LOCUS VIT1_CAEEL 1616 aa linear INV 27-NOV-2024
DEFINITION RecName: Full=Vitellogenin-1; Flags: Precursor.
ACCESSION P55155
VERSION P55155.2
DBSOURCE UniProtKB: locus VIT1_CAEEL, accession P55155;
class: standard.
created: Oct 1, 1996.
sequence updated: Nov 1, 1997.
annotation updated: Nov 27, 2024.
xrefs: FO080893.2, CCD67565.1, T16600, NP_509305.1
xrefs (non-sequence databases): AlphaFoldDB:P55155, SMR:P55155,
BioGRID:45958, IntAct:P55155, STRING:6239.K09F5.2.1,
GlyCosmos:P55155, iPTMnet:P55155, PaxDb:6239-K09F5.2,
PeptideAtlas:P55155, EnsemblMetazoa:K09F5.2.1,
EnsemblMetazoa:K09F5.2.1, EnsemblMetazoa:WBGene00006925,
UCSC:K09F5.2, AGR:WB:WBGene00006925, WormBase:K09F5.2,
WormBase:CE04746, eggNOG:KOG4338, GeneTree:ENSGT00530000064273,
HOGENOM:CLU_003821_0_0_1, InParanoid:P55155, OMA:CTPYSEA,
OrthoDB:3076121at2759, PhylomeDB:P55155, PRO:PR:P55155,
Proteomes:UP000001940, Bgee:WBGene00006925, GO:0005576, GO:0005319,
GO:0045735, FunFam:1.25.10.20:FF:000003,
FunFam:2.30.230.10:FF:000004, FunFam:2.20.80.10:FF:000004,
Gene3D:2.20.80.10, Gene3D:1.25.10.20, InterPro:IPR015819,
InterPro:IPR011030, InterPro:IPR015816, InterPro:IPR015255,
InterPro:IPR050733, InterPro:IPR001747, InterPro:IPR001846,
PANTHER:PTHR23345:SF12, PANTHER:PTHR23345, Pfam:PF09172,
Pfam:PF01347, Pfam:PF00094, SMART:SM01169, SMART:SM00638,
SMART:SM00216, SUPFAM:SSF48431, PROSITE:PS51211, PROSITE:PS51233
KEYWORDS Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
Storage protein.
SOURCE Caenorhabditis elegans
ORGANISM Caenorhabditis elegans
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
REFERENCE 1 (residues 1 to 1616)
CONSRTM C. elegans Sequencing Consortium
TITLE Genome sequence of the nematode C. elegans: a platform for
investigating biology
JOURNAL Science 282 (5396), 2012-2018 (1998)
PUBMED 9851916
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=Bristol N2
Erratum:[Science 1999 Jan 1;283(5398):35]
REFERENCE 2 (residues 1 to 1616)
AUTHORS Kaji,H., Kamiie,J., Kawakami,H., Kido,K., Yamauchi,Y., Shinkawa,T.,
Taoka,M., Takahashi,N. and Isobe,T.
TITLE Proteomics reveals N-linked glycoprotein diversity in
Caenorhabditis elegans and suggests an atypical translocation
mechanism for integral membrane proteins
JOURNAL Mol Cell Proteomics 6 (12), 2100-2109 (2007)
PUBMED 17761667
REMARK GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1270, AND
IDENTIFICATION BY MASS SPECTROMETRY.;
STRAIN=Bristol N2
REFERENCE 3 (residues 1 to 1616)
AUTHORS Seah,N.E., de Magalhaes Filho,C.D., Petrashen,A.P., Henderson,H.R.,
Laguer,J., Gonzalez,J., Dillin,A., Hansen,M. and Lapierre,L.R.
TITLE Autophagy-mediated longevity is modulated by lipoprotein biogenesis
JOURNAL Autophagy 12 (2), 261-272 (2016)
PUBMED 26671266
REMARK FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
COMMENT On or before Jun 21, 2005 this sequence version replaced
gi:7442002, gi:1722701.
[FUNCTION] Precursor of the egg-yolk proteins that are sources of
nutrients during embryonic development (Probable). Together with
other vitellogenins, may play a role in modulating life-span,
acting via induction of autophagy and lysosomal lipolysis
(PubMed:26671266). {ECO:0000269|PubMed:26671266, ECO:0000305}.
[SUBCELLULAR LOCATION] Secreted {ECO:0000305|PubMed:26671266}.
[TISSUE SPECIFICITY] Expressed in the intestine of adult
hermaphrodites. {ECO:0000305|PubMed:26671266}.
[DISRUPTION PHENOTYPE] Simultaneous RNAi-mediated knockdown of
vitellogenins vit-1, vit-2, vit-3, vit-4 and vit-5 increases life
span, causes accumulation of neutral lipid and an increase in lgg-1
foci in the proximal intestine; however, does not affect fertility
or pharyngeal pumping rates (PubMed:26671266). Expression of
transcription factors pha-4 and daf-16 are increased
(PubMed:26671266). {ECO:0000269|PubMed:26671266}.
[CAUTION] High sequence similarity with other vitellogenin genes
means that assigning functions to individual proteins is difficult;
authors sometimes refer to VITs or vitellogenins.
{ECO:0000305|PubMed:26671266}.
FEATURES Location/Qualifiers
source 1..1616
/organism="Caenorhabditis elegans"
/db_xref="taxon:6239"
gene 1..1616
/gene="vit-1"
/locus_tag="K09F5.2"
Protein 1..1616
/product="Vitellogenin-1"
/UniProtKB_evidence="Evidence at protein level"
Region 1..19
/region_name="Signal"
/note="/evidence=ECO:0000255."
Region 20..1616
/region_name="Mature chain"
/note="Vitellogenin-1. /id=PRO_0000041532."
Region 24..689
/region_name="Domain"
/note="Vitellogenin.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00557."
Region 24..620
/region_name="Vitellogenin_N"
/note="Lipoprotein amino terminal region; pfam01347"
/db_xref="CDD:460170"
Region 655..939
/region_name="Vit_open_b-sht"
/note="Vitellinogen, open beta-sheet; pfam09172"
/db_xref="CDD:462702"
Site 1270
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:17761667."
Region 1301..1458
/region_name="VWD"
/note="von Willebrand factor (vWF) type D domain;
smart00216"
/db_xref="CDD:214566"
Region 1310..1479
/region_name="Domain"
/note="VWFD.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00580."
Bond bond(1312,1442)
/bond_type="disulfide"
/note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00580."
Bond bond(1334,1478)
/bond_type="disulfide"
/note="/evidence=ECO:0000255|PROSITE-ProRule:PRU00580."
Region 1505..1531
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 1512..1531
/region_name="Compositionally biased region"
/note="Basic and acidic residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
1 mrsiiiasiv alaiafspaf ertfepkidy hykfdglvls glptassels qsrfsarvri
61 qavddrhihl qlvnihmaas hlpeseqips lnsmeqrels eeykqmlklp lraqlrngli
121 aelqfdkeda ewsknmkrav vnmisfnpia prneiekies sydkeeqsee ntsfftnekt
181 legdcqvayt vireqkktii tksinfdkct erseiayglr yssecpecek dtvlirpqtv
241 ytyileneel kesevrslyt vnvngqevmk tetrsklvle enhsikshie kvngekesii
301 yssrweqlve dffkngdkae fapfekfpld kkmhliktit eqiqevenni petshflarl
361 vrifrttsts qlkeihetly vkadkkiqsl mehalaiagt kntiqhilvh ienedivple
421 aaqllksiqe tpfpsqtiae alikfaesrv sknnqvvrqs awlaagsvvr givdyknirp
481 lvredkrelk ekflrvfmqq ykdaettyek ilalksigna gldisvnqln eiivdkrqll
541 pvrkeaidal rllkdtmprk iqkvllpiyk nrqyepeirm lalwrmmhtr peesllvqvv
601 sqmeketnqq vaalthqmir hfakstnpcy qrvaivcskv lsftryqpqe qmiassyaql
661 plflqnsfsg aqfdfaaife knsfllkdlh asldavfggn wnkyfaqigf sqqhmdkyvq
721 maleklesie kesttvvrgr riqtgitllk elalkmnira rpanynekda famvylrykd
781 mdyailpvdt qlieklieky isngkvqfse irrllnqehe fethhaayfy eairkfpttl
841 glplivsgki ptvfsaegqf slgleetelr ltvearpsva athvyemrmf tplfeqgvks
901 vqsvraytpi kiqavvgmkr nfeivykvvv penqksiisl ttrpvvflrf pgfskfeyie
961 aeertvvvpq wqqktqeiek vfnflglevs trgnilnqht lenwllaeqd fevsvenkyr
1021 paeftarltv gqlektelsq ikynkifeke feleqentes rreyftkmvk siqkeqgyks
1081 vvslrleapr dytmntevtt vcdkqvrmcq weveirrspi leetkewtlr sqllvvrpem
1141 psslrqlhdq phrevqlslt stwgsqkkse vtvnaqlqqs keqkkyernm drhfngmpey
1201 ellikaarln qinavaeykl treteqvlar yfdlvkayny wtvssrpenn endrvvvqlt
1261 vepmsrqyvn itmqspierv elknvqvprv ylpsiaqrsv khllneasgs vckvqknqir
1321 tfddvlyntp lttcysliak dcseeptfav lskkteknse emiikvirge qeivaqlqne
1381 eirvkvdgkk ilsedysahq ierlgesdiv ielpegevrf dgytiktqlp sysrknqlcg
1441 lcgnnddest nefytsdnte tkdieefhrs yllkneecea eeerlsekkn yrkyderkye
1501 seeysfeety dyeqentnkk qknqrsqkks dlvektqike fshricfsve pvaecrrrgy
1561 eaveqqqrkv rftclprhss earrlvkear qgtvqlddhk isfvhsvqvp vacvay
//