ID   APOB_CHICK              Reviewed;         433 AA.
AC   P11682;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-NOV-2023, entry version 85.
DE   RecName: Full=Apolipoprotein B;
DE   Flags: Fragment;
GN   Name=APOB;
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 [MRNA].
RX   PubMed=3436530; DOI=10.1016/0378-1119(87)90332-5;
RA   Kirchgessner T.G., Heinzmann C., Svenson K.L., Gordon D.A., Nicosia M.,
RA   Lebherz H.G., Lusis A.J., Williams D.L.;
RT   "Regulation of chicken apolipoprotein B: cloning, tissue distribution, and
RT   estrogen induction of mRNA.";
RL   Gene 59:241-251(1987).
CC   -!- FUNCTION: Apolipoprotein B is a major protein constituent of
CC       chylomicrons, VLDL and LDL. It functions as a recognition signal for
CC       the cellular binding and internalization of LDL particles by the apoB/E
CC       receptor.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
CC       Secreted {ECO:0000250|UniProtKB:P04114}. Lipid droplet
CC       {ECO:0000250|UniProtKB:P04114}.
CC   -!- INDUCTION: Within 24 hours after estradiol administration, APOB mRNA is
CC       increased five- to seven-fold in liver but is unchanged in intestine
CC       and kidney.
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DR   EMBL; M18421; AAA48595.1; -; mRNA.
DR   PIR; A29626; A29626.
DR   AlphaFoldDB; P11682; -.
DR   SMR; P11682; -.
DR   STRING; 9031.ENSGALP00000026550; -.
DR   GlyCosmos; P11682; 1 site, No reported glycans.
DR   PaxDb; 9031-ENSGALP00000026550; -.
DR   VEuPathDB; HostDB:geneid_396535; -.
DR   eggNOG; KOG4338; Eukaryota.
DR   InParanoid; P11682; -.
DR   PhylomeDB; P11682; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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.
DR   InterPro; IPR022176; ApoB100_C.
DR   PANTHER; PTHR13769; APOLIPOPROTEIN B; 1.
DR   PANTHER; PTHR13769:SF1; APOLIPOPROTEIN B-100; 1.
DR   Pfam; PF12491; ApoB100_C; 1.
PE   2: Evidence at transcript level;
KW   Cholesterol metabolism; Chylomicron; Cytoplasm; Glycoprotein;
KW   Heparin-binding; LDL; Lipid droplet; Lipid metabolism; Lipid transport;
KW   Reference proteome; Secreted; Steroid metabolism; Sterol metabolism;
KW   Transport; VLDL.
FT   CHAIN           <1..433
FT                   /note="Apolipoprotein B"
FT                   /id="PRO_0000064638"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   433 AA;  50848 MW;  FD8808C9CFF48925 CRC64;
     IPGLSEKYTG EELYLMTTEK AAKTADICLS KLQEYFDALI AAISELEVRV PASETILRGR
     NVLDQIKEML KHLQEKIRQT FVTLQEADFA GKLNRLKQVV QKTFQKAGNM VRSLQSKNFE
     DIKVQMQQLY KDAMASDYAH KLRSLAENVK KYISQIKNFS QKTLQKLSEN LQQLVLYIKA
     LREEYFDPTT LGWSVKYYEV EDKVLGLLKN LMDTLVIWYN EYAKDLSDLV TRLTDQVREL
     VENYRQEYYD LITDVEGKGR QKVMELSSAA QEKIRYWSAV AKRKINEHNR QVKAKLQEIY
     GQLSDSQEKL INVAKMLIDL TVEKYSTFMK YIFELLRWFE QATADSIKPY IAVREGELRI
     DVPFDWEYIN QMPQKSREAL RNKVELTRAL IQQGVEQGTR KWEEMQAFID EQLATEQLSF
     QQIVENIQKR MKT
//