ID   APOB_RABIT              Reviewed;         144 AA.
AC   P17165;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Apolipoprotein B;
DE   Flags: Fragment;
GN   Name=APOB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3419914; DOI=10.1093/nar/16.16.8187;
RA   Sudarickov A., Surguchov A.;
RT   "Probe for rabbit apolipoprotein B gene.";
RL   Nucleic Acids Res. 16:8187-8187(1988).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=3171395;
RA   Lenich C., Brecher P., Makrides S., Chobanian A., Zannis V.I.;
RT   "Apolipoprotein gene expression in the rabbit: abundance, size, and
RT   distribution of apolipoprotein mRNA species in different tissues.";
RL   J. Lipid Res. 29:755-764(1988).
RN   [3]
RP   RNA EDITING.
RX   PubMed=2911593; DOI=10.1073/pnas.86.2.500;
RA   Tennyson G.E., Sabatos C.A., Higuchi K., Meglin N., Brewer H.B. Jr.;
RT   "Expression of apolipoprotein B mRNAs encoding higher- and lower-molecular
RT   weight isoproteins in rat liver and intestine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:500-504(1989).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=1463445; DOI=10.1042/bj2880413;
RA   Wilkinson J., Higgins J.A., Groot P.H.E., Gherardi E., Bowyer D.E.;
RT   "Determination of the intracellular distribution and pool sizes of
RT   apolipoprotein B in rabbit liver.";
RL   Biochem. J. 288:413-419(1992).
CC   -!- FUNCTION: Apolipoprotein B is a major protein constituent of
CC       chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-
CC       100 functions as a recognition signal for the cellular binding and
CC       internalization of LDL particles by the apoB/E receptor.
CC   -!- SUBUNIT: Interacts with PCSK9. Interacts with MTTP. Interacts with
CC       AUP1. {ECO:0000250|UniProtKB:P04114}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
CC       Secreted {ECO:0000269|PubMed:1463445}. Lipid droplet
CC       {ECO:0000250|UniProtKB:P04114}.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Highly
CC       expressed in liver. Detected at lower levels in jejunum, duodenum and
CC       kidney. {ECO:0000269|PubMed:1463445, ECO:0000269|PubMed:3171395}.
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DR   EMBL; X07480; CAA30366.1; -; Genomic_DNA.
DR   PIR; S01290; S01290.
DR   AlphaFoldDB; P17165; -.
DR   STRING; 9986.ENSOCUP00000004631; -.
DR   PRIDE; P17165; -.
DR   eggNOG; KOG4338; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Chylomicron; Cytoplasm; Heparin-binding; LDL;
KW   Lipid droplet; Lipid metabolism; Lipid transport; Reference proteome;
KW   RNA editing; Secreted; Steroid metabolism; Sterol metabolism; Transport;
KW   VLDL.
FT   CHAIN           <1..>144
FT                   /note="Apolipoprotein B"
FT                   /id="PRO_0000064639"
FT   NON_TER         1
FT   NON_TER         144
SQ   SEQUENCE   144 AA;  15664 MW;  5ED9F09D0A9EFA26 CRC64;
     DLTFSKQNAL LRAEYQADYK SLRFFTLLSG LLNTHGLELN ADILGTDKMN TAAHKATLRI
     GQNGVSTSAT TSLRYSPLML ENELNAELAL SGASMKLATN GRFKEHNAKF SLDGKATLTE
     LSLGSAYQAM ILGADSKNIF NFKI