APOB_CHICK
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 03-AUG-2022, entry version 82.
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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18421; AAA48595.1; -; mRNA.
DR PIR; A29626; A29626.
DR AlphaFoldDB; P11682; -.
DR SMR; P11682; -.
DR STRING; 9031.ENSGALP00000026550; -.
DR PaxDb; P11682; -.
DR VEuPathDB; HostDB:geneid_396535; -.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; P11682; -.
DR PhylomeDB; P11682; -.
DR Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0034359; C:mature chylomicron; IBA:GO_Central.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central.
DR GO; GO:0006642; P:triglyceride mobilization; IBA:GO_Central.
DR InterPro; IPR022176; ApoB100_C.
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