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Database: UniProt
Entry: F2Y9S5_MORSA
LinkDB: F2Y9S5_MORSA
Original site: F2Y9S5_MORSA 
ID   F2Y9S5_MORSA            Unreviewed;      1275 AA.
AC   F2Y9S5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Vitellogenin C {ECO:0000313|EMBL:ADZ57174.1};
OS   Morone saxatilis (Striped bass) (Perca saxatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=34816 {ECO:0000313|EMBL:ADZ57174.1};
RN   [1] {ECO:0000313|EMBL:ADZ57174.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:ADZ57174.1};
RX   PubMed=24005815; DOI=10.1007/s10695-013-9852-0;
RA   Williams V.N., Reading B.J., Hiramatsu N., Amano H., Glassbrook N.,
RA   Hara A., Sullivan C.V.;
RT   "Multiple vitellogenins and product yolk proteins in striped bass, Morone
RT   saxatilis: molecular characterization and processing during oocyte growth
RT   and maturation.";
RL   Fish Physiol. Biochem. 40:395-415(2014).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR   EMBL; HQ846511; ADZ57174.1; -; mRNA.
DR   AlphaFoldDB; F2Y9S5; -.
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; 2.20.50.20; Lipovitellin. Chain A, domain 3; 2.
DR   Gene3D; 2.20.90.10; Vitellinogen, beta-sheet shell domain; 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; IPR015258; Vitellinogen_b-sht_shell.
DR   InterPro; IPR037088; Vitellinogen_b-sht_shell_sf.
DR   InterPro; IPR015255; Vitellinogen_open_b-sht.
DR   InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR   InterPro; IPR001747; Vitellogenin_N.
DR   PANTHER; PTHR23345:SF29; VITELLOGENIN 3, PHOSVITINLESS PRECURSOR; 1.
DR   PANTHER; PTHR23345; VITELLOGENIN-RELATED; 1.
DR   Pfam; PF09175; Vit_b-sht_shell; 1.
DR   Pfam; PF09172; Vit_open_b-sht; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   SMART; SM01169; DUF1943; 1.
DR   SMART; SM01170; DUF1944; 1.
DR   SMART; SM00638; LPD_N; 1.
DR   SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR   PROSITE; PS51211; VITELLOGENIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00557}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Storage protein {ECO:0000256|ARBA:ARBA00022761}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..1275
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012181035"
FT   DOMAIN          24..662
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000259|PROSITE:PS51211"
FT   DISULFID        162..188
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00557"
SQ   SEQUENCE   1275 AA;  142930 MW;  45460341103D1E18 CRC64;
     MQGLLFCCLV ALATCQSVHY ELSLNPKKTY EYKYEGGVNF GLGIPNLAES GVRMTCKVKI
     VGVSAQTFIL QASNLVFEEF NGFPGKNTYN ASPKLTQRIA AQLIKPFMFN YTCGHVSDIH
     ASAEISDTVV NIVRGILGFF QVTVKTTQRI YELEEVGIHG KCQSNYATEE NMETKDMTIT
     QVVDVSGCRE KAAIYRGMAT AVLDNVSKQR GESVISTVRY VYTVKATEEG GLITRAHGLE
     QQHFSSFNVK GGSFKMQAMK EIVLLGVSDT ARAVIFGPME NKGNLVYKFV NAEANVPIMM
     QNLEDPLPKA VELIKHLAEA NKYQIDSATT EDTIKLYQLL RVMPYEELEA VWKQLLGNEE
     HRRWFLDMIV EVSDARILKF LEVRFQSGDI SVVEAGEILL LAINHLQAIP ELVEMAKVFL
     TMPFSKSNIY LWHTVALTYG SLVYKHCAYY TPCPINSVQP LLDMAMESLR NGNEADMVIA
     LKALGNAGHP GSIKTIMRFL PGVAATPVDL PPRVLSAAVQ SMRLIAARDP HSVQDITMSL
     FLQKNLPTEI RMLAFMILFD TKPTLALVST VTAHLQEEKD LHVVSFAYSY FRSFARSSTP
     ENHFLSIACN VAVKVLAPKF GRLSYHYSKA MRMDWFNDDF LIGTAAEVFM LRSATNIFPT
     EIMMKGKFFF IGRILQLLEL GIRAEGIKEL FGTSIPGFTG DLSFSDFQAI FNVFQNWEIL
     PNDKPLLSAF SRVFGQEWFF ADINKDFIQN IIRAVTPSAE KESPLWAVIE DLQRGVSWHR
     TKPFLIFEVR YFQATTLGLP LEISKYYESI NGITVNAKTA VNPPLTEHLA QLLTSEISLE
     TDGFIGFTKD LWVFYGINTA LFQCGSEFKS KMPLAIPWKF SAKINVREKK FELDFLPCKK
     EFEVFSVSSN VYAVTRNIEE PALAKMTPIM PNAIDSNDEV VHIGPTVVRP EPEQMLTPNT
     WHPIAKMCAE NNIYGAGLCV ESELRREYYH EEYPLYYFLG YTHLAFKVVP AQAIKAVDKI
     HFEVNAGPSR HPMSARQLLD TLRRISKEAT QRVHLSSDSA SSVRGSPNNH HDHLMEGWNS
     TPEAVFNIKA FAMSGNQKPE GYDAAIYYTP EANTENAQLI VSQVGEDINW KMCVDTIVHA
     HAEAKAHIRW GAECQTYEMS MGGATAHLPG SKPTLMAKVH WARIPETMAD MGRGIESYIP
     GIAFLLGFSE QHERNAKQEV SASVVAASAD SINMKIKFPE YTVFRQAIPV PLPPASFLEF
     QQDIRNTTMD SFGRA
//
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