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VIT_ACITR
ID   VIT_ACITR               Reviewed;        1677 AA.
AC   Q90243;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Vitellogenin;
DE            Short=VTG;
DE   Contains:
DE     RecName: Full=Lipovitellin I;
DE              Short=LVI;
DE   Contains:
DE     RecName: Full=Phosvitin;
DE              Short=PV;
DE   Contains:
DE     RecName: Full=Lipovitellin II;
DE              Short=LVII;
DE   Flags: Precursor; Fragment;
OS   Acipenser transmontanus (White sturgeon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX   NCBI_TaxID=7904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=UC Davis Broodstock; TISSUE=Liver;
RX   PubMed=7608984; DOI=10.1007/bf00174046;
RA   Bidwell C.A., Carlson D.M.;
RT   "Characterization of vitellogenin from white sturgeon, Acipenser
RT   transmontanus.";
RL   J. Mol. Evol. 41:104-112(1995).
CC   -!- FUNCTION: Precursor of the major egg-yolk proteins that are sources of
CC       nutrients during early development of oviparous organisms.
CC   -!- TISSUE SPECIFICITY: Found in liver, testis and undifferentiated gonads
CC       of estrogen-treated fish. Not detected in the brain and spleen.
CC   -!- INDUCTION: By steroids (estrogen).
CC   -!- PTM: Phosvitin, an egg yolk storage protein, is one of the most highly
CC       phosphorylated (10%) proteins in nature. {ECO:0000250}.
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DR   EMBL; U00455; AAA87392.1; -; mRNA.
DR   PIR; T43021; T43021.
DR   AlphaFoldDB; Q90243; -.
DR   SMR; Q90243; -.
DR   PRIDE; Q90243; -.
DR   GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.20; -; 1.
DR   Gene3D; 2.20.50.20; -; 1.
DR   Gene3D; 2.20.90.10; -; 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; 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   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF09172; DUF1943; 1.
DR   Pfam; PF09175; DUF1944; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM01169; DUF1943; 1.
DR   SMART; SM01170; DUF1944; 1.
DR   SMART; SM00638; LPD_N; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF48431; SSF48431; 1.
DR   SUPFAM; SSF56968; SSF56968; 3.
DR   PROSITE; PS51211; VITELLOGENIN; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Phosphoprotein; Signal; Storage protein.
FT   SIGNAL          <1..8
FT                   /evidence="ECO:0000255"
FT   CHAIN           9..1677
FT                   /note="Vitellogenin"
FT                   /id="PRO_0000041576"
FT   CHAIN           9..?1091
FT                   /note="Lipovitellin I"
FT                   /id="PRO_0000041577"
FT   CHAIN           ?1092..?1300
FT                   /note="Phosvitin"
FT                   /id="PRO_0000041578"
FT   CHAIN           ?1301..1677
FT                   /note="Lipovitellin II"
FT                   /id="PRO_0000041579"
FT   DOMAIN          17..655
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT   DOMAIN          1490..1675
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   REGION          1089..1232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1252..1280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1636..1659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1089..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1208..1232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1255..1280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        1182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1218
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        1492..1631
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   DISULFID        1515..1674
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   NON_TER         1
SQ   SEQUENCE   1677 AA;  186022 MW;  5F49DA86E434DC35 CRC64;
     LTIALVGSQQ TKYEPSFSGS KTYQYKYEGV ILTGLPEKGL ARAGLKVHCK VEISEVAQKT
     YLLKILNPEI QEYNGIWPKA PFYPASKLTQ ALASQLTQPI KFQYRNGQVG DIFASEDVSD
     TVLNIQRGIL NMLQLTIKTT QNVYGLQENG IAGICEASYV IQEDRKANKI IVTKSKDLNN
     CNEKIKMDIG MAYSHTCSNC RKIRKNTRGT AAYTYILKPT DTGTLITQAT SQEVHQLTPF
     NEMTGAAITE ARQKLVLEDA KVIHVTVPEQ ELKNRGSIQY QFASEILQTP IQLFKTRSPE
     TKIKEVLQHL VQNNQQQVQS DAPSKFLQLT QLLRACTHEN IEGIWRQYEK TQLYRRWILD
     ALPAAATPTA FRFITQRIMK RDLTDAEAIQ TLVTAMHLVQ TNHQIVQMAA ELVFDRANLK
     CPVLRKHAVL AYGSMVNRYC AETLNCREEA LKPLHDFAND AISRAHEEET VLALKALGNA
     GQPSSIKRIQ KCLPGFSSGA SQLPVKIQVD AVMALRNIAK KEPGKVQELT MQLFMDHQLH
     SEVRMVASMV LLETRPSMAL VATLAEALLK ETSLQVASFT YSHMKAITRS TAPENHALSS
     ACNVAVKLLS RKLDRLSYRY SKAMHMDTFK YPLMAGAAAN IHIINNAASI LPSAVVMKFQ
     AYILSATADP LEIGLHTEGL QEVLMQNHEH IDQMPSAGKI QQIMKMLSGW KSVPSEKTLA
     SAYIKLFGQE ISFSRLDKKT IQEALQAVRE PVERQTVIKR VVNQLERGAA AQLSKPLLVA
     EVRRILPTCI GLPMEMSLYV SAVTTADINV QAHITPSPTN DFNVAQLLNS NIVLHTDVTP
     SIAMHTIAVM GINTHVIQTG VELHVKARTT VPMKFTAKID LKEKNFKIES EPCQQETEVL
     SLSAQAFAIS RNVEDLDAAK KNPLLPEEAV RNILNEQFNS GTEDSNERER AGKFARPSAE
     MMSQELMNSG EHQNRKGAHA TRSACAKAKN FGFEVCFEGK SENVAFLRDS PLYKIIGQHH
     CKIALKPSHS SEATIEKIQL ELQTGNKAAS KIIRVVAMQS LAEADEMKGN ILKKLNKLLT
     VDGETQDSTL RGFKRRSSSS SSSSSSSSSS SSSSSSSSSQ QSRMEKRMEQ DKLTENLERD
     RDHMRGKQSK NKKQEWKNKQ KKHHKQLPSS SSSSSSSSSG SNSSSSSSSS SSSSSRSHNH
     RNNTRTLSKS KRYQNNNNSS SSSGSSSSSE EIQKNPEIFA YRFRSHRDKL GFQNKRGRMS
     SSSSSSSSSS SQSTLNSKQD AKFLGDSSPP IFAFVARAVR SDGLQQGYQV AAYTDNRVSR
     PRVQLLATEI IEKSRWQICA DAILASNYKA MALMRWGEEC QDYKVAVSAV TGRLASHPSL
     QIKAKWSRIP RAAKQTQNIL AEYVPGAAFM LGFSQKEQRN PSKQFKIILA VTSPNTIDTL
     IKAPKITLFK QAVQIPVQIP MEPSDAERRS PGLASIMNEI PFLIEEATKS KCVAQENKFI
     TFDGVKFSYQ MPGGCYHILA QDCRSKVRFM VMLKQASMSK NLRAVNAKIY NKDIDILPTT
     KGSVRLLINN NEIPLSQLPF TDSSGNIHIK RADEGVSVSA QQYGLESLYF DGKTVQVKVT
     SEMRGKTCGL CGHNDGERRK EFRMPDGRQA RGPSVSPTPG LCLEKTATEA ASFCVIM
 
 
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