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Putative nucleotidyltransferase MAB21L1 (EC 2.7.7.-) (Protein mab-21-like 1)

 MB211_HUMAN             Reviewed;         359 AA.
Q13394; Q6I9T5;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 124.
RecName: Full=Putative nucleotidyltransferase MAB21L1 {ECO:0000305};
EC=2.7.7.- {ECO:0000305};
AltName: Full=Protein mab-21-like 1 {ECO:0000312|HGNC:HGNC:6757};
Name=MAB21L1 {ECO:0000312|HGNC:HGNC:6757};
Synonyms=CAGR1 {ECO:0000303|PubMed:8733127};
ORFNames=Nbla00126 {ECO:0000303|PubMed:12880961};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND POLYMORPHISM.
PubMed=8733127; DOI=10.1093/hmg/5.5.607;
Margolis R.L., Stine Q.C., Mcinnis M.G., Ranen N.G., Rubinsztein D.C.,
Leggo J., Jones Brando L.V., Kidwai A.S., Loev S.J., Breschel T.S.,
Callahan C., Simpson S.G., DePaulo J.R., McMahon F.J., Jain S.,
Paykel E.S., Walsh C., DeLisi L.E., Crow T.J., Torrey E.F.,
Ashworth R.G., Macke J.P., Nathans J., Ross C.A.;
"cDNA cloning of a human homologue of the Caenorhabditis elegans cell
fate-determining gene mab-21: expression, chromosomal localization and
analysis of a highly polymorphic (CAG)n trinucleotide repeat.";
Hum. Mol. Genet. 5:607-616(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neuroblastoma;
PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
Hirato J., Nakagawara A.;
"Neuroblastoma oligo-capping cDNA project: toward the understanding of
the genesis and biology of neuroblastoma.";
Cancer Lett. 197:63-68(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
POLYMORPHISM.
PubMed=9152839; DOI=10.1136/jmg.34.5.411;
Potter N.T.;
"Meiotic instability associated with the CAGR1 trinucleotide repeat at
13q13.";
J. Med. Genet. 34:411-413(1997).
[8]
POLYMORPHISM.
PubMed=9950369;
Margolis R.L., Stine O.C., Ward C.M., Franz M.L., Rosenblatt A.,
Callahan C., Sherr M., Ross C.A., Potter N.T.;
"Unstable expansion of the CAG trinucleotide repeat in MAB21L1: report
of a second pedigree and effect on protein expression.";
J. Med. Genet. 36:62-64(1999).
[9]
POLYMORPHISM.
PubMed=15526290; DOI=10.1002/bdra.20084;
Merello E., De Marco P., Moroni A., Raso A., Calevo M.G.,
Consalez G.G., Cama A., Capra V.;
"Molecular genetic analysis of human homologs of Caenorhabditis
elegans mab-21-like 1 gene in patients with neural tube defects.";
Birth Defects Res. A Clin. Mol. Teratol. 70:885-888(2004).
[10] {ECO:0000244|PDB:5EOG, ECO:0000244|PDB:5EOM}
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 2-359 IN COMPLEX WIT5H CTP,
FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-51 AND ARG-247.
PubMed=27271801; DOI=10.1038/srep27498;
de Oliveira Mann C.C., Kiefersauer R., Witte G., Hopfner K.P.;
"Structural and biochemical characterization of the cell fate
determining nucleotidyltransferase fold protein MAB21L1.";
Sci. Rep. 6:27498-27498(2016).
-!- FUNCTION: Putative nucleotidyltransferase required for several
aspects of embryonic development including normal development of
the eye (By similarity). It is unclear whether it displays
nucleotidyltransferase activity in vivo (PubMed:27271801). Binds
single-stranded RNA (ssRNA) (PubMed:27271801).
{ECO:0000250|UniProtKB:O70299, ECO:0000269|PubMed:27271801}.
-!- SUBUNIT: Monomer (PubMed:27271801). Homodecamer; composed of 2
back to back homopentamers (PubMed:27271801). The protein may
exist as monomer in solution and oiligomerizes upon ligand binding
(PubMed:27271801). {ECO:0000305|PubMed:27271801}.
-!- INTERACTION:
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-10229059, EBI-747107;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O70299}.
-!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and skeletal
muscle. {ECO:0000269|PubMed:8733127}.
-!- DOMAIN: While it shares structure similarities with MB21D1/cGAS,
it also features a number of differences. The crystal structure is
in inactive conformation and the enzyme would require a
conformational change to be active. The nucleotidyltransferase
activity is therefore unclear. {ECO:0000269|PubMed:27271801}.
-!- POLYMORPHISM: A CAG trinucleotide repeat occurs in the 5'-UTR of
this gene. This repeat has been found to be highly polymorphic,
although expanded alleles have not yet been definitely linked with
any phenotypic abnormality. {ECO:0000269|PubMed:15526290,
ECO:0000269|PubMed:8733127, ECO:0000269|PubMed:9152839,
ECO:0000269|PubMed:9950369}.
-!- SIMILARITY: Belongs to the mab-21 family. {ECO:0000305}.
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EMBL; U38810; AAB47576.1; -; mRNA.
EMBL; AB073388; BAE45718.1; -; mRNA.
EMBL; CR457420; CAG33701.1; -; mRNA.
EMBL; AL390071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08547.1; -; Genomic_DNA.
EMBL; BC028170; AAH28170.1; -; mRNA.
CCDS; CCDS9353.1; -.
PIR; G02221; G02221.
RefSeq; NP_005575.1; NM_005584.4.
UniGene; Hs.584776; -.
PDB; 5EOG; X-ray; 3.05 A; A/B/C/D/F=2-359.
PDB; 5EOM; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I/J=2-359.
PDBsum; 5EOG; -.
PDBsum; 5EOM; -.
ProteinModelPortal; Q13394; -.
SMR; Q13394; -.
BioGrid; 110256; 11.
IntAct; Q13394; 1.
STRING; 9606.ENSP00000369251; -.
iPTMnet; Q13394; -.
PhosphoSitePlus; Q13394; -.
BioMuta; MAB21L1; -.
DMDM; 74739786; -.
PaxDb; Q13394; -.
PeptideAtlas; Q13394; -.
PRIDE; Q13394; -.
TopDownProteomics; Q13394; -.
DNASU; 4081; -.
Ensembl; ENST00000379919; ENSP00000369251; ENSG00000180660.
GeneID; 4081; -.
KEGG; hsa:4081; -.
UCSC; uc032aca.2; human.
CTD; 4081; -.
DisGeNET; 4081; -.
EuPathDB; HostDB:ENSG00000180660.7; -.
GeneCards; MAB21L1; -.
HGNC; HGNC:6757; MAB21L1.
HPA; HPA049324; -.
HPA; HPA059864; -.
MIM; 601280; gene.
neXtProt; NX_Q13394; -.
OpenTargets; ENSG00000180660; -.
PharmGKB; PA30516; -.
eggNOG; KOG3963; Eukaryota.
eggNOG; ENOG410XNRJ; LUCA.
GeneTree; ENSGT00510000046791; -.
HOGENOM; HOG000007337; -.
HOVERGEN; HBG053080; -.
InParanoid; Q13394; -.
OMA; YFLPHVD; -.
OrthoDB; EOG091G0939; -.
PhylomeDB; Q13394; -.
TreeFam; TF315012; -.
GenomeRNAi; 4081; -.
PRO; PR:Q13394; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000180660; -.
CleanEx; HS_MAB21L1; -.
ExpressionAtlas; Q13394; baseline and differential.
Genevisible; Q13394; HS.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
InterPro; IPR024810; Mab-21_dom.
Pfam; PF03281; Mab-21; 1.
SMART; SM01265; Mab-21; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Developmental protein;
GTP-binding; Metal-binding; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome;
Transferase.
CHAIN 1 359 Putative nucleotidyltransferase MAB21L1.
/FTId=PRO_0000312781.
NP_BIND 23 24 NTP. {ECO:0000244|PDB:5EOM,
ECO:0000269|PubMed:27271801}.
NP_BIND 63 66 NTP. {ECO:0000244|PDB:5EOM,
ECO:0000269|PubMed:27271801}.
NP_BIND 252 255 NTP. {ECO:0000244|PDB:5EOM,
ECO:0000269|PubMed:27271801}.
METAL 73 73 Magnesium; catalytic.
{ECO:0000250|UniProtKB:Q8N884}.
METAL 75 75 Magnesium; catalytic.
{ECO:0000250|UniProtKB:Q8N884}.
BINDING 248 248 NTP. {ECO:0000244|PDB:5EOM,
ECO:0000269|PubMed:27271801}.
VARIANT 70 70 S -> P (in dbSNP:rs1065316).
/FTId=VAR_037568.
MUTAGEN 51 51 R->C: Decreased protein stability.
{ECO:0000269|PubMed:27271801}.
MUTAGEN 247 247 R->Q: Decreased protein stability.
{ECO:0000269|PubMed:27271801}.
CONFLICT 132 132 F -> L (in Ref. 3; CAG33701).
{ECO:0000305}.
HELIX 2 48 {ECO:0000244|PDB:5EOM}.
STRAND 66 70 {ECO:0000244|PDB:5EOM}.
STRAND 73 79 {ECO:0000244|PDB:5EOM}.
STRAND 86 89 {ECO:0000244|PDB:5EOM}.
STRAND 97 106 {ECO:0000244|PDB:5EOM}.
TURN 108 110 {ECO:0000244|PDB:5EOM}.
HELIX 114 116 {ECO:0000244|PDB:5EOM}.
STRAND 121 123 {ECO:0000244|PDB:5EOM}.
HELIX 125 142 {ECO:0000244|PDB:5EOM}.
HELIX 146 148 {ECO:0000244|PDB:5EOM}.
STRAND 149 151 {ECO:0000244|PDB:5EOM}.
STRAND 159 162 {ECO:0000244|PDB:5EOM}.
TURN 163 165 {ECO:0000244|PDB:5EOM}.
STRAND 166 176 {ECO:0000244|PDB:5EOM}.
HELIX 182 184 {ECO:0000244|PDB:5EOM}.
HELIX 197 205 {ECO:0000244|PDB:5EOM}.
STRAND 208 211 {ECO:0000244|PDB:5EOM}.
STRAND 230 233 {ECO:0000244|PDB:5EOM}.
HELIX 235 241 {ECO:0000244|PDB:5EOM}.
HELIX 247 261 {ECO:0000244|PDB:5EOM}.
HELIX 271 284 {ECO:0000244|PDB:5EOM}.
HELIX 288 291 {ECO:0000244|PDB:5EOM}.
HELIX 293 295 {ECO:0000244|PDB:5EOM}.
HELIX 296 312 {ECO:0000244|PDB:5EOM}.
TURN 326 329 {ECO:0000244|PDB:5EOM}.
HELIX 332 351 {ECO:0000244|PDB:5EOM}.
HELIX 353 358 {ECO:0000244|PDB:5EOM}.
SEQUENCE 359 AA; 40956 MW; A27C53FBC997A049 CRC64;
MIAAQAKLVY HLNKYYNEKC QARKAAIAKT IREVCKVVSD VLKEVEVQEP RFISSLNEMD
NRYEGLEVIS PTEFEVVLYL NQMGVFNFVD DGSLPGCAVL KLSDGRKRSM SLWVEFITAS
GYLSARKIRS RFQTLVAQAV DKCSYRDVVK MVADTSEVKL RIRDRYVVQI TPAFKCTGIW
PRSAAHWPLP HIPWPGPNRV AEVKAEGFNL LSKECHSLAG KQSSAESDAW VLQFAEAENR
LQMGGCRKKC LSILKTLRDR HLELPGQPLN NYHMKTLVSY ECEKHPRESD WDESCLGDRL
NGILLQLISC LQCRRCPHYF LPNLDLFQGK PHSALENAAK QTWRLAREIL TNPKSLEKL


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