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Ankyrin repeat domain-containing protein 17 (Ankyrin repeat domain-containing protein FOE) (Gene trap ankyrin repeat protein)

 ANR17_MOUSE             Reviewed;        2603 AA.
Q99NH0; Q3TV99; Q5F4T7; Q6PG69; Q6ZQ66; Q8CHT4;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 2.
12-SEP-2018, entry version 133.
RecName: Full=Ankyrin repeat domain-containing protein 17;
AltName: Full=Ankyrin repeat domain-containing protein FOE;
AltName: Full=Gene trap ankyrin repeat protein;
Name=Ankrd17; Synonyms=Foe, Gtar, Kiaa0697;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Chen X., Shen J.C.-K.;
"A novel ankyrin repeat domain-containing protein.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING,
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
PubMed=11165478; DOI=10.1016/S0925-4773(00)00530-X;
Watt A.J., Jones E.A., Ure J.M., Peddie D., Wilson D.I.,
Forrester L.M.;
"A gene trap integration provides an early in situ marker for hepatic
specification of the foregut endoderm.";
Mech. Dev. 100:205-215(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1034-1482 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2603 (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1902-2603 (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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).
[7]
TISSUE SPECIFICITY.
PubMed=11740861; DOI=10.1006/excr.2001.5396;
Jones E.A., Tosh D., Wilson D.I., Lindsay S., Forrester L.M.;
"Hepatic differentiation of murine embryonic stem cells.";
Exp. Cell Res. 272:15-22(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2043, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19619540; DOI=10.1016/j.febslet.2009.07.025;
Hou S.C., Chan L.W., Chou Y.C., Su C.Y., Chen X., Shih Y.L.,
Tsai P.C., Shen C.K., Yan Y.T.;
"Ankrd17, an ubiquitously expressed ankyrin factor, is essential for
the vascular integrity during embryogenesis.";
FEBS Lett. 583:2765-2771(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-42; SER-1692;
SER-1696; SER-1705; SER-2040; SER-2041; SER-2043; SER-2055 AND
SER-2401, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1870, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Could play pivotal roles in cell cycle and DNA
regulation. Involved in innate immune defense against viruse by
positively regulating the viral dsRNA receptors DDX58 and IFIH1
signaling pathways. Involves in NOD2- and NOD1-mediated responses
to bacteria suggesting a role in innate antibacterial immune
pathways too. Could play a central role for the formation and/or
maintenance of the blood vessels of the circulation system
(PubMed:19619540). {ECO:0000250|UniProtKB:O75179,
ECO:0000269|PubMed:19619540}.
-!- SUBUNIT: Interacts (via N-terminus) with NOD2. Interacts with
CDK2, MCM3, MCM5, MCM7, CDC6 and PCNA. Interacts with MAVS and
IFIH1. Interacts (via the second ankyrin repeat cluster) with
DDX58. {ECO:0000250|UniProtKB:O75179}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75179}.
Nucleus {ECO:0000250|UniProtKB:O75179}. Note=Detected around the
nucleolus. {ECO:0000250|UniProtKB:O75179}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=The N-terminus of another isoform lacking the first 141
amino acids is described in. {ECO:0000269|PubMed:11165478};
Name=1;
IsoId=Q99NH0-1; Sequence=Displayed;
Name=2;
IsoId=Q99NH0-2; Sequence=VSP_028866, VSP_028867, VSP_028871;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q99NH0-3; Sequence=VSP_028868, VSP_028869, VSP_028870;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in fetal liver. Detected in
adult liver cells, ovarian oocytes, seminiferous tubules of the
testes and pelvic region of the kidney. It was not detected in
heart, gut, lung, spleen and skeletal muscle. Earliest specific in
situ marker of hepatic differentiation during embryogenesis,
useful for characterization of inductive events involved in
hepatic specification. {ECO:0000269|PubMed:11165478,
ECO:0000269|PubMed:11740861, ECO:0000269|PubMed:19619540}.
-!- DEVELOPMENTAL STAGE: Expressed at 8.0-8.5 dpc in the foregut
endoderm and at 9.5 dpc in cells migrating into the septum
transversum. At 10.5 dpc, highly expressed exclusively in the
fetal liver. From 10.5 dpc, expressed in the developing liver
throughout gestation and in neonates. At 17.5 dpc, detected in the
dorsal root ganglia of the peripheral nervous system.
{ECO:0000269|PubMed:11165478}.
-!- PTM: Phosphorylated by CDK2. {ECO:0000250|UniProtKB:O75179}.
-!- DISRUPTION PHENOTYPE: Deficient mice display embryonic lethality
during organogenesis with hemorrhages, impaired vascular smooth
muscle cell development, impaired vascular integrity and growth
retardation. {ECO:0000269|PubMed:19619540}.
-!- SEQUENCE CAUTION:
Sequence=AAH39213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC98003.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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EMBL; AF130371; AAQ13559.1; -; mRNA.
EMBL; AC117578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY026253; AAK07672.1; -; mRNA.
EMBL; AK160263; BAE35720.1; -; mRNA.
EMBL; AK129193; BAC98003.1; ALT_SEQ; Transcribed_RNA.
EMBL; BC039213; AAH39213.1; ALT_INIT; mRNA.
EMBL; BC057195; AAH57195.1; -; mRNA.
CCDS; CCDS57354.1; -. [Q99NH0-1]
RefSeq; NP_112148.2; NM_030886.2. [Q99NH0-1]
UniGene; Mm.245522; -.
UniGene; Mm.441490; -.
ProteinModelPortal; Q99NH0; -.
SMR; Q99NH0; -.
BioGrid; 219887; 5.
IntAct; Q99NH0; 5.
MINT; Q99NH0; -.
STRING; 10090.ENSMUSP00000014421; -.
iPTMnet; Q99NH0; -.
PhosphoSitePlus; Q99NH0; -.
EPD; Q99NH0; -.
PaxDb; Q99NH0; -.
PeptideAtlas; Q99NH0; -.
PRIDE; Q99NH0; -.
Ensembl; ENSMUST00000014421; ENSMUSP00000014421; ENSMUSG00000055204. [Q99NH0-1]
GeneID; 81702; -.
KEGG; mmu:81702; -.
UCSC; uc008yav.1; mouse. [Q99NH0-2]
UCSC; uc008yay.1; mouse. [Q99NH0-3]
UCSC; uc029vje.1; mouse. [Q99NH0-1]
CTD; 26057; -.
MGI; MGI:1932101; Ankrd17.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4369; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00920000148967; -.
HOGENOM; HOG000033942; -.
HOVERGEN; HBG071352; -.
InParanoid; Q99NH0; -.
KO; K16726; -.
OMA; DCGTASP; -.
OrthoDB; EOG091G04SM; -.
PhylomeDB; Q99NH0; -.
TreeFam; TF328552; -.
ChiTaRS; Ankrd17; mouse.
PRO; PR:Q99NH0; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000055204; Expressed in 297 organ(s), highest expression level in zygote.
CleanEx; MM_ANKRD17; -.
ExpressionAtlas; Q99NH0; baseline and differential.
Genevisible; Q99NH0; MM.
GO; GO:0000785; C:chromatin; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0001955; P:blood vessel maturation; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0007492; P:endoderm development; TAS:MGI.
GO; GO:0045087; P:innate immune response; ISO:MGI.
GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:1900245; P:positive regulation of MDA-5 signaling pathway; ISS:UniProtKB.
GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; ISS:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
CDD; cd00204; ANK; 7.
Gene3D; 1.25.40.20; -; 8.
Gene3D; 3.30.1370.10; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 9.
Pfam; PF00013; KH_1; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 25.
SMART; SM00322; KH; 1.
SUPFAM; SSF48403; SSF48403; 3.
SUPFAM; SSF54791; SSF54791; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 20.
PROSITE; PS50084; KH_TYPE_1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Coiled coil;
Complete proteome; Cytoplasm; Immunity; Innate immunity;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Ubl conjugation.
CHAIN 1 2603 Ankyrin repeat domain-containing protein
17.
/FTId=PRO_0000307918.
REPEAT 229 258 ANK 1.
REPEAT 262 291 ANK 2.
REPEAT 296 325 ANK 3.
REPEAT 329 358 ANK 4.
REPEAT 362 391 ANK 5.
REPEAT 396 425 ANK 6.
REPEAT 429 458 ANK 7.
REPEAT 462 491 ANK 8.
REPEAT 495 524 ANK 9.
REPEAT 529 558 ANK 10.
REPEAT 559 588 ANK 11.
REPEAT 592 621 ANK 12.
REPEAT 625 654 ANK 13.
REPEAT 659 688 ANK 14.
REPEAT 692 721 ANK 15.
REPEAT 1078 1107 ANK 16.
REPEAT 1111 1140 ANK 17.
REPEAT 1145 1174 ANK 18.
REPEAT 1178 1207 ANK 19.
REPEAT 1213 1242 ANK 20.
REPEAT 1247 1276 ANK 21.
REPEAT 1280 1309 ANK 22.
REPEAT 1315 1344 ANK 23.
REPEAT 1348 1377 ANK 24.
REPEAT 1381 1410 ANK 25.
DOMAIN 1721 1785 KH. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
COILED 1438 1522 {ECO:0000255}.
COMPBIAS 4 40 Ala-rich.
COMPBIAS 94 106 Gly-rich.
COMPBIAS 854 1004 Gln-rich.
COMPBIAS 1533 1537 Poly-Thr.
COMPBIAS 1599 1696 Ser-rich.
COMPBIAS 1946 2102 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 799 799 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 1453 1453 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 1631 1631 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 1692 1692 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1696 1696 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1705 1705 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1870 1870 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 2038 2038 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 2040 2040 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2041 2041 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2043 2043 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2055 2055 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2063 2063 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 2373 2373 Phosphoserine.
{ECO:0000250|UniProtKB:O75179}.
MOD_RES 2401 2401 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 314 314 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O75179}.
VAR_SEQ 1 141 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_028866.
VAR_SEQ 774 1024 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_028867.
VAR_SEQ 1024 1024 Missing (in isoform 3).
{ECO:0000303|PubMed:11165478}.
/FTId=VSP_028868.
VAR_SEQ 1597 1600 GESK -> VSFL (in isoform 3).
{ECO:0000303|PubMed:11165478}.
/FTId=VSP_028869.
VAR_SEQ 1601 2603 Missing (in isoform 3).
{ECO:0000303|PubMed:11165478}.
/FTId=VSP_028870.
VAR_SEQ 1723 2603 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_028871.
CONFLICT 347 347 K -> E (in Ref. 3; AAK07672).
{ECO:0000305}.
CONFLICT 357 357 E -> G (in Ref. 3; AAK07672).
{ECO:0000305}.
CONFLICT 908 908 F -> L (in Ref. 3; AAK07672).
{ECO:0000305}.
SEQUENCE 2603 AA; 274213 MW; 246DAA0E473C3D55 CRC64;
MEKATVPAAA EGEGSPPAAA AVAAPPAAAA AEVGGGARPA SSPRGMVRVC DLLLKKKPPQ
QQQQQQPPHH KAKRNRTCRP PSSSESSSDS DNSGGGGGGG GGGGGGTSSN NSEEEEDDDD
EEEEVSEVES FILDQDDLEN PMLETASKLL LSGTADGADL RTVDPETQAR LEALLEAAGI
GKLSTADGKA FADPEVLRRL TSSVSCALDE AAAALTRMRA ESTANAGQSD NRSLAEACSE
GDVNAVRKLL IEGRSVNEHT EEGESLLCLA CSAGYYELAQ VLLAMHANVE DRGIKGDITP
LMAAANGGHV KIVKLLLAHK ADVNAQSSTG NTALTYACAG GYVDVVKVLL ESGASIEDHN
ENGHTPLMEA GSAGHVEVAR LLLENGAGIN THSNEFKESA LTLACYKGHL EMVRFLLEAG
ADQEHKTDEM HTALMEACMD GHVEVARLLL DSGAQVNMPA DSFESPLTLA ACGGHVELAA
LLIERGASLE EVNDEGYTPL MEAAREGHEE MVALLLGQGA NINAQTEETQ ETALTLACCG
GFLEVADFLI KAGADIELGC STPLMEAAQE GHLELVKYLL AAGANVHATT ATGDTALTYA
CENGHTDVAD VLLQAGADLE HESEGGRTPL MKAARAGHVC TVQFLISKGA NVNRTTANND
HTVLSLACAG GHLAVVELLL AHGADPTHRL KDGSTMLIEA AKGGHTSVVC YLLDYPNNLL
AAPPPDVTQL TPPSHDLNRA PRVPVQALPM VVPPQEPDKP PANLAATLPV RSKAASKQKS
NSHLPANSQD VQGYITNQSP ESIVEEAQGK LTELEQRIKE AIEKNAQLQS LELAHADQLT
KEKIEELNKT REEQIQKKQK ILEELQKVER ELQLKTQQQL KKQYLEVKAQ RIQLQQQQQQ
SCQHLGLFTS VGVGEQLSEG DYARLQQVDP VLLKDEPQQT AAQMGFAPIQ PLAMPQALPL
ATGPLPPGSI ANLTELQGVI VGQPVLGQAQ LAGLGQGILT ETQQGLMVAS PAQTLNDTLD
DIMAAVSGRA SAMSNTPTHS IAASVSQPQT PTPSPIISPS AMLPIYPAID IDAQTESNHD
TALTLACAGG HEELVQTLLE RGASIEHRDK KGFTPLILAA TAGHVGVVEI LLDNGADIEA
QSERTKDTPL SLACSGGRQE VVELLLARGA NKEHRNVSDY TPLSLAASGG YVNIIKILLN
AGAEINSRTG SKLGISPLML AAMNGHTAAV KLLLDMGSDI NAQIETNRNT ALTLACFQGR
TEVVSLLLDR KANVEHRAKT GLTPLMEAAS GGYAEVGRVL LDKGADVNAP PVPSSRDTAL
TIAADKGHYK FCELLIGKGA HIDVRNKKGN TPLWLAANGG HLDVVQLLVQ ATADVDAADN
RKITPLMAAF RKGHVKVVRY LVKEVNQFPS DSECMRYIAT ITDKEMLKKC HLCMESIVQA
KDRQAAEANK NASILLEELD LEKLREESRR LALAAKREKR KEKRRKKKEE QRRKLEEIEA
KNKENFELQA AQEKEKLKVE EEPEVLTEPP SATTTTTIGI SATWTTLAGS HGKRNNTITT
TSSKRKNRKN KITPENVQII FDDPLPISYS QPEKVNGESK SSSTSESGDS DNMRISSCSD
ESSNSNSSRK SNNHASAVVT TTMASKKQPS VLVTFPKEER KSVSGKASIK LSETVNEGTS
NSLSTCTKSG PSPLSSPNGK LTVASPKRGP KREEGWKEVV RRSKKVSVPS TVISRVIGRG
GCNINAIREC TGAHIDIDKQ KDKTGDRIIT IRGGTESTRQ ATQLINALIK DPDKEIDELI
PKNRLKSSTA NSKIGSSAPT TTAANSSLMG IKMTTVALSS TSQTATALTV PAISSASTHK
TIKNPVNNVR PGFPVSLPLA YPPPQFAHAL LAAQTFQQIR PPRLPMTHFG GTFPPAQSTW
GPFPVRPLSP ARATNSPKPH MVPRHSNQNS SGSQVNSAGS LTSSPTTTAS SSASAVPGTT
SNGSPSSPSV RRQLFVTVVK TSNATTTTVT TTASNNSTAP TNATYPMPTA KEHYPVSSPS
SPSPPAQPGG VSRNSPLDCG SASPNKGASA SEQEASSPPV VEPANSRPPH SSSSSGSSSG
HSTQQQPPGS VPQEPRPPLQ QSQVPSPDVR MTVPPTATSS APVAVPSTAP VTYPMPQTQM
GCSQPPKMEA PAIRPPSHAT AAPHKTPAPV QSSSASVLNV NHIKRPHSVP SSVQLPSTLS
TQSACQNSVH PANKPVAPNF SAPLPFGPFS TLFENNPTNA HAFWGGPVVS SQSTPESMLS
GKSSYLPNSD PLHQSDTSKA PGFRPPLQRP APSPSGIVNM DTPYGSVTPS STHLGNFASS
LSGGQMYGPG APLGGAPLGG APTAANFNRQ HFSPLSLLTP CSSASNESPA QSVSSGVRAP
SPAPSSVPLG SEKPSSVSQD RKVPVPIGTE RSARIRQTGT SAPSVIGSNL STSVGHSGIW
SFEGIGGNQD KVDWCNPGMG NPMIHRPMSD PGVFSQHQAM ERDSTGIVTP SGTFHQHVPA
GYMDFPKVGS MPFSVYGNAM LPPVAPIADG AGGPIFNGPH SAEPSWNSLI KMVSSSTENN
GPQTVWTGPW APHMNSVHMN QLG


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ANR49_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 49; organism: Bovine; gene name: ANKRD49 96T
ANR39_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 39; organism: Bovine; gene name: ANKRD39 96T
ANR46_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 46; organism: Bovine; gene name: ANKRD46 96T
ANR37_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 37; organism: Bovine; gene name: ANKRD37 96T
ANR54_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 54; organism: Bovine; gene name: ANKRD54 96T
ANR32_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 32; organism: Bovine; gene name: ANKRD32 96T
ANKR1_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 1; organism: Bovine; gene name: ANKRD1 96T
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ANR61_BOVIN ELISA Kit FOR Ankyrin repeat domain-containing protein 61; organism: Bovine; gene name: ANKRD61 96T
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