VIT1_CAEEL
ID VIT1_CAEEL Reviewed; 1616 AA.
AC P55155;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Vitellogenin-1;
DE Flags: Precursor;
GN Name=vit-1; ORFNames=K09F5.2;
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 [LARGE SCALE GENOMIC DNA].
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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1270, 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).
CC -!- FUNCTION: Precursor of the egg-yolk proteins that are sources of
CC nutrients during embryonic development. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; FO080893; CCD67565.1; -; Genomic_DNA.
DR PIR; T16600; T16600.
DR RefSeq; NP_509305.1; NM_076904.8.
DR AlphaFoldDB; P55155; -.
DR SMR; P55155; -.
DR BioGRID; 45958; 14.
DR IntAct; P55155; 1.
DR STRING; 6239.K09F5.2; -.
DR iPTMnet; P55155; -.
DR EPD; P55155; -.
DR PaxDb; P55155; -.
DR PeptideAtlas; P55155; -.
DR PRIDE; P55155; -.
DR EnsemblMetazoa; K09F5.2.1; K09F5.2.1; WBGene00006925.
DR UCSC; K09F5.2; c. elegans.
DR WormBase; K09F5.2; CE04746; WBGene00006925; vit-1.
DR eggNOG; KOG4338; Eukaryota.
DR GeneTree; ENSGT00530000064273; -.
DR HOGENOM; CLU_003821_0_0_1; -.
DR InParanoid; P55155; -.
DR OMA; CTPYSEA; -.
DR OrthoDB; 36651at2759; -.
DR PhylomeDB; P55155; -.
DR PRO; PR:P55155; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006925; Expressed in adult organism and 3 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 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 Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW Storage protein.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1616
FT /note="Vitellogenin-1"
FT /id="PRO_0000041532"
FT DOMAIN 24..689
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DOMAIN 1310..1479
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REGION 1505..1531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 1312..1442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1334..1478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ SEQUENCE 1616 AA; 188063 MW; F173D7C452D123F5 CRC64;
MRSIIIASIV ALAIAFSPAF ERTFEPKIDY HYKFDGLVLS GLPTASSELS QSRFSARVRI
QAVDDRHIHL QLVNIHMAAS HLPESEQIPS LNSMEQRELS EEYKQMLKLP LRAQLRNGLI
AELQFDKEDA EWSKNMKRAV VNMISFNPIA PRNEIEKIES SYDKEEQSEE NTSFFTNEKT
LEGDCQVAYT VIREQKKTII TKSINFDKCT ERSEIAYGLR YSSECPECEK DTVLIRPQTV
YTYILENEEL KESEVRSLYT VNVNGQEVMK TETRSKLVLE ENHSIKSHIE KVNGEKESII
YSSRWEQLVE DFFKNGDKAE FAPFEKFPLD KKMHLIKTIT EQIQEVENNI PETSHFLARL
VRIFRTTSTS QLKEIHETLY VKADKKIQSL MEHALAIAGT KNTIQHILVH IENEDIVPLE
AAQLLKSIQE TPFPSQTIAE ALIKFAESRV SKNNQVVRQS AWLAAGSVVR GIVDYKNIRP
LVREDKRELK EKFLRVFMQQ YKDAETTYEK ILALKSIGNA GLDISVNQLN EIIVDKRQLL
PVRKEAIDAL RLLKDTMPRK IQKVLLPIYK NRQYEPEIRM LALWRMMHTR PEESLLVQVV
SQMEKETNQQ VAALTHQMIR HFAKSTNPCY QRVAIVCSKV LSFTRYQPQE QMIASSYAQL
PLFLQNSFSG AQFDFAAIFE KNSFLLKDLH ASLDAVFGGN WNKYFAQIGF SQQHMDKYVQ
MALEKLESIE KESTTVVRGR RIQTGITLLK ELALKMNIRA RPANYNEKDA FAMVYLRYKD
MDYAILPVDT QLIEKLIEKY ISNGKVQFSE IRRLLNQEHE FETHHAAYFY EAIRKFPTTL
GLPLIVSGKI PTVFSAEGQF SLGLEETELR LTVEARPSVA ATHVYEMRMF TPLFEQGVKS
VQSVRAYTPI KIQAVVGMKR NFEIVYKVVV PENQKSIISL TTRPVVFLRF PGFSKFEYIE
AEERTVVVPQ WQQKTQEIEK VFNFLGLEVS TRGNILNQHT LENWLLAEQD FEVSVENKYR
PAEFTARLTV GQLEKTELSQ IKYNKIFEKE FELEQENTES RREYFTKMVK SIQKEQGYKS
VVSLRLEAPR DYTMNTEVTT VCDKQVRMCQ WEVEIRRSPI LEETKEWTLR SQLLVVRPEM
PSSLRQLHDQ PHREVQLSLT STWGSQKKSE VTVNAQLQQS KEQKKYERNM DRHFNGMPEY
ELLIKAARLN QINAVAEYKL TRETEQVLAR YFDLVKAYNY WTVSSRPENN ENDRVVVQLT
VEPMSRQYVN ITMQSPIERV ELKNVQVPRV YLPSIAQRSV KHLLNEASGS VCKVQKNQIR
TFDDVLYNTP LTTCYSLIAK DCSEEPTFAV LSKKTEKNSE EMIIKVIRGE QEIVAQLQNE
EIRVKVDGKK ILSEDYSAHQ IERLGESDIV IELPEGEVRF DGYTIKTQLP SYSRKNQLCG
LCGNNDDEST NEFYTSDNTE TKDIEEFHRS YLLKNEECEA EEERLSEKKN YRKYDERKYE
SEEYSFEETY DYEQENTNKK QKNQRSQKKS DLVEKTQIKE FSHRICFSVE PVAECRRRGY
EAVEQQQRKV RFTCLPRHSS EARRLVKEAR QGTVQLDDHK ISFVHSVQVP VACVAY
