ID A0A261CUJ9_9PELO Unreviewed; 1629 AA.
AC A0A261CUJ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Vitellogenin domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=FL83_00810 {ECO:0000313|EMBL:OZG25606.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG25606.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG25606.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG25606.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZG25606.1}.
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DR EMBL; NIPN01000001; OZG25606.1; -; Genomic_DNA.
DR STRING; 1503980.A0A261CUJ9; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.80.10; Lipovitellin-phosvitin complex, chain A, domain 4; 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; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR23345:SF8; VITELLOGENIN-3-RELATED; 1.
DR PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR Pfam; PF09172; Vit_open_b-sht; 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; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00557};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Storage protein {ECO:0000256|ARBA:ARBA00022761};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..715
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1336..1505
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DISULFID 252..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG25606.1"
SQ SEQUENCE 1629 AA; 188128 MW; D8F5F0392323150C CRC64;
MVNSVTSNHL LSISCSCIKR VPGRGIITLA MKSIIIASLV ALAIAASPAF DRTFSPKSEY
VYKFDGLILS GLPTTSSDAS QTRISCRTRI QVIDDRYIHL QLTDVTYSAS HIPQTEQWPK
MESLEQRELS DELKELLELP FRVQMKNGLI SEIQFSSEDA EWSKNSKRSI VNLLSLHRSA
PVDELNQEEK DMETEKDSRF FNVHEKTMEG DCEVAYTIIQ EGEKTIYTKS VNFDKCITRP
ETAYGLRSGS ECKECEKEGQ FVRPQTVYTY TFKNEQLEQS EAHSVYTLSV NGQEMIKSET
RSKMVFVEEK KWNKEIKKVT GPKEDIVYST GEEVLIEKFC QEGDKAKNPF EVIPSAQKIE
QLQEIFRQVQ EHEQNTPETV HLIARAVRLF RMSTIDELKK VHSAIYTKSE EKIRSLIENS
LAVAGTKNAV QHLIHHIQKK TISPLRAAEL LKSIQETLTP SELIADLLIE LAQSPLAEQN
EPLRQSAWLA AGSVVRGFTS KTQNLPLARP ATRQLKEKYV RVFMQHFRSA ESTYEKVLAL
KTLGNAGIDM SVNELVQLIQ DPRQPLAIRT EAVDALRLLK DVMPRKIQKV LLPXXXXXXX
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
XXXXXXILLF TRYQPQEQIL STYAQLPIFQ SEMLSGVQFD FATIFEKNSF LPXEIYXSFE
SVLGGNWNKY FAQVGFSQQN FEQIILKALE RLSLYGKQPD ELRSRRVQSG IQMLQEIVKK
MNIRPRVQRT DEQSAHAVFY LRYKDMDFVV LPLDMETIDN LLEKYVRNGE FDIKSILALL
NNDSEFEIHR AIYFYESVRR IPTTIGLPLT ITGKMPTVIS LTGKVSVEMQ KLGARVTLDV
VPSVAATHIT EMRFWSPSLD QGVKSLQSAR VHTPLRLELN AELKKNTLEI THKFVVPENK
KTTVAVHTRP VAFMRVQRDQ ETKYTEAEEK TISHPQYQLA SEEINREYEI LGLKINVQGN
ILSQWSLPKV LMSEQDFEYT LENKNRPAEF VARFTIGNLE KTDLSEIKFD KIFEKEFDME
NNESENRRQH FNKMIREIQS EQGYKNLISM KFEAPQQWYW NHEVRTVCDQ YVRMCKIEMD
CRRSPVAEET KEWTLHTELL AVRPQMPSSL RQLREQPHRE VQLALNAKWG SSKKSEITVN
AQLEQSKEQK KYVRNMEREF NGIPEYELLI KAARLNQINV VSEYKLTQEA EHTFSRLFDL
IKAYNFWTVS EKRVENEERR VVLQLTVEPL SRQYINMTIQ TPQQQVELKN VRIPRVFLPT
IARRAMYQQV WEKTGASCKV DQSEVSTFDN VIYRAPLTTC FSLVAKDCSE QPTFAILSKK
MNKNSDELIV KVVRREEELV IKKTDDEFVV KVDGKKIQQS EFEQYEIEVL GDNLIVIRLP
QGEVRFDGYT IKTNVPSNAT KSQLCGLCGN NDGENDNEFT TADNYETDDV EEFHRSYLLK
DEECAVENDR LSEKKNYLNK WNREEKRQES QYESNKDDDE SENKSVEKTL IKEFSNRVCF
SLEPVTECRR GFESEKTTSK KLRFTCMPRH SKNARRFMKE ARDQTILDLA DFPVSYVEAV
KIPTACVVY
//
