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Protein lin-28 homolog A (Lin-28A) (Testis-expressed protein 17)

 LN28A_MOUSE             Reviewed;         209 AA.
Q8K3Y3; Q6NV62;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
08-MAY-2019, entry version 139.
RecName: Full=Protein lin-28 homolog A;
AltName: Full=Testis-expressed protein 17;
Name=Lin28a; Synonyms=Lin28, Tex17;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
PubMed=12798299; DOI=10.1016/S0012-1606(03)00126-X;
Moss E.G., Tang L.;
"Conservation of the heterochronic regulator Lin-28, its developmental
expression and microRNA complementary sites.";
Dev. Biol. 258:432-442(2003).
Moss E.G., Tang L.;
Dev. Biol. 262:361-361(2003).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
PubMed=11279525; DOI=10.1038/86927;
Wang P.J., McCarrey J.R., Yang F., Page D.C.;
"An abundance of X-linked genes expressed in spermatogonia.";
Nat. Genet. 27:422-426(2001).
PubMed=14643679; DOI=10.1016/S1567-133X(03)00140-6;
Yang D.-H., Moss E.G.;
"Temporally regulated expression of Lin-28 in diverse tissues of the
developing mouse.";
Gene Expr. Patterns 3:719-726(2003).
PubMed=15003116; DOI=10.1186/gb-2004-5-3-r13;
Sempere L.F., Freemantle S., Pitha-Rowe I., Moss E.G., Dmitrovsky E.,
Ambros V.;
"Expression profiling of mammalian microRNAs uncovers a subset of
brain-expressed microRNAs with possible roles in murine and human
neuronal differentiation.";
Genome Biol. 5:R13.1-R13.11(2004).
PubMed=15722555; DOI=10.1074/jbc.M412247200;
Lee Y.S., Kim H.K., Chung S., Kim K.-S., Dutta A.;
"Depletion of human micro-RNA miR-125b reveals that it is critical for
the proliferation of differentiated cells but not for the down-
regulation of putative targets during differentiation.";
J. Biol. Chem. 280:16635-16641(2005).
PubMed=16227573; DOI=10.1128/MCB.25.21.9198-9208.2005;
Wu L., Belasco J.G.;
"Micro-RNA regulation of the mammalian lin-28 gene during neuronal
differentiation of embryonal carcinoma cells.";
Mol. Cell. Biol. 25:9198-9208(2005).
GLY-119; PRO-124; 138-ARG-CYS-139 AND CYS-142.
PubMed=17473174; DOI=10.1101/gad.415007;
Polesskaya A., Cuvellier S., Naguibneva I., Duquet A., Moss E.G.,
Harel-Bellan A.;
"Lin-28 binds IGF-2 mRNA and participates in skeletal myogenesis by
increasing translation efficiency.";
Genes Dev. 21:1125-1138(2007).
PubMed=18604195; DOI=10.1038/ncb1759;
Rybak A., Fuchs H., Smirnova L., Brandt C., Pohl E.E., Nitsch R.,
Wulczyn F.G.;
"A feedback loop comprising lin-28 and let-7 controls pre-let-7
maturation during neural stem-cell commitment.";
Nat. Cell Biol. 10:987-993(2008).
PubMed=18566191; DOI=10.1261/rna.1155108;
Newman M.A., Thomson J.M., Hammond S.M.;
"Lin-28 interaction with the Let-7 precursor loop mediates regulated
microRNA processing.";
RNA 14:1539-1549(2008).
PubMed=18292307; DOI=10.1126/science.1154040;
Viswanathan S.R., Daley G.Q., Gregory R.I.;
"Selective blockade of microRNA processing by Lin28.";
Science 320:97-100(2008).
PubMed=19703396; DOI=10.1016/j.cell.2009.08.002;
Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H.,
Han J., Kim V.N.;
"TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through
pre-microRNA uridylation.";
Cell 138:696-708(2009).
PubMed=23102813; DOI=10.1016/j.cell.2012.10.019;
Cho J., Chang H., Kwon S.C., Kim B., Kim Y., Choe J., Ha M., Kim Y.K.,
Kim V.N.;
"LIN28A is a suppressor of ER-associated translation in embryonic stem
Cell 151:765-777(2012).
PubMed=24209617; DOI=10.1016/j.cell.2013.09.059;
Shyh-Chang N., Zhu H., Yvanka de Soysa T., Shinoda G., Seligson M.T.,
Tsanov K.M., Nguyen L., Asara J.M., Cantley L.C., Daley G.Q.;
"Lin28 enhances tissue repair by reprogramming cellular metabolism.";
Cell 155:778-792(2013).
PubMed=26045559; DOI=10.1074/jbc.M115.665521;
O'Day E., Le M.T., Imai S., Tan S.M., Kirchner R., Arthanari H.,
Hofmann O., Wagner G., Lieberman J.;
"An RNA-binding Protein, Lin28, Recognizes and Remodels G-quartets in
the MicroRNAs (miRNAs) and mRNAs It Regulates.";
J. Biol. Chem. 290:17909-17922(2015).
OF 139-CYS--CYS-142 AND 161-CYS--CYS-164.
PubMed=28671666; DOI=10.1038/nsmb.3428;
Faehnle C.R., Walleshauser J., Joshua-Tor L.;
"Multi-domain utilization by TUT4 and TUT7 in control of let-7
Nat. Struct. Mol. Biol. 24:658-665(2017).
PubMed=22078496; DOI=10.1016/j.cell.2011.10.020;
Nam Y., Chen C., Gregory R.I., Chou J.J., Sliz P.;
"Molecular basis for interaction of let-7 microRNAs with Lin28.";
Cell 147:1080-1091(2011).
-!- FUNCTION: RNA-binding protein that inhibits processing of pre-let-
7 miRNAs and regulates translation of mRNAs that control
developmental timing, pluripotency and metabolism
(PubMed:17473174, PubMed:18604195, PubMed:18566191,
PubMed:18292307, PubMed:19703396, PubMed:23102813,
PubMed:24209617). Seems to recognize a common structural G-quartet
(G4) feature in its miRNA and mRNA targets (PubMed:26045559).
'Translational enhancer' that drives specific mRNAs to polysomes
and increases the efficiency of protein synthesis. Its association
with the translational machinery and target mRNAs results in an
increased number of initiation events per molecule of mRNA and,
indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA,
ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for
skeletal muscle differentiation program through the translational
up-regulation of IGF2 expression (PubMed:17473174). Suppressor of
microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-
143 and miR-200c. Specifically binds the miRNA precursors (pre-
miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA
terminal loop, and recruits TUT4 and TUT7 uridylyltransferaseS.
This results in the terminal uridylation of target pre-miRNAs.
Uridylated pre-miRNAs fail to be processed by Dicer and undergo
degradation. The repression of let-7 expression is required for
normal development and contributes to maintain the pluripotent
state by preventing let-7-mediated differentiation of embryonic
stem cells (PubMed:19703396, PubMed:28671666). Localized to the
periendoplasmic reticulum area, binds to a large number of spliced
mRNAs and inhibits the translation of mRNAs destined for the ER,
reducing the synthesis of transmembrane proteins, ER or Golgi
lumen proteins, and secretory proteins (PubMed:23102813). Binds to
and enhances the translation of mRNAs for several metabolic
enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and
oxidative phosphorylation. Which, with the let-7 repression may
enhance tissue repair in adult tissue (PubMed:24209617).
{ECO:0000269|PubMed:17473174, ECO:0000269|PubMed:18292307,
ECO:0000269|PubMed:18566191, ECO:0000269|PubMed:18604195,
ECO:0000269|PubMed:19703396, ECO:0000269|PubMed:23102813,
ECO:0000269|PubMed:24209617, ECO:0000269|PubMed:26045559,
-!- SUBUNIT: Monomer (PubMed:22078496). During skeletal muscle
differentiation, associated with translation initiation complexes
in the polysomal compartment (By similarity). Directly interacts
with EIF3S2 (PubMed:17473174). Interacts with NCL in an RNA-
dependent manner (By similarity). Interacts with TUT4 in the
presence of pre-let-7 RNA (PubMed:28671666). {ECO:0000250,
ECO:0000250|UniProtKB:Q9H9Z2, ECO:0000269|PubMed:17473174,
ECO:0000269|PubMed:22078496, ECO:0000269|PubMed:28671666}.
Q8CI75:Dis3l2; NbExp=2; IntAct=EBI-11109197, EBI-16045218;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12798299,
ECO:0000269|PubMed:17473174}. Rough endoplasmic reticulum
{ECO:0000269|PubMed:23102813}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:Q9H9Z2}. Cytoplasm, Stress granule
{ECO:0000269|PubMed:17473174}. Nucleus, nucleolus
{ECO:0000269|PubMed:17473174}. Note=Predominantly cytoplasmic
(PubMed:12798299). In the cytoplasm, localizes to peri-endoplasmic
reticulum regions and detected in the microsomal fraction derived
from rough endoplasmic reticulum (RER) following subcellular
fractionation. May be bound to the cytosolic surface of RER on
which ER-associated mRNAs are translated (PubMed:23102813).
Shuttle from the nucleus to the cytoplasm requires RNA-binding
(PubMed:17473174). Nucleolar localization observed in 10-15% of
the nuclei in differentiated myotubes (PubMed:17473174).
{ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:17473174,
-!- TISSUE SPECIFICITY: Expressed in embryonic stem cells (ES cells),
spermatagonia and testis. Expressed in numerous epithelial tissues
including the epithelia of the small intestine, the intralobular
duct epithelium of the mammary gland and the epithelia of Henle's
loop in the kidney and in the collecting duct (at protein level).
Also expressed in the myocardium and skeletal muscle (at protein
level). {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:12798299,
ECO:0000269|PubMed:14643679, ECO:0000269|PubMed:15722555}.
-!- DEVELOPMENTAL STAGE: Strongly expressed throughout the whole
embryo at 6.5 dpc, including the embryonic and extraembryonic
ectoderm and endoderm (at protein level). Subsequently expressed
in the ectoderm, endoderm and mesoderm at 7.5 dpc (at protein
level). At 9.5 dpc, expressed in epithelia covering the first
branchial arch and the coelomic cavity, the myocardium of the
developing heart, the neuroepithelium and some extraembryonic
tissues such as the visceral yolk sac (at protein level).
Expression persists in a variety of epithelial tissues at 10.5
dpc. At 15.5 dpc, expression is lost in bronchial epithelium and
becomes weaker in neuroepithelium, while increasing in the myotome
of somites, the foregut epithelium, stratified epithelium and some
kidney tubules (at protein level). At 17.5 dpc, expression
persists in the myocardium and in the epithelium covering the body
surface and skeletal muscles (at protein level). Expression is
reduced during differentiation of ES cells. In adult primary
myoblasts, barely detectable during proliferation, but
dramatically up-regulated during terminal differentiation. Induced
as early as 24 hours after differentiation signal and remains high
as late as 7 days of differentiation. Little expression in resting
muscle, but strongly up-regulated during regeneration of skeletal
muscle fibers. Expression decreases when regeneration is
histologically and functionally complete.
{ECO:0000269|PubMed:12798299, ECO:0000269|PubMed:14643679,
ECO:0000269|PubMed:15722555, ECO:0000269|PubMed:17473174}.
-!- INDUCTION: Negatively regulated by the microRNA miR-125b in
response to retinoic acid. {ECO:0000269|PubMed:15003116,
-!- DOMAIN: The CSD domain is required for function in muscle
differentiation. {ECO:0000269|PubMed:22078496}.
-!- DOMAIN: The CCHC zinc fingers interact with the GGAG motif at the
3' end of let-7 miRNAs precursors, more generally they bind the
5'-NGNNG-3' consensus motif with micromolar affinity. The CSD
domain recognizes the loop at the 5' end. The flexible linker
allows accommodating variable sequences and lengths among let-7
family members. {ECO:0000269|PubMed:22078496,
-!- MISCELLANEOUS: Reactivation of LIN28A expression enhances tissue
repair in some adult tissues by reprogramming cellular
bioenergetics. Improves hair regrowth by promoting anagen in hair
follicle and accelerates regrowth of cartilage, bone and
mesenchyme after ear and digit injuries.
-!- SIMILARITY: Belongs to the lin-28 family. {ECO:0000305}.
Copyrighted by the UniProt Consortium, see
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AF521097; AAM77749.1; -; mRNA.
EMBL; BC068304; AAH68304.1; -; mRNA.
CCDS; CCDS18761.1; -.
RefSeq; NP_665832.1; NM_145833.1.
PDB; 3TRZ; X-ray; 2.90 A; A/B/C/D/E/F=31-187.
PDB; 3TS0; X-ray; 2.76 A; A/B=33-187.
PDB; 3TS2; X-ray; 2.01 A; A/B=31-187.
PDBsum; 3TRZ; -.
PDBsum; 3TS0; -.
PDBsum; 3TS2; -.
SMR; Q8K3Y3; -.
BioGrid; 219943; 8.
DIP; DIP-48573N; -.
IntAct; Q8K3Y3; 17.
STRING; 10090.ENSMUSP00000050488; -.
iPTMnet; Q8K3Y3; -.
PhosphoSitePlus; Q8K3Y3; -.
MaxQB; Q8K3Y3; -.
PaxDb; Q8K3Y3; -.
PeptideAtlas; Q8K3Y3; -.
PRIDE; Q8K3Y3; -.
Ensembl; ENSMUST00000051674; ENSMUSP00000050488; ENSMUSG00000050966.
GeneID; 83557; -.
KEGG; mmu:83557; -.
UCSC; uc008vdw.1; mouse.
CTD; 79727; -.
MGI; MGI:1890546; Lin28a.
eggNOG; KOG3070; Eukaryota.
eggNOG; COG1278; LUCA.
GeneTree; ENSGT00940000153295; -.
HOGENOM; HOG000047091; -.
InParanoid; Q8K3Y3; -.
KO; K18754; -.
OrthoDB; 1604809at2759; -.
PhylomeDB; Q8K3Y3; -.
TreeFam; TF316240; -.
PRO; PR:Q8K3Y3; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000050966; Expressed in 77 organ(s), highest expression level in epiblast (generic).
ExpressionAtlas; Q8K3Y3; baseline and differential.
Genevisible; Q8K3Y3; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0005844; C:polysome; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0002151; F:G-quadruplex RNA binding; IDA:UniProtKB.
GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071333; P:cellular response to glucose stimulus; IMP:BHF-UCL.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0010587; P:miRNA catabolic process; IMP:UniProtKB.
GO; GO:0010586; P:miRNA metabolic process; IDA:MGI.
GO; GO:0045686; P:negative regulation of glial cell differentiation; IDA:MGI.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:1901724; P:positive regulation of cell proliferation involved in kidney development; IMP:BHF-UCL.
GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0032008; P:positive regulation of TOR signaling; IDA:BHF-UCL.
GO; GO:0045727; P:positive regulation of translation; IDA:MGI.
GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IGI:MGI.
GO; GO:0031123; P:RNA 3'-end processing; ISO:MGI.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISO:MGI.
CDD; cd04458; CSP_CDS; 1.
InterPro; IPR011129; CSD.
InterPro; IPR002059; CSP_DNA-bd.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00313; CSD; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00357; CSP; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS51857; CSD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H9Z2}.
CHAIN 2 209 Protein lin-28 homolog A.
DOMAIN 39 112 CSD.
ZN_FING 137 154 CCHC-type 1. {ECO:0000255|PROSITE-
ZN_FING 159 176 CCHC-type 2. {ECO:0000255|PROSITE-
REGION 113 136 Flexible linker.
MOD_RES 2 2 N-acetylglycine.
MOD_RES 3 3 Phosphoserine.
MOD_RES 120 120 Phosphoserine.
MOD_RES 200 200 Phosphoserine.
MUTAGEN 42 42 G->S: Erroneous subcellular location. No
positive effect on terminal myogenic
MUTAGEN 44 47 Missing: Erroneous subcellular location.
No positive effect on terminal myogenic
MUTAGEN 81 81 M->I: Erroneous subcellular location;
when associated with Q-85. No positive
effect on terminal myogenic
differentiation; when associated with Q-
85. {ECO:0000269|PubMed:17473174}.
MUTAGEN 85 85 R->Q: Erroneous subcellular location;
when associated with I-81. No positive
effect on terminal myogenic
differentiation; when associated with I-
81. {ECO:0000269|PubMed:17473174}.
MUTAGEN 119 119 G->R: Erroneous subcellular location;
when associated with S-124. No positive
effect on terminal myogenic
differentiation; when associated with S-
124. {ECO:0000269|PubMed:17473174}.
MUTAGEN 124 124 P->S: Erroneous subcellular location;
when associated with R-119. No positive
effect on terminal myogenic
differentiation; when associated with R-
119. {ECO:0000269|PubMed:17473174}.
MUTAGEN 138 139 Missing: No effect on subcellular
location; when associated with S-142.
Normal terminal myogenic differentiation;
when associated with S-142.
MUTAGEN 139 142 CYNC->AYNA: Disrupts 5'-GGAG-3' motif
interaction. Disrupts oligoU-addition to
pre-miRNA pre-let-7 by TUT4.
MUTAGEN 142 142 C->S: No effect on subcellular location;
when associated with 44-C--F-47. Normal
terminal myogenic differentiation; when
associated with 44-C--F-47.
MUTAGEN 161 164 CHFC->AHFA: Disrupts 5'-GGAG-3' motif
interaction. Binds miRNA but not TUT4.
CONFLICT 194 194 E -> D (in Ref. 3; AAH68304).
STRAND 38 48 {ECO:0000244|PDB:3TS2}.
TURN 49 52 {ECO:0000244|PDB:3TS2}.
STRAND 53 61 {ECO:0000244|PDB:3TS2}.
STRAND 64 75 {ECO:0000244|PDB:3TS2}.
HELIX 76 78 {ECO:0000244|PDB:3TS2}.
STRAND 81 84 {ECO:0000244|PDB:3TS2}.
STRAND 92 100 {ECO:0000244|PDB:3TS2}.
STRAND 103 111 {ECO:0000244|PDB:3TS2}.
HELIX 112 114 {ECO:0000244|PDB:3TS2}.
TURN 124 126 {ECO:0000244|PDB:3TS0}.
TURN 140 142 {ECO:0000244|PDB:3TS2}.
HELIX 149 151 {ECO:0000244|PDB:3TS2}.
TURN 162 164 {ECO:0000244|PDB:3TS2}.
HELIX 171 173 {ECO:0000244|PDB:3TS2}.
TURN 175 178 {ECO:0000244|PDB:3TS2}.
SEQUENCE 209 AA; 22720 MW; 4BD14DCAF13CD659 CRC64;

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WP346: Protein Modifications
WP1493: Carbon assimilation C4 pathway
WP1909: Signal regulatory protein (SIRP) family interactions
WP210: Cytoplasmic Ribosomal Proteins
WP1676: Non-homologous end-joining
WP73: G Protein Signaling Pathways
WP1566: Citrate cycle (TCA cycle)
WP931: G Protein Signaling Pathways
WP1624: Bacterial secretion system
WP2203: TSLP Signaling Pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1693: Purine metabolism
WP1650: Fluorobenzoate degradation
WP2292: Chemokine signaling pathway
WP1659: Glycine, serine and threonine metabolism

Related Genes :
[Lin28a Lin28 Tex17] Protein lin-28 homolog A (Lin-28A) (Testis-expressed protein 17)
[LIN28A CSDD1 LIN28 ZCCHC1] Protein lin-28 homolog A (Lin-28A) (Zinc finger CCHC domain-containing protein 1)
[lin28a lin28 si:ch211-232d9.4 zgc:55584] Protein lin-28 homolog A (Lin-28A)
[lin28a lin28] Protein lin-28 homolog A (Lin-28A)
[LIN7A MALS1 VELI1] Protein lin-7 homolog A (Lin-7A) (hLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Tax interaction protein 33) (TIP-33) (Vertebrate lin-7 homolog 1) (Veli-1)
[LIN28A LIN28] Protein lin-28 homolog A (Lin-28A)
[lin28a lin28 TGas109o22.1] Protein lin-28 homolog A (Lin-28A)
[Lin7a Mals1 Veli1] Protein lin-7 homolog A (Lin-7A) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1)
[Lin7c Mals3 Veli3] Protein lin-7 homolog C (Lin-7C) (mLin7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[LIN7B MALS2 VELI2 UNQ3116/PRO10200] Protein lin-7 homolog B (Lin-7B) (hLin7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) (hVeli2)
[Lin7a Mals1 Veli1] Protein lin-7 homolog A (Lin-7A) (mLin-7) (Mammalian lin-seven protein 1) (MALS-1) (Vertebrate lin-7 homolog 1) (Veli-1)
[Lin7b Mals2 Veli1a Veli2] Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2)
[CDK1 CDC2 CDC28A CDKN1 P34CDC2] Cyclin-dependent kinase 1 (CDK1) (EC (EC (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[LIN7C MALS3 VELI3] Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[] 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 (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC; Protease 3C (P3C); RNA-directed RNA polymerase (RdRp) (EC (3D polymerase) (3Dpol) (Protein 3D) (3D)] (Fragment)
[Lin7c Mals3 Veli3] Protein lin-7 homolog C (Lin-7C) (Mammalian lin-seven protein 3) (MALS-3) (Vertebrate lin-7 homolog 3) (Veli-3)
[Lin7b Mals2 Veli2] Protein lin-7 homolog B (Lin-7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2)
[lin-35 C32F10.2] Retinoblastoma-like protein homolog lin-35 (Abnormal cell lineage protein 35) (Synthetic multivulva protein lin-35)
[SLC28A3 CNT3] Solute carrier family 28 member 3 (Concentrative Na(+)-nucleoside cotransporter 3) (CNT 3) (hCNT3)
[CASK LIN2] Peripheral plasma membrane protein CASK (hCASK) (EC (Calcium/calmodulin-dependent serine protein kinase) (Protein lin-2 homolog)
[SLC28A2 CNT2] Sodium/nucleoside cotransporter 2 (Concentrative nucleoside transporter 2) (CNT 2) (hCNT2) (Na(+)/nucleoside cotransporter 2) (Sodium-coupled nucleoside transporter 2) (Sodium/purine nucleoside co-transporter) (SPNT) (Solute carrier family 28 member 2)
[LIN54 CXCDC1 KIAA2037] Protein lin-54 homolog (CXC domain-containing protein 1)
[lin-10 C09H6.2] Protein lin-10 (Abnormal cell lineage protein 10)
[Trim71 Gm1127 Lin41] E3 ubiquitin-protein ligase TRIM71 (EC (Protein lin-41 homolog) (mLin41) (RING-type E3 ubiquitin transferase TRIM71) (Tripartite motif-containing protein 71)
[lin-42 F47F6.1] Period protein homolog lin-42 (Abnormal cell lineage protein 42)
[SLC28A1 CNT1] Sodium/nucleoside cotransporter 1 (Concentrative nucleoside transporter 1) (CNT 1) (hCNT1) (Na(+)/nucleoside cotransporter 1) (Sodium-coupled nucleoside transporter 1) (Solute carrier family 28 member 1)
[Mbl2] Mannose-binding protein C (MBP-C) (Mannan-binding protein) (RA-reactive factor P28A subunit) (RARF/P28A)
[SETTUDRAFT_30757] E3 ubiquitin-protein ligase (EC
[mip120 CG6061] Protein lin-54 homolog (Myb complex protein of 120 kDa)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

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