GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]

 APOA1_MACFA             Reviewed;         267 AA.
P68292; P15568; P17929;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 1.
13-FEB-2019, entry version 65.
RecName: Full=Apolipoprotein A-I;
Short=Apo-AI;
Short=ApoA-I;
AltName: Full=Apolipoprotein A1;
Contains:
RecName: Full=Proapolipoprotein A-I;
Short=ProapoA-I;
Contains:
RecName: Full=Truncated apolipoprotein A-I;
Flags: Precursor;
Name=APOA1;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3106152; DOI=10.1016/0378-1119(86)90389-6;
Polites H.G., Melchior G.W., Castle C.K., Marotti K.R.;
"The primary structure of cynomolgus monkey apolipoprotein A-1 deduced
from the cDNA sequence: comparison to the human sequence.";
Gene 49:103-110(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1610902; DOI=10.1016/0167-4781(92)90079-F;
Murray R.W., Marotti K.R.;
"Nucleotide sequence of the cynomolgus monkey apolipoprotein A-I gene
and corresponding flanking regions.";
Biochim. Biophys. Acta 1131:207-210(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
PubMed=1917942;
Sorci-Thomas M., Kearns M.W.;
"Transcriptional regulation of the apolipoprotein A-I gene. Species-
specific expression correlates with rates of gene transcription.";
J. Biol. Chem. 266:18045-18050(1991).
[4]
PROTEIN SEQUENCE OF 25-48.
PubMed=3105581; DOI=10.1021/bi00379a037;
Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L.,
Kantor M.A., Nicolosi R.J., Shulman R.S.;
"Homologues of the human C and A apolipoproteins in the Macaca
fascicularis (cynomolgus) monkey.";
Biochemistry 26:1457-1463(1987).
-!- FUNCTION: Participates in the reverse transport of cholesterol
from tissues to the liver for excretion by promoting cholesterol
efflux from tissues and by acting as a cofactor for the lecithin
cholesterol acyltransferase (LCAT). As part of the SPAP complex,
activates spermatozoa motility.
-!- SUBUNIT: Interacts with APOA1BP and CLU. Component of a sperm
activating protein complex (SPAP), consisting of APOA1, an
immunoglobulin heavy chain, an immunoglobulin light chain and
albumin. Interacts with NDRG1. Interacts with SCGB3A2.
{ECO:0000250|UniProtKB:P02647}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
chylomicrons.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- PTM: Palmitoylated. {ECO:0000250}.
-!- PTM: Phosphorylation sites are present in the extracellular
medium. {ECO:0000250}.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M15411; AAA36834.1; -; mRNA.
EMBL; M83242; AAA36832.1; -; Genomic_DNA.
EMBL; M69223; AAA36831.1; -; Genomic_DNA.
PIR; A26529; A26529.
RefSeq; NP_001270674.1; NM_001283745.1.
RefSeq; XP_015290827.1; XM_015435341.1.
UniGene; Mfa.8179; -.
ProteinModelPortal; P68292; -.
SMR; P68292; -.
PRIDE; P68292; -.
Ensembl; ENSMFAT00000011499; ENSMFAP00000037249; ENSMFAG00000037868.
GeneID; 101925978; -.
KEGG; mcf:101925978; -.
CTD; 335; -.
GeneTree; ENSGT00530000063081; -.
HOVERGEN; HBG105708; -.
KO; K08757; -.
OrthoDB; 1553412at2759; -.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IEA:Ensembl.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IEA:Ensembl.
GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
GO; GO:0051180; P:vitamin transport; IEA:Ensembl.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 1.
1: Evidence at protein level;
Cholesterol metabolism; Direct protein sequencing; Glycoprotein; HDL;
Lipid metabolism; Lipid transport; Lipoprotein; Oxidation; Palmitate;
Phosphoprotein; Repeat; Secreted; Signal; Steroid metabolism;
Sterol metabolism; Transport.
SIGNAL 1 18
CHAIN 19 267 Proapolipoprotein A-I.
/FTId=PRO_0000425324.
CHAIN 25 267 Apolipoprotein A-I.
/FTId=PRO_0000001942.
CHAIN 25 266 Truncated apolipoprotein A-I.
{ECO:0000250}.
/FTId=PRO_0000416574.
REPEAT 68 89 1.
REPEAT 90 111 2.
REPEAT 112 122 3; half-length.
REPEAT 123 144 4.
REPEAT 145 166 5.
REPEAT 167 188 6.
REPEAT 189 210 7.
REPEAT 211 232 8.
REPEAT 233 243 9; half-length.
REPEAT 244 267 10.
REGION 68 267 10 X approximate tandem repeats.
MOD_RES 110 110 Methionine sulfoxide. {ECO:0000250}.
MOD_RES 136 136 Methionine sulfoxide. {ECO:0000250}.
CONFLICT 13 13 L -> P (in Ref. 1; AAA36834).
{ECO:0000305}.
SEQUENCE 267 AA; 30735 MW; 869955C024088E21 CRC64;
MKATVLTLAV LFLTGSQARH FWQQDEPPQT PWDRVKDLVT VYVEALKDSG KDYVSQFEGS
ALGKQLNLKL LDNWDSVTST VSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL HEGTRQKLHE LHEKLSPLGE EVRDRARAHV
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA SEHLSTLSEK AKPALEDLRQ
GLLPVLESFK VSFLSALEEY TKKLSTQ


Related products :

Catalog number Product name Quantity
E0604h ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
E0604h ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
E0604Rb ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
U0604Rb CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
E0604Rb ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Oryctolagus cuniculus,Rabbit 96T
U0604h CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Homo sapiens,Human 96T
E0604b ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Bos taurus,Bovine 96T
E0604m ELISA Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Mouse,Mus musculus 96T
E0604r ELISA Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Rat,Rattus norvegicus 96T
E0604r ELISA kit Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Rat,Rattus norvegicus 96T
E0604m ELISA kit Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Mouse,Mus musculus 96T
U0604r CLIA Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Rat,Rattus norvegicus 96T
U0604m CLIA Apoa1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Mouse,Mus musculus 96T
E0604b ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Bos taurus,Bovine 96T
U0604b CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Bos taurus,Bovine 96T
E0604p ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Pig,Sus scrofa 96T
E0604p ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Pig,Sus scrofa 96T
U0604p CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Pig,Sus scrofa 96T
U0604c CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Chicken,Gallus gallus 96T
E0604c ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Chicken,Gallus gallus 96T
E0604c ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Chicken,Gallus gallus 96T
E0604c ELISA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Canis familiaris,Canis lupus familiaris,Dog 96T
U0604c CLIA APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Canis familiaris,Canis lupus familiaris,Dog 96T
E0604c ELISA kit APOA1,Apo-AI,ApoA-I,Apolipoprotein A1,Apolipoprotein A-I,Canis familiaris,Canis lupus familiaris,Dog 96T
20-272-192023 Apolipoprotein J - Mouse monoclonal [Hs - 3] to Apolipoprotein J; Complement-associated protein SP-40.40; Complement cytolysis inhibitor; CLI; NA1_NA2; Apolipoprotein J; Apo-J; Testosterone-repressed 0.05 mg

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
No related Items

Related Genes :
[APOA1] Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I (Apolipoprotein A-I(1-242))]
[APOA2] Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II (Apolipoprotein A-II(1-76))]
[APOA5 RAP3 UNQ411/PRO773] Apolipoprotein A-V (Apo-AV) (ApoA-V) (Apolipoprotein A5) (Regeneration-associated protein 3)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Apoa4] Apolipoprotein A-IV (Apo-AIV) (ApoA-IV) (Apolipoprotein A4)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[cypB cyp102A3 yrhJ BSU27160] Bifunctional cytochrome P450/NADPH--P450 reductase 2 (CYP102A3) (Fatty acid hydroxylase CypB) (Flavocytochrome P450 102A3) [Includes: Cytochrome P450 102A3 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[ctxA toxA VC_1457] Cholera enterotoxin subunit A (Cholera enterotoxin, A chain) [Cleaved into: Cholera enterotoxin subunit A1 (EC 2.4.2.-) (Cholera enterotoxin A1 chain) (Cholera enterotoxin alpha chain) (NAD(+)--diphthamide ADP-ribosyltransferase); Cholera enterotoxin subunit A2 (Cholera enterotoxin A2 chain) (Cholera enterotoxin gamma chain)]
[APOC1] Apolipoprotein C-I (Apo-CI) (ApoC-I) (Apolipoprotein C1) [Cleaved into: Truncated apolipoprotein C-I]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[DGL DAL6 At1g05800 T20M3.6] Galactolipase DONGLE, chloroplastic (EC 3.1.1.26) (EC 3.1.1.32) (DAD1-like lipase 6) (Phospholipase A1 DONGLE) (Phospholipase A1-Ialpha1)
[iolA mmsA yxdA BSU39760 E83A] Malonate-semialdehyde dehydrogenase (MSA dehydrogenase) (EC 1.2.1.-) (Methylmalonate-semialdehyde dehydrogenase) (MMSA dehydrogenase) (MMSDH) (MSDH) (EC 1.2.1.27)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[pldA b3821 JW3794] Phospholipase A1 (EC 3.1.1.32) (EC 3.1.1.4) (Detergent-resistant phospholipase A) (DR-phospholipase A) (Outer membrane phospholipase A) (OM PLA) (OMPLA) (Phosphatidylcholine 1-acylhydrolase)
[PLA2G16 HRASLS3 HREV107] HRAS-like suppressor 3 (HRSL3) (EC 3.1.1.32) (EC 3.1.1.4) (Adipose-specific phospholipase A2) (AdPLA) (Group XVI phospholipase A1/A2) (H-rev 107 protein homolog) (H-REV107) (HREV107-1) (HRAS-like suppressor 1) (HREV107-3) (Renal carcinoma antigen NY-REN-65)
[Cryaa Crya1] Alpha-crystallin A chain [Cleaved into: Alpha-crystallin A(1-168); Alpha-crystallin A(1-165); Alpha-crystallin A(1-163); Alpha-crystallin A(1-162); Alpha-crystallin A(1-157); Alpha-crystallin A(1-156); Alpha-crystallin A(1-151)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[NAXE AIBP APOA1BP YJEFN1] NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (YjeF N-terminal domain-containing protein 1) (YjeF_N1)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

Bibliography :
?>