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AMTN_MOUSE
ID   AMTN_MOUSE              Reviewed;         213 AA.
AC   Q9D3J8;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Amelotin;
DE   Flags: Precursor;
GN   Name=Amtn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
RC   TISSUE=Incisor;
RX   PubMed=16304441; DOI=10.1177/154405910508401207;
RA   Iwasaki K., Bajenova E., Somogyi-Ganss E., Miller M., Nguyen V.,
RA   Nourkeyhani H., Gao Y., Wendel M., Ganss B.;
RT   "Amelotin -- a novel secreted, ameloblast-specific protein.";
RL   J. Dent. Res. 84:1127-1132(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16787391; DOI=10.1042/bj20060662;
RA   Moffatt P., Smith C.E., St Arnaud R., Simmons D., Wright J.T., Nanci A.;
RT   "Cloning of rat amelotin and localization of the protein to the basal
RT   lamina of maturation stage ameloblasts and junctional epithelium.";
RL   Biochem. J. 399:37-46(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=25407797; DOI=10.1002/jbmr.2411;
RA   Abbarin N., Miguel S.S., Holcroft J., Iwasaki K., Ganss B.;
RT   "The enamel protein amelotin is a promoter of hydroxyapatite
RT   mineralization.";
RL   J. Bone Miner. Res. 30:775-785(2015).
CC   -!- FUNCTION: Is a promoter of calcium phosphate mineralization, playing a
CC       critical role in the formation of the compact, mineralized, aprismatic
CC       enamel surface layer during the maturation stage of amelogenesis.
CC       {ECO:0000269|PubMed:16304441, ECO:0000269|PubMed:25407797}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16304441}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in maturation-stage
CC       ameloblasts. {ECO:0000269|PubMed:16304441,
CC       ECO:0000269|PubMed:16787391}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases greatly with the transition
CC       from secretory to maturation-stage ameloblasts, is maintained during
CC       the maturation stage and gradually declines towards the zone of reduced
CC       ameloblasts. {ECO:0000269|PubMed:16304441}.
CC   -!- PTM: Phosphorylated by FAM20C in vitro. {ECO:0000250|UniProtKB:Q6UX39}.
CC   -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q3HS82}.
CC   -!- SIMILARITY: Belongs to the amelotin family. {ECO:0000305}.
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DR   EMBL; AK017352; BAB30704.1; -; mRNA.
DR   CCDS; CCDS51538.1; -.
DR   RefSeq; NP_082069.1; NM_027793.1.
DR   AlphaFoldDB; Q9D3J8; -.
DR   STRING; 10090.ENSMUSP00000073081; -.
DR   PhosphoSitePlus; Q9D3J8; -.
DR   PaxDb; Q9D3J8; -.
DR   PRIDE; Q9D3J8; -.
DR   Antibodypedia; 50435; 192 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000073363; ENSMUSP00000073081; ENSMUSG00000029282.
DR   GeneID; 71421; -.
DR   KEGG; mmu:71421; -.
DR   UCSC; uc008xzq.1; mouse.
DR   CTD; 401138; -.
DR   MGI; MGI:1918671; Amtn.
DR   VEuPathDB; HostDB:ENSMUSG00000029282; -.
DR   eggNOG; ENOG502SFV7; Eukaryota.
DR   GeneTree; ENSGT00390000006715; -.
DR   HOGENOM; CLU_082745_0_0_1; -.
DR   InParanoid; Q9D3J8; -.
DR   OMA; PQMLPIF; -.
DR   OrthoDB; 1353258at2759; -.
DR   PhylomeDB; Q9D3J8; -.
DR   TreeFam; TF337677; -.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 71421; 3 hits in 74 CRISPR screens.
DR   PRO; PR:Q9D3J8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9D3J8; protein.
DR   Bgee; ENSMUSG00000029282; Expressed in molar tooth and 15 other tissues.
DR   Genevisible; Q9D3J8; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:HGNC-UCL.
DR   GO; GO:0005911; C:cell-cell junction; IDA:HGNC-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IMP:HGNC-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:HGNC-UCL.
DR   GO; GO:0070169; P:positive regulation of biomineral tissue development; ISO:MGI.
DR   GO; GO:0070175; P:positive regulation of enamel mineralization; IMP:UniProtKB.
DR   InterPro; IPR031501; Amelotin.
DR   PANTHER; PTHR36858; PTHR36858; 1.
DR   Pfam; PF15757; Amelotin; 1.
PE   2: Evidence at transcript level;
KW   Biomineralization; Cell adhesion; Glycoprotein; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..213
FT                   /note="Amelotin"
FT                   /id="PRO_0000022614"
FT   REGION          22..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  22119 MW;  1A72333D547179F1 CRC64;
     MKTMILLLCL LGSAQSLPKQ LNPASGVPAT KPTPGQVTPL PQQQPNQVFP SISLIPLTQL
     LTLGSDLPLF NPAAGPHGAH TLPFTLGPLN GQQQLQPQML PIIVAQLGAQ GALLSSEELP
     LASQIFTGLL IHPLFPGAIP PSGQAGTKPD VQNGVLPTRQ AGAKAVNQGT TPGHVTTPGV
     TDDDDYEMST PAGLRRATHT TEGTTIDPPN RTQ
 
 
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