APOA4_CANLF
ID APOA4_CANLF Reviewed; 378 AA.
AC E2RE76;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Apolipoprotein A-IV {ECO:0000250|UniProtKB:P06727};
DE Short=Apo-AIV;
DE Short=ApoA-IV;
DE AltName: Full=Apolipoprotein A4 {ECO:0000250|UniProtKB:P06727};
DE Flags: Precursor;
GN Name=APOA4 {ECO:0000250|UniProtKB:P06727};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|EMBL:AAEX03003469};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|EMBL:AAEX03003469};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (AUG-2014).
CC -!- FUNCTION: May have a role in chylomicrons and VLDL secretion and
CC catabolism. Required for efficient activation of lipoprotein lipase by
CC ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL
CC and chylomicrons. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06727}.
CC -!- DOMAIN: Nine of the thirteen 22-amino acid tandem repeats (each 22-mer
CC is actually a tandem array of two, A and B, related 11-mers) occurring
CC in this sequence are predicted to be highly alpha-helical, and many of
CC these helices are amphipathic. They may therefore serve as lipid-
CC binding domains with lecithin:cholesterol acyltransferase (LCAT)
CC activating abilities. {ECO:0000250|UniProtKB:P06727}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; AAEX03003469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E2RE76; -.
DR SMR; E2RE76; -.
DR STRING; 9612.ENSCAFP00000019615; -.
DR PaxDb; E2RE76; -.
DR PRIDE; E2RE76; -.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR HOGENOM; CLU_058447_0_0_1; -.
DR InParanoid; E2RE76; -.
DR OMA; KGHLTPY; -.
DR TreeFam; TF334458; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0034364; C:high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 2.
PE 3: Inferred from homology;
KW Chylomicron; HDL; Lipid transport; Reference proteome; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..378
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000430569"
FT REPEAT 33..54
FT /note="1"
FT REPEAT 60..81
FT /note="2"
FT REPEAT 82..98
FT /note="3"
FT REPEAT 110..130
FT /note="4"
FT REPEAT 131..152
FT /note="5"
FT REPEAT 153..174
FT /note="6"
FT REPEAT 175..196
FT /note="7"
FT REPEAT 197..218
FT /note="8"
FT REPEAT 219..240
FT /note="9"
FT REPEAT 241..262
FT /note="10"
FT REPEAT 263..280
FT /note="11"
FT REPEAT 281..302
FT /note="12"
FT REPEAT 303..324
FT /note="13"
FT REGION 33..324
FT /note="13 X 22 AA approximate tandem repeats"
FT REGION 354..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 42536 MW; 8471FBC9E8F8ED41 CRC64;
MFLKAVVLTL SLVAITGARA EVSADQVATV VWDYFSQLSN NAKEAVEHLQ QSELTQQLKS
VTKGHISALR VIEKGRERNS WEHSRRVGPC EIMGRQVGIF GQPLRVATLP NCDLPVNSVP
PNTHLSQAVG PYAEELRTQV NTHAEQLRNQ LTSHAQRMQS ALRQNVDDLH SSLTPFADEL
KAKIDQNVEE LKGHLTPYTD ELKVKIDQNV EELRRSLAPY AQDVQEKLNH QLEGLAFQMK
KNAEELKAKI SANAEELRQR LAPVAEDVRG KLKDNTAGLH KSLAELSSRL DQQVEEFRRN
VGPYGETFNK ALLQQVEELR QKLGPYAGDM EDHLSFLEKD LRDKVNSFFS TLQEKESQDT
PVALPKQEQE QSAVPLES
