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Q6RG02 (VIT_FENME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitellogenin

Cleaved into the following chain:

  1. Vitellin
OrganismFenneropenaeus merguiensis (Banana prawn) (Penaeus merguiensis)
Taxonomic identifier71412 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Dendrobranchiata › Penaeoidea › Penaeidae › Fenneropenaeus

Protein attributes

Sequence length2586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Precursor of the egg-yolk proteins that are sources of nutrients during embryonic development.

Tissue specificity

Expressed in the ovary and hepatopancrease of vitellogenic females. Not expressed in the muscle, heart and intestine of female or in the hepatopancrease of the male. Detected in the ovary and hemolymph of female (at protein level). Not detected in the female hepatopancreas or in the male hemolymph and testis (at protein level). Ref.1 Ref.2

Developmental stage

Vitellogenin is detected in stage 1 of the ovarian cycle and protein levels increase to reach a maximum in stage 3. Thereafter vitellogen levels in the ovary decrease gradually. Vitellin is detected at low levels in stage 1 of the ovarian cycle and protein levels increase steadily in stages 2 through to 4. Ref.2

Post-translational modification

Glycosylated. Ref.2

May be modified covalently by lipidation. Ref.2

Sequence similarities

Contains 1 vitellogenin domain.

Contains 1 VWFD domain.

Ontologies

Keywords
   Biological processLipid transport
Transport
   DomainSignal
   LigandLipid-binding
   Molecular functionStorage protein
   PTMDisulfide bond
Glycoprotein
Lipoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoogenesis

Inferred from expression pattern Ref.2. Source: UniProtKB

   Molecular functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid transporter activity

Inferred from direct assay Ref.2. Source: UniProtKB

nutrient reservoir activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 25862568Vitellogenin Ref.2
PRO_0000259413
Chain19 – ?Vitellin Ref.2PRO_0000259414

Regions

Domain42 – 653612Vitellogenin
Domain2354 – 2546193VWFD

Amino acid modifications

Disulfide bond170 ↔ 194 Potential

Sequences

Sequence LengthMass (Da)Tools
Q6RG02 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: E68C3991C9783F06

FASTA2,586283,029
        10         20         30         40         50         60 
MTTSTLLFVL AFVAGGLAAP WGADVPRCST ECPVTGSPKL AYQPDKTYAY AYSGKSTVQL 

        70         80         90        100        110        120 
KGVDNGDTET EWTAGVDLTW ISPCDMAISF RNTKMDGARG PTAARTLERY PLVVAVVDGR 

       130        140        150        160        170        180 
VQHVCAHPED EAWAINLKKG VASAFQNSIP SLSAVSSGIT VTETDVVGKC PTKYEIETEG 

       190        200        210        220        230        240 
EKVIVVKEKN HRHCQERYPT PAALPAPWLK APLPIEESKS QCRQEIANGI YTAITCQDKN 

       250        260        270        280        290        300 
IVRPAIGIYK YVEASQYSTL RFISESSDTS AISGIPSGEL NIESLLYNHE TMKDPQLAPE 

       310        320        330        340        350        360 
LDELMKEICD KTKDTVEAEA GALVAKALHV LRRIPDTVVV ETAQKVRQGH YCSDSARLES 

       370        380        390        400        410        420 
IFLDAVAFIH ESGAVKVMVN EIENGRATGG RLALYTAALY LIPRPNIEAV KALTPLFESP 

       430        440        450        460        470        480 
RPMPSLLLAA ATMVNHYCRH TPACYEKAPV ARIAEILANR VQTHCSPSAG VEDNEVALAI 

       490        500        510        520        530        540 
FKTIGNMGVA TPAVTRAAVH CIEVEGLETS VRVAAAEAFR QANCFRPAVE KLVDIAVRPA 

       550        560        570        580        590        600 
FETEVRIASY LAAVRCAEQE HLETIIEKIS KEENTQVRGF VLGHLINIQE STCPAKENLR 

       610        620        630        640        650        660 
YLLANVIPTD FERDFRKFSR NIDVAYHAPA FGMGAGLESN IIYAPGSFVP RAVNLKMKAD 

       670        680        690        700        710        720 
VDETHMDIAE IGARFVGIES IIEEPLGPQG YLRTATFGKI MEDITGFAGE KGYKVMEQLK 

       730        740        750        760        770        780 
HTLRTRRSID SSVIADFFGK LYGKSRSHTH AELFARFMGH EITYADVAGS LKGVTADTLI 

       790        800        810        820        830        840 
ETFFSFFENS LEHMKDLNLN TARTAQLSMD YSLPTIQGTP LRLRLAGTAV AGLKMEGNVN 

       850        860        870        880        890        900 
IAQILSDLGN SQTGVKFFPG LSVHATGFVG FDWLLARVGI EMQNTISSAT GAAIKIRTTE 

       910        920        930        940        950        960 
NKKIEMELEV PEKMELLNIK AETYLVKAVG KKMTEISPSS MRDVRIQRNS CIGALEPVFG 

       970        980        990       1000       1010       1020 
LKVCYDMNIP DVFRANALPL GEPAIAKLYV EKADPSMRGY LVTAAIKNKR GNKVIKMNVE 

      1030       1040       1050       1060       1070       1080 
AAGASTPRRA EMTLSYTKEE GSHIVSAKLD SSSIAAGVWT TLTNEQGHKA METYVNFNYG 

      1090       1100       1110       1120       1130       1140 
QIAISRGIKL EAIAREASVG EEFQVNVFSS GTRSFPSESH IVEARFIKKT SGPEFNVDVI 

      1150       1160       1170       1180       1190       1200 
CRTKNALAEL FDLNIEVGAD FMKFSPKNLY PARYIPKTRI VLPVNLRKME INAATAAWKL 

      1210       1220       1230       1240       1250       1260 
ISYIRAGSQS GGSREFISAL KLAKGRKDFI SVQATHTIEG TFPQNIIIKN VATAEVGRSS 

      1270       1280       1290       1300       1310       1320 
YKAMYDLFYH SEKMGASLEV LQAAGNEKVA HLEAIYELSG SKYCTKFLAE IPGYIQPVKV 

      1330       1340       1350       1360       1370       1380 
EAGIEQGAEG RYTLESAITY GQRTVLEASG PIMARFSSKI AKLQANIKVR AMASEPYIIG 

      1390       1400       1410       1420       1430       1440 
ANVAFGSKKQ MIAMEIKGRS EAVIGLEWKM VRESSEKTTV GIVFVLPALI ENKIDAEITD 

      1450       1460       1470       1480       1490       1500 
GLIHVSFNNL VLPKTSSRRR VKGFADVHIA EKKANVEFSW DADNAPEKKL VLDASLISSS 

      1510       1520       1530       1540       1550       1560 
ANPGHAEIHG NIVIAGEPFH AKLVLTAANL VEHMEGENGF KLILTTPSQK TIVLGASCDV 

      1570       1580       1590       1600       1610       1620 
QVAGATTKVI STVEYKNMKD RKYKYASVIA YEKLGGPFDY AVEAKVTYKQ PGTAEIKLGT 

      1630       1640       1650       1660       1670       1680 
AVKHHWTPEE HVVAVRVEAD APILKTPATI EFSIHNAPNA FVGFCKIERN APATVFEWNV 

      1690       1700       1710       1720       1730       1740 
QITPEGGIEA VEAGVDMKAI IEVLKIVHAA ATLQEESYET YGPHTSQYQY RFTRPSPTSY 

      1750       1760       1770       1780       1790       1800 
TMQMRTPTRT MEGRAKLSPR ESGIKFYPNK GKTESKYEIG YKANHEGRWG GHASKLEVRM 

      1810       1820       1830       1840       1850       1860 
NHPVLPKPIM AAVQYTVAEE TTKGTIELDI FPEEANKITG SLETQRISEN AIRAEAFLTS 

      1870       1880       1890       1900       1910       1920 
RMLKVNPKAI ITAAYAPETV AFDVVFHKTP SAAPIFAIAA KYDKTAAHNA AATFTVKMEE 

      1930       1940       1950       1960       1970       1980 
RPVFEITAVT EPEEAATCNG IRMRAVAYAA TFGKYNVISK MCRPAFIEVT AMRPGGAKEY 

      1990       2000       2010       2020       2030       2040 
IAKLGLRYPD AAEAGVYVAS GRAGETHGVA VAAVKLASPT MLKVEMAYEP QEAEAIINEM 

      2050       2060       2070       2080       2090       2100 
TEEFEKIAAS FTSVEMEVVE FLKQEAAAKG IQFPSSQLVN LLGVAKEEIA EIYRDIVSEA 

      2110       2120       2130       2140       2150       2160 
IIFDTEILGD ILGSPVVSFI SRVYFGVWSE IIHLQHHLSV SLIQTIERFQ QELGSISEIL 

      2170       2180       2190       2200       2210       2220 
MEVVMTAARM AETGEVPGVV FDALEEIKAT KVFRIVRREV DAILEEYPEE YEAVKHIVHN 

      2230       2240       2250       2260       2270       2280 
VVAILKRDVG IVRERLMEIP AVLKIIDYTM YHFHSERAFA AEAEKLVSLM LNELLFVSME 

      2290       2300       2310       2320       2330       2340 
REGNGVAVRI PLHRPLYSLT QVAQEAVPNP VTMLENLIFA YVDYIPIPVS DAIWAFYNLV 

      2350       2360       2370       2380       2390       2400 
PRYITDVLPP YPRTATVVGG SEILTFSGLV VRAPRSPCKV VLAAHGSHRL MMSHPQASAP 

      2410       2420       2430       2440       2450       2460 
AQFELKTPAA TVMIKPDFEV VVNGQPLAGS QQTIGNVRIV NTAEHIEVGC PLMKVVVAKA 

      2470       2480       2490       2500       2510       2520 
GEAVAVEASG WVFGRVAGLL GPNNGEIAHD RLMPSGAAAS NPRDLVAAWQ EDRQCSTPEV 

      2530       2540       2550       2560       2570       2580 
PRAETTVARL IQCEALLGIR SRCNPVVHPQ PFIKMCHAAH KACDAAQAYR TVCSLRGVGE 


VFPLGC

« Hide

References

[1]"Molecular characterization of a cDNA encoding vitellogenin in the banana shrimp, Penaeus (Litopenaeus) merguiensis and sites of vitellogenin mRNA expression."
Phiriyangkul P., Utarabhand P.
Mol. Reprod. Dev. 73:410-423(2006) [PubMed: 16432892] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Ovary.
[2]"Characterization of vitellin from the ovaries of the banana shrimp Litopenaeus merguiensis."
Auttarat J., Phiriyangkul P., Utarabhand P.
Comp. Biochem. Physiol. 143B:27-36(2006) [PubMed: 16289995] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-28, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY499620 mRNA. Translation: AAR88442.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3DG3DSA:2.30.230.10. Vitellinogen_b-sht_N. 1 hit.
G3DSA:2.20.50.20. Vitellinogen_open_b-sht_sub1. 2 hits.
G3DSA:2.20.80.10. Vitellinogen_open_b-sht_sub2. 1 hit.
G3DSA:1.25.10.20. Vitellinogen_superhlx. 1 hit.
InterProIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR009454. Lipid_transpt_open_b-sht.
IPR015816. Vitellinogen_b-sht_N.
IPR015255. Vitellinogen_open_b-sht.
IPR015817. Vitellinogen_open_b-sht_sub1.
IPR015818. Vitellinogen_open_b-sht_sub2.
IPR011030. Vitellinogen_superhlx.
IPR001846. VWF_type-D.
[Graphical view]
PfamPF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTSM00638. LPD_N. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMSSF56968. Lipid_transp_b-sht_shell. 2 hits.
SSF48431. LV_superhelical. 1 hit.
PROSITEPS51211. VITELLOGENIN. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIT_FENME
AccessionPrimary (citable) accession number: Q6RG02
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 10, 2005
Last modified: April 18, 2012
This is version 33 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents