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APOV1_CHICK
ID   APOV1_CHICK             Reviewed;         106 AA.
AC   P02659; Q90882;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Apovitellenin-1;
DE   AltName: Full=Apo-VLDL-II;
DE            Short=Apo-II;
DE   AltName: Full=Apovitellenin I;
DE   AltName: Full=Very low density lipoprotein II;
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6856469; DOI=10.1093/nar/11.9.2529;
RA   van Het Schip A.D., Meijlink F.C.P.W., Strijker R., Gruber M.,
RA   van Vliet A.J., van de Klundert J.A.M., Ab G.;
RT   "The nucleotide sequence of the chicken apo very low density lipoprotein II
RT   gene.";
RL   Nucleic Acids Res. 11:2529-2540(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7012793; DOI=10.1093/nar/9.3.489;
RA   Wieringa B., Ab G., Gruber M.;
RT   "The nucleotide sequence of the very low density lipoprotein II mRNA from
RT   chicken.";
RL   Nucleic Acids Res. 9:489-501(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=7286648; DOI=10.1016/0378-1119(81)90113-x;
RA   Dugaiczyk A., Inglis A.S., Strike P.M., Burley R.W., Beattie W.G., Chan L.;
RT   "Comparison of the nucleotide sequence of cloned DNA coding for an
RT   apolipoprotein (apo VLDL-II) from avian blood and the amino acid sequence
RT   of an egg-yolk protein (apovitellenin I): equivalence of the two
RT   sequences.";
RL   Gene 14:175-182(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2703502; DOI=10.1016/s0021-9258(18)83375-0;
RA   Cochrane A., Deeley R.G.;
RT   "Detection and characterization of degradative intermediates of avian apo
RT   very low density lipoprotein II mRNA present in estrogen-treated birds and
RT   following destabilization by hormone withdrawal.";
RL   J. Biol. Chem. 264:6495-6503(1989).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-51 (PRECURSOR PROTEIN).
RX   PubMed=7430115; DOI=10.1016/s0021-9258(19)70427-x;
RA   Chan L., Bradley W.A., Means A.R.;
RT   "Amino acid sequence of the signal peptide of apoVLDL-II, a major
RT   apoprotein in avian very low density lipoproteins.";
RL   J. Biol. Chem. 255:10060-10063(1980).
RN   [6]
RP   PROTEIN SEQUENCE OF 25-106.
RC   TISSUE=Egg yolk;
RX   PubMed=988817; DOI=10.1071/bi9760175;
RA   Dopheide T.A.A., Inglis A.S.;
RT   "Primary structure of apovitellenin I from hen egg yolk and its comparison
RT   with emu apovitellenin I.";
RL   Aust. J. Biol. Sci. 29:175-180(1976).
RN   [7]
RP   PROTEIN SEQUENCE OF 25-106.
RC   TISSUE=Plasma;
RX   PubMed=188805; DOI=10.1016/s0021-9258(17)32824-7;
RA   Jackson R.L., Lin H.-Y., Chan L., Means A.R.;
RT   "Amino acid sequence of a major apoprotein from hen plasma very low density
RT   lipoproteins.";
RL   J. Biol. Chem. 252:250-253(1977).
CC   -!- FUNCTION: Protein component of the very low density lipoprotein (VLDL)
CC       of egg-laying females. Potent lipoprotein lipase inhibitor, preventing
CC       the loss of triglycerides from VLDL on their way from the liver to the
CC       growing oocytes.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- TISSUE SPECIFICITY: Produced by the liver, secreted into the blood and
CC       then sequestred by receptor mediated endocytosis into growing oocytes.
CC   -!- DEVELOPMENTAL STAGE: ApoII mRNA induction by estrogen in kidney at day
CC       11 is at 10% of the level in the liver but estrogen-responsiveness
CC       decreases later in development and is low in the adult.
CC   -!- INDUCTION: By steroids (estrogen).
CC   -!- SIMILARITY: Belongs to the apovitellenin family. {ECO:0000305}.
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DR   EMBL; V00449; CAA23727.1; -; mRNA.
DR   EMBL; J00810; AAA48596.1; -; Genomic_DNA.
DR   EMBL; M25774; AAA48938.1; -; mRNA.
DR   PIR; A93464; VLCH1.
DR   PIR; I50374; I50374.
DR   RefSeq; NP_990814.2; NM_205483.2.
DR   RefSeq; XP_015151420.1; XM_015295934.1.
DR   AlphaFoldDB; P02659; -.
DR   SMR; P02659; -.
DR   STRING; 9031.ENSGALP00000024373; -.
DR   Allergome; 2740; Gal d Apo I.
DR   PaxDb; P02659; -.
DR   Ensembl; ENSGALT00000024419; ENSGALP00000024373; ENSGALG00000015134.
DR   GeneID; 396476; -.
DR   KEGG; gga:396476; -.
DR   CTD; 396476; -.
DR   VEuPathDB; HostDB:geneid_396476; -.
DR   eggNOG; ENOG502SRWC; Eukaryota.
DR   GeneTree; ENSGT00530000066877; -.
DR   HOGENOM; CLU_176392_0_0_1; -.
DR   InParanoid; P02659; -.
DR   OMA; RRDWLVI; -.
DR   OrthoDB; 1497857at2759; -.
DR   PhylomeDB; P02659; -.
DR   PRO; PR:P02659; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000015134; Expressed in liver and 4 other tissues.
DR   GO; GO:0042627; C:chylomicron; IEA:InterPro.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR008404; Apo-VLDL-II.
DR   Pfam; PF05418; Apo-VLDL-II; 1.
DR   PIRSF; PIRSF002369; Apo-VLDL-II; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Reference proteome; Signal;
KW   Storage protein; VLDL.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:188805,
FT                   ECO:0000269|PubMed:7012793, ECO:0000269|PubMed:988817"
FT   CHAIN           25..106
FT                   /note="Apovitellenin-1"
FT                   /id="PRO_0000002064"
FT   DISULFID        99
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:188805"
FT   CONFLICT        2
FT                   /note="Missing (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="H -> C (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68..69
FT                   /note="TV -> NS (in Ref. 4; AAA48938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71..73
FT                   /note="SGI -> IGS (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91..92
FT                   /note="LM -> ML (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   106 AA;  11966 MW;  8A17DA72F574AF67 CRC64;
     MVQYRALVIA VILLLSTTVP EVHSKSIIDR ERRDWLVIPD AAAAYIYEAV NKVSPRAGQF
     LLDVSQTTVV SGIRNFLINE TARLTKLAEQ LMEKIKNLCY TKVLGY
 
 
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