VIT6_CAEEL
ID VIT6_CAEEL Reviewed; 1651 AA.
AC P18948; O45176; Q7KPP7; Q7YXH2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 5.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Vitellogenin-6;
DE Flags: Precursor;
GN Name=vit-6; ORFNames=K07H8.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=1904098; DOI=10.1007/bf02101283;
RA Spieth J., Nettleton M., Zucker-Aprison E., Lea K., Blumenthal T.;
RT "Vitellogenin motifs conserved in nematodes and vertebrates.";
RL J. Mol. Evol. 32:429-438(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-259.
RX PubMed=3841791; DOI=10.1128/mcb.5.10.2495-2501.1985;
RA Spieth J., Blumenthal T.;
RT "The Caenorhabditis elegans vitellogenin gene family includes a gene
RT encoding a distantly related protein.";
RL Mol. Cell. Biol. 5:2495-2501(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=4022780; DOI=10.1093/nar/13.14.5283;
RA Spieth J., Denison K., Kirtland S., Cane J., Blumenthal T.;
RT "The C. elegans vitellogenin genes: short sequence repeats in the promoter
RT regions and homology to the vertebrate genes.";
RL Nucleic Acids Res. 13:5283-5295(1985).
RN [5]
RP PROTEIN SEQUENCE OF 779-780 AND 1220-1232.
RX PubMed=10529405; DOI=10.1006/bbrc.1999.1549;
RA Nakamura A., Yasuda K., Adachi H., Sakurai Y., Ishii N., Goto S.;
RT "Vitellogenin-6 is a major carbonylated protein in aged nematode,
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 264:580-583(1999).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-252 AND ASN-1288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24957743; DOI=10.1007/s12263-014-0414-6;
RA Fischer M., Fitzenberger E., Kull R., Boll M., Wenzel U.;
RT "The zinc matrix metalloproteinase ZMP-2 increases survival of
RT Caenorhabditis elegans through interference with lipoprotein absorption.";
RL Genes Nutr. 9:414-414(2014).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development (Probable). May play a role in
CC cholesterol uptake. May be involved in thermotolerance
CC (PubMed:24957743). {ECO:0000269|PubMed:24957743, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c;
CC IsoId=P18948-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P18948-2; Sequence=VSP_020107;
CC Name=b;
CC IsoId=P18948-3; Sequence=VSP_020106;
CC -!- TISSUE SPECIFICITY: Synthesized in Caenorhabditis only by 32 cells
CC building the intestine of adult hermaphroditic individuals; they are
CC cotranslationally secreted into the body cavity and subsequently taken
CC up by the gonad.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in the
CC uptake of cholesterol analog dehydroergosterol (DHE). Simultaneous
CC RNAi-mediated knockdown of zmp-2 prevents a reduction in survival upon
CC heat stress. {ECO:0000269|PubMed:24957743}.
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DR EMBL; X56213; CAA39670.1; -; Genomic_DNA.
DR EMBL; FO081300; CCD70603.1; -; Genomic_DNA.
DR EMBL; FO081300; CCD70604.1; -; Genomic_DNA.
DR EMBL; FO081300; CCD70605.1; -; Genomic_DNA.
DR EMBL; M11499; AAA28165.1; -; Genomic_DNA.
DR EMBL; X02756; CAA26533.1; -; Genomic_DNA.
DR PIR; B43081; B43081.
DR PIR; F88750; F88750.
DR RefSeq; NP_001023274.1; NM_001028103.2. [P18948-2]
DR RefSeq; NP_001023275.1; NM_001028104.5.
DR RefSeq; NP_001023276.1; NM_001028105.3. [P18948-1]
DR AlphaFoldDB; P18948; -.
DR SMR; P18948; -.
DR BioGRID; 42732; 22.
DR IntAct; P18948; 5.
DR STRING; 6239.K07H8.6c; -.
DR iPTMnet; P18948; -.
DR World-2DPAGE; 0011:P18948; -.
DR EPD; P18948; -.
DR PaxDb; P18948; -.
DR PeptideAtlas; P18948; -.
DR EnsemblMetazoa; K07H8.6a.1; K07H8.6a.1; WBGene00006930. [P18948-2]
DR EnsemblMetazoa; K07H8.6c.1; K07H8.6c.1; WBGene00006930. [P18948-1]
DR GeneID; 177619; -.
DR KEGG; cel:CELE_K07H8.6; -.
DR UCSC; K07H8.6b; c. elegans. [P18948-1]
DR CTD; 177619; -.
DR WormBase; K07H8.6a; CE28594; WBGene00006930; vit-6. [P18948-2]
DR WormBase; K07H8.6b; CE34921; WBGene00006930; vit-6. [P18948-3]
DR WormBase; K07H8.6c; CE18026; WBGene00006930; vit-6. [P18948-1]
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; P18948; -.
DR OMA; KLYYDGH; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P18948; -.
DR PRO; PR:P18948; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006930; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR GO; GO:1904807; P:negative regulation of protein oxidation; IGI:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IGI:UniProtKB.
DR GO; GO:1904109; P:positive regulation of cholesterol import; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1651
FT /note="Vitellogenin-6"
FT /id="PRO_0000041537"
FT DOMAIN 34..716
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1340..1515
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1527..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633"
FT CARBOHYD 1288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT DISULFID 1342..1479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1364..1514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT VAR_SEQ 188..1637
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020106"
FT VAR_SEQ 1591
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020107"
FT CONFLICT 23
FT /note="N -> F (in Ref. 1; CAA39670, 3; AAA28165 and 4;
FT CAA26533)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="E -> K (in Ref. 1; CAA39670 and 3; AAA28165)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="F -> L (in Ref. 1; CAA39670 and 3; AAA28165)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> P (in Ref. 1; CAA39670)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="A -> R (in Ref. 1; CAA39670)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="N -> D (in Ref. 1; CAA39670)"
FT /evidence="ECO:0000305"
FT CONFLICT 1623..1624
FT /note="KL -> NV (in Ref. 1; CAA39670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1651 AA; 193318 MW; CD9D49B72546611C CRC64;
MKFFIALALL GAALASTHLD RYNSIERNIQ ESSFRAGREY RYLFNGQLSA GLPVPSTPQG
ISRLQSQVTL QWTDGNTVRM QLQKTRFATS QQESNSMKML PFERFEEVER MNREHQELLS
MPVEFDYEHG LVREIRFAEN DQPWSENIKR AVINMLQVNI LKKEKYEGAE KSDNQEPTFS
FTNVERTLEG ECEVLYTVEE IKKEDEQRWA KSINFDKCTR RPYIHHVQTP VCKDCQQTLE
QDKMSSTVLN YNITGTSSSF LINSVELRSQ HLFAPISEKH QLVSAFTLNT MELIYAGEKK
TEIKQVRNEK TSELVYNQES EWAEQQWAQT GEEKYLRQLP QWTENKVEMI KKMFSLMAKQ
IEQGEAELEA AHTVARIVKV LRECNEEQLE QIYRHVAEHK DEKIAEQLRS IYFNTLALAG
TRVTIQQFVD KVQSRKNIAP LKASVAIKTL VDMRYPSLAI AEDIARLCES DVSSSFPALR
QSCWLTYGAI VNGVCGQTPR VFVQKNGVKM CPRDAKQRIV DKLVQQFESA STRYEKVLAL
KTLANAGLDL SVYPLEKIIL NEQHETTIRT QAIESFRRLR TQMPTKIQRV LMPVYLNRQQ
PQHIRMSALH QIIYTQPEWS VLSQIGNQLR QERNQQVRAF TLSLLRSYAN NESPCEQTFS
SRVQSLLNNI PFSSQEIDRF ESVYGKWSTY SRRHQSGFEA NFASLFTTES VLPTEMMASI
EGVLSGEWNQ YFAQIGFTQK NMEKIIKKLL SNVQEKGLEQ IVVRGKRASG SFQPTEFLSN
LLEKLRITRR QSSEQDPHAF VYIRHRDMDY AFLPIDADSI PEVVRSMIQG GRLEIGDIER
VLAQGIHFSA SNAAFLYETV RRVPTPMGLP VQFTSKMPTI SSIRGQVTFE LEPKNGKSFD
GLRLRVQAGP RVASTHVLSL RVICPIAEVG TKFLHQAVLN TPVDTEIRMN WEDKVVIRAI
YNTPSEEKRI AMIQSRPVTF TRTVAPDARQ YPEPIEMTYM LPAHKQLSQS LDREYPQIRV
QGTLNRPTSV RIPQWIVDSN VEVYYKPNVE QYEAIFELNL YNNYKMEKNY EKVYKKHNGR
RYLEAEPEYD EEEHREQITK KFEWLQNEKV YQHVAKFEIK PEVVKMEVEA VCNNDFHFCK
TQIRGEELKA TIQYVYPQTP RTVEELKEQK YRQLVVMGEM NYGENTIHIN INGQQSQEQK
KFVKQIEQAP EHETLLEASR LDQYQTVVEY EFEPKPAQYF ARYWNMVQAY LRTQYPWTSR
IETREEPSRK NMIRATINVE PRQRLTVNMT IETPMETTVL ERVELPFRLP TAQIHYQPRN
SRYEQKPVME KIAHHASKQA NCVVKSTKIN TFDQVAYRNQ FTPCYSVLAK DCGSEKSEPR
FVVLMKKINE KKEWKNVKVV YGENEIEMYK TEEGLICRVN GEEIEYQPES EIEKKQYNII
WLNKNTLKFD SDDVTVQFDG VNARIHLSAL YRNQQCGLCG HYDNEKETEF YDAENQENTI
PKFAKSYLYK DSKCNYEREM FEKEENFQRI EKNQEEEKDQ EMNYEESRRE QDDEPTEQVA
IVERQHEICF TQKPVLRCQN GKSQESKKQK VTSVYCLPSS NSWARRQMRE IRREPLAQWP
EHKLRNLRDQ PQMEERTVRV AVDQKCDKFD Y
