ID VIT_PENME Reviewed; 2586 AA. AC Q6RG02; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 02-SEP-2026, entry version 64. DE RecName: Full=Vitellogenin; DE Contains: DE RecName: Full=Vitellin; DE Flags: Precursor; OS Penaeus merguiensis (Banana prawn) (Fenneropenaeus merguiensis). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Communostraca; OC Malacostraca; Eumalacostraca; Stomatocarida; Decapoda; Dendrobranchiata; OC Penaeoidea; Penaeidae; Penaeus. OX NCBI_TaxID=71412; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR88442.2} RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Ovary {ECO:0000312|EMBL:AAR88442.2}; RX PubMed=16432892; DOI=10.1002/mrd.20424; RA Phiriyangkul P., Utarabhand P.; RT "Molecular characterization of a cDNA encoding vitellogenin in the banana RT shrimp, Penaeus (Litopenaeus) merguiensis and sites of vitellogenin mRNA RT expression."; RL Mol. Reprod. Dev. 73:410-423(2006). RN [2] {ECO:0000305, ECO:0000312|EMBL:AAR88442.2} RP PROTEIN SEQUENCE OF 19-28, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP GLYCOSYLATION. RC TISSUE=Ovary {ECO:0000312|EMBL:AAR88442.2}; RX PubMed=16289995; DOI=10.1016/j.cbpb.2005.09.009; RA Auttarat J., Phiriyangkul P., Utarabhand P.; RT "Characterization of vitellin from the ovaries of the banana shrimp RT Litopenaeus merguiensis."; RL Comp. Biochem. Physiol. 143B:27-36(2006). CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of CC nutrients during embryonic development. {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in the ovary and hepatopancrease of CC vitellogenic females. Not expressed in the muscle, heart and intestine CC of female or in the hepatopancrease of the male. Detected in the ovary CC and hemolymph of female (at protein level). Not detected in the female CC hepatopancreas or in the male hemolymph and testis (at protein level). CC {ECO:0000269|PubMed:16289995, ECO:0000269|PubMed:16432892}. CC -!- DEVELOPMENTAL STAGE: Vitellogenin is detected in stage 1 of the ovarian CC cycle and protein levels increase to reach a maximum in stage 3. CC Thereafter vitellogen levels in the ovary decrease gradually. Vitellin CC is detected at low levels in stage 1 of the ovarian cycle and protein CC levels increase steadily in stages 2 through to 4. CC {ECO:0000269|PubMed:16289995}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16289995}. CC -!- PTM: May be modified covalently by lipidation. CC {ECO:0000269|PubMed:16289995}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY499620; AAR88442.2; -; mRNA. DR AlphaFoldDB; Q6RG02; -. DR SMR; Q6RG02; -. DR GO; GO:0005319; F:lipid carrier activity; IEA:InterPro. DR GO; GO:0019915; P:lipid storage; IDA:UniProtKB. DR GO; GO:0006869; P:lipid transport; IEA:InterPro. DR GO; GO:0048477; P:oogenesis; IEP:UniProtKB. DR FunFam; 2.20.50.20:FF:000007; von Willebrand factor type D domaincontaining protein; 1. DR Gene3D; 2.30.230.10; Lipovitellin, beta-sheet shell regions, chain A; 1. 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; 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; IPR015255; Vitellinogen_open_b-sht. DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1. DR InterPro; IPR050733; Vitellogenin/Apolipophorin. DR InterPro; IPR001747; Vitellogenin_M. DR InterPro; IPR063611; Vitellogenin_N. DR InterPro; IPR001846; VWF_type-D. DR PANTHER; PTHR23345:SF15; VITELLOGENIN 1-RELATED; 1. DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1. DR Pfam; PF01347; TPR_Vitellogenin; 1. DR Pfam; PF09172; Vit_open_b-sht; 1. DR Pfam; PF29934; Vitellogenin_N; 1. DR Pfam; PF00094; VWD; 1. DR SMART; SM01169; DUF1943; 1. DR SMART; SM00638; LPD_N; 1. DR SUPFAM; SSF56968; Lipovitellin-phosvitin complex, beta-sheet shell regions; 2. DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1. DR PROSITE; PS51211; VITELLOGENIN; 1. DR PROSITE; PS51233; VWFD; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid transport; KW Lipid-binding; Lipoprotein; Signal; Storage protein; Transport. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:16289995" FT CHAIN 19..2586 FT /note="Vitellogenin" FT /evidence="ECO:0000269|PubMed:16289995" FT /id="PRO_0000259413" FT CHAIN 19..? FT /note="Vitellin" FT /evidence="ECO:0000269|PubMed:16289995" FT /id="PRO_0000259414" FT DOMAIN 42..653 FT /note="Vitellogenin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557" FT DOMAIN 2353..2516 FT /note="VWFD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 170..194 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557, FT ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 2378..2515 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" SQ SEQUENCE 2586 AA; 283029 MW; E68C3991C9783F06 CRC64; MTTSTLLFVL AFVAGGLAAP WGADVPRCST ECPVTGSPKL AYQPDKTYAY AYSGKSTVQL KGVDNGDTET EWTAGVDLTW ISPCDMAISF RNTKMDGARG PTAARTLERY PLVVAVVDGR VQHVCAHPED EAWAINLKKG VASAFQNSIP SLSAVSSGIT VTETDVVGKC PTKYEIETEG EKVIVVKEKN HRHCQERYPT PAALPAPWLK APLPIEESKS QCRQEIANGI YTAITCQDKN IVRPAIGIYK YVEASQYSTL RFISESSDTS AISGIPSGEL NIESLLYNHE TMKDPQLAPE LDELMKEICD KTKDTVEAEA GALVAKALHV LRRIPDTVVV ETAQKVRQGH YCSDSARLES IFLDAVAFIH ESGAVKVMVN EIENGRATGG RLALYTAALY LIPRPNIEAV KALTPLFESP RPMPSLLLAA ATMVNHYCRH TPACYEKAPV ARIAEILANR VQTHCSPSAG VEDNEVALAI FKTIGNMGVA TPAVTRAAVH CIEVEGLETS VRVAAAEAFR QANCFRPAVE KLVDIAVRPA FETEVRIASY LAAVRCAEQE HLETIIEKIS KEENTQVRGF VLGHLINIQE STCPAKENLR YLLANVIPTD FERDFRKFSR NIDVAYHAPA FGMGAGLESN IIYAPGSFVP RAVNLKMKAD VDETHMDIAE IGARFVGIES IIEEPLGPQG YLRTATFGKI MEDITGFAGE KGYKVMEQLK HTLRTRRSID SSVIADFFGK LYGKSRSHTH AELFARFMGH EITYADVAGS LKGVTADTLI ETFFSFFENS LEHMKDLNLN TARTAQLSMD YSLPTIQGTP LRLRLAGTAV AGLKMEGNVN IAQILSDLGN SQTGVKFFPG LSVHATGFVG FDWLLARVGI EMQNTISSAT GAAIKIRTTE NKKIEMELEV PEKMELLNIK AETYLVKAVG KKMTEISPSS MRDVRIQRNS CIGALEPVFG LKVCYDMNIP DVFRANALPL GEPAIAKLYV EKADPSMRGY LVTAAIKNKR GNKVIKMNVE AAGASTPRRA EMTLSYTKEE GSHIVSAKLD SSSIAAGVWT TLTNEQGHKA METYVNFNYG QIAISRGIKL EAIAREASVG EEFQVNVFSS GTRSFPSESH IVEARFIKKT SGPEFNVDVI CRTKNALAEL FDLNIEVGAD FMKFSPKNLY PARYIPKTRI VLPVNLRKME INAATAAWKL ISYIRAGSQS GGSREFISAL KLAKGRKDFI SVQATHTIEG TFPQNIIIKN VATAEVGRSS YKAMYDLFYH SEKMGASLEV LQAAGNEKVA HLEAIYELSG SKYCTKFLAE IPGYIQPVKV EAGIEQGAEG RYTLESAITY GQRTVLEASG PIMARFSSKI AKLQANIKVR AMASEPYIIG ANVAFGSKKQ MIAMEIKGRS EAVIGLEWKM VRESSEKTTV GIVFVLPALI ENKIDAEITD GLIHVSFNNL VLPKTSSRRR VKGFADVHIA EKKANVEFSW DADNAPEKKL VLDASLISSS ANPGHAEIHG NIVIAGEPFH AKLVLTAANL VEHMEGENGF KLILTTPSQK TIVLGASCDV QVAGATTKVI STVEYKNMKD RKYKYASVIA YEKLGGPFDY AVEAKVTYKQ PGTAEIKLGT AVKHHWTPEE HVVAVRVEAD APILKTPATI EFSIHNAPNA FVGFCKIERN APATVFEWNV QITPEGGIEA VEAGVDMKAI IEVLKIVHAA ATLQEESYET YGPHTSQYQY RFTRPSPTSY TMQMRTPTRT MEGRAKLSPR ESGIKFYPNK GKTESKYEIG YKANHEGRWG GHASKLEVRM NHPVLPKPIM AAVQYTVAEE TTKGTIELDI FPEEANKITG SLETQRISEN AIRAEAFLTS RMLKVNPKAI ITAAYAPETV AFDVVFHKTP SAAPIFAIAA KYDKTAAHNA AATFTVKMEE RPVFEITAVT EPEEAATCNG IRMRAVAYAA TFGKYNVISK MCRPAFIEVT AMRPGGAKEY IAKLGLRYPD AAEAGVYVAS GRAGETHGVA VAAVKLASPT MLKVEMAYEP QEAEAIINEM TEEFEKIAAS FTSVEMEVVE FLKQEAAAKG IQFPSSQLVN LLGVAKEEIA EIYRDIVSEA IIFDTEILGD ILGSPVVSFI SRVYFGVWSE IIHLQHHLSV SLIQTIERFQ QELGSISEIL MEVVMTAARM AETGEVPGVV FDALEEIKAT KVFRIVRREV DAILEEYPEE YEAVKHIVHN VVAILKRDVG IVRERLMEIP AVLKIIDYTM YHFHSERAFA AEAEKLVSLM LNELLFVSME REGNGVAVRI PLHRPLYSLT QVAQEAVPNP VTMLENLIFA YVDYIPIPVS DAIWAFYNLV PRYITDVLPP YPRTATVVGG SEILTFSGLV VRAPRSPCKV VLAAHGSHRL MMSHPQASAP AQFELKTPAA TVMIKPDFEV VVNGQPLAGS QQTIGNVRIV NTAEHIEVGC PLMKVVVAKA GEAVAVEASG WVFGRVAGLL GPNNGEIAHD RLMPSGAAAS NPRDLVAAWQ EDRQCSTPEV PRAETTVARL IQCEALLGIR SRCNPVVHPQ PFIKMCHAAH KACDAAQAYR TVCSLRGVGE VFPLGC //