APOA2_CANLF
ID APOA2_CANLF Reviewed; 100 AA.
AC E2RAK7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Apolipoprotein A-II;
DE Short=Apo-AII;
DE Short=ApoA-II;
DE AltName: Full=Apolipoprotein A2;
DE Contains:
DE RecName: Full=Proapolipoprotein A-II;
DE Short=ProapoA-II;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-II;
DE AltName: Full=Apolipoprotein A-II(1-76);
DE Flags: Precursor;
GN Name=APOA2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
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 PROTEIN SEQUENCE OF 79-94, AND MASS SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=20483223; DOI=10.1016/j.cbd.2008.08.002;
RA Puppione D.L., Bassilian S., Souda P., MacDonald M.H., Halgand F.,
RA Hagland F., Whitelegge J.P.;
RT "Mass spectral analysis of the apolipoproteins on dog (Canis lupus
RT familiaris) high density lipoproteins. Detection of apolipoprotein A-II.";
RL Comp. Biochem. Physiol. 3:290-296(2008).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC -!- SUBUNIT: Monomer. Interacts with NAXE and NDRG1 (By similarity).
CC {ECO:0000250|UniProtKB:P02652}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=8681.5;
CC Mass_error=0.354; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20483223};
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR EMBL; AAEX03018445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001300728.1; NM_001313799.1.
DR AlphaFoldDB; E2RAK7; -.
DR SMR; E2RAK7; -.
DR STRING; 9612.ENSCAFP00000018988; -.
DR PaxDb; E2RAK7; -.
DR PRIDE; E2RAK7; -.
DR Ensembl; ENSCAFT00030036082; ENSCAFP00030031475; ENSCAFG00030019630.
DR Ensembl; ENSCAFT00030036201; ENSCAFP00030031579; ENSCAFG00030019630.
DR Ensembl; ENSCAFT00845051946; ENSCAFP00845040756; ENSCAFG00845029343.
DR GeneID; 478982; -.
DR KEGG; cfa:478982; -.
DR CTD; 336; -.
DR VEuPathDB; HostDB:ENSCAFG00845029343; -.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR GeneTree; ENSGT00390000003306; -.
DR HOGENOM; CLU_157351_0_0_1; -.
DR InParanoid; E2RAK7; -.
DR OMA; LTICSFE; -.
DR OrthoDB; 1612564at2759; -.
DR TreeFam; TF338165; -.
DR Reactome; R-CFA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CFA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-CFA-8963888; Chylomicron assembly.
DR Reactome; R-CFA-975634; Retinoid metabolism and transport.
DR Proteomes; UP000002254; Chromosome 38.
DR Bgee; ENSCAFG00000012886; Expressed in liver and 32 other tissues.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IEA:Ensembl.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
DR GO; GO:0060695; P:negative regulation of cholesterol transporter activity; IEA:Ensembl.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0060192; P:negative regulation of lipase activity; IBA:GO_Central.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0018206; P:peptidyl-methionine modification; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR006801; ApoA-II.
DR InterPro; IPR036172; ApoA-II_sf.
DR PANTHER; PTHR11027; PTHR11027; 1.
DR Pfam; PF04711; ApoA-II; 1.
DR SUPFAM; SSF82936; SSF82936; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing; HDL;
KW Lipid transport; Oxidation; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..100
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425726"
FT CHAIN 24..100
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:20483223"
FT /id="PRO_0000425727"
FT CHAIN 24..99
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT /id="PRO_0000425728"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02652"
SQ SEQUENCE 100 AA; 11225 MW; DBA661E8FDFAE188 CRC64;
MKLLAVTVLL LVICSLEGAF VRRQAEEPNL QSLVSQYFQT VTDYGKDLME KAKGPELQAQ
AKAYFEKTQE QLTPLVKKAG TDLLNFLSNF MDLKTQPATQ
