-1"
FT /id="PRO_0000041550"
FT DOMAIN 20..835
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1512..1705
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 325..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1514..1667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1896 AA; 212728 MW; 4B80FBC9788372C5 CRC64;
MWKGFLCCLL VAGVTSLQEW DPNRQYVYKV ESRAFTALHQ ISNQYAGILM RAKLIIQPKT
REELHAQLVE VEHSQINKEL PSGWDQEIEI HDWQQLSALK DAFAIILQNG HIVNVKVKDS
TPNWAVNILK GILSTLQVNT QADNLVRHRY NILPNASTDS AVYSIRETTI TGECEVEYDV
SPLPALPLLQ HPELAPLSNV NDNVIDIEKT QNFSNCKRRP AVHYGLAGIP DLEPGQNQMG
DFLARSSVSR VVISGTLNKF TVQSSVTTNQ VVMSPEMYNS QKGLIVSRVN VTIKDIEEAR
PIPLPGNLQD TGDLLYSYNN AHDIEPLQRD RQDSDFTLES DSSSSSSSSS SDENSWSRDS
HSRISEENKK AQIKQQRIKA NRHSDDDVTN DEISFASRER QRRSRTRRSI RNDDSSSSSS
SSEEDYQPRP LRGQPPNIPL LPFFVGNRGN AAFLLSSDDP AEIVKSLAEE IKSDMKKPAY
IPERSTHAKL MMMRDIVRTM TAKQLQKATS LIHSESKHDL GWIAYRDMVS ESGTHPALEE
LSIWIISKKL SSEEGAELLA TLPRAVIMPT PEYFEAFNKL VMDKRVRNQP IVNSTGLLAL
ATLHRQVHDA EFSHNNYPVH AFGRMVPRNY NATNDFIDYL GKQLHAAMAD GNRPKIQVII
RALGNTGNKR ILNYLEPYLE RKKNATEFER LLMVTSLDIL AEINPELARQ VLYNVYINIG
ENHELRCASV ILLMRTQPPA AMLQRMAEFS NIDPVKQVVS AVQSAIRSAA NLKEPGNLNL
ARAARSAVNI LNPMSMDIAY SNDILSSNMI QDMDLGYKDN MAHVGSSDSI IPNTILRKFN
RYAGGQAHSD INFSEMVSSV KQLLKALRNP LKQREDPLLR REPVADRREF NIPPIIIDIA
PPLEGNMMLR WLGNDRFFSY DKNDIKQLFR NYNAAALPLA DMHMLDDMKV YNQKSLAIAF
PNALGLPSLF TIDVPTVLRA NSTFRLLLNN TSSESSSIEV LPWKLGARSE TSLTYSVKEM
SKIAIVTPFN SMEHMAALER NILINIPIKL DVDFDLEAQN IALNMKLIGK DSNPRLAQLS
TNTYTTNHKI TIIKPAIQDE EANEIHVRPA RMMRDTFGKL QTGIALNLEI ETEDEFLDME
FVRQELQGRD FTSALAFIWA RRTINNHNVT LSIDEDQSTT NAVRIEGKYA SKINDVDAGT
WTEWRSSRVE RSAKRHHRPR PEAQEYDSSA NPAIVDRADK LEEFLNRASG NRVHGLAVRV
AFTGSSDATF DLTAALGLSN VNGSARALVS YISQPAHPAD VMPRKTEYDL FAALSMPAPP
IINFNQALEF DPDSNLDAGL SIFTNDKPSG NLRIKGELQQ SEERRNAIRS TPAALACMRE
MANGNNNLLP SCRNATEMAN RLDRIRLQAK FENLSDDLIN NTYKAYTWIR YFTQPYVTEN
IAQEQNPGRL NINVDVNNDG TALNASVDTA LMSITWTNIR LNRWTRSLVE PSPQDTALDR
LAREALPLYY EPTCVLDVSQ AATFDNTTYP LTLSSAWHMM LQYQPKRSQD DENLDDVPDI
IRPPVAILAR ETSNRRKEIL MNLDHTIVAF KPTSEVNVEV NGRILIIEQS RTTDIMAEGN
LVLQIHRLPS RAVYMVAPQH KLLMIHDGKR VLLQASNGYR DEVRGLCGTF DGEPTTDFTT
PSNCILNDPK AFINSYRLGG DREDNAWMLN YRAQPCVSRN FTSTDIIGKH MPRNPASRGF
ELPHPVNDTS SSSSSSSESS SSSSSSSSES ASNSDLHNNS TSSSSSSSSS SSESAEGAPE
KSSRKTSPPQ TSTLHRTMVV EEVTEICFSM RPLPECAPRF KPADTLKKKI KFHCLTKGPT
ASHWLKMVKK GVNPDFSKKR EHKQLEVDIP AKCVRH
