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AMBN_RAT
ID   AMBN_RAT                Reviewed;         422 AA.
AC   Q62840; Q540J9; Q63043;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Ameloblastin;
DE            Short=Amelin;
DE   Flags: Precursor;
GN   Name=Ambn;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Incisor;
RX   PubMed=8626794; DOI=10.1074/jbc.271.8.4431;
RA   Krebsbach P.H., Lee S.K., Matsuki Y., Kozak C.A., Yamada K.M., Yamada Y.;
RT   "Full-length sequence, localization, and chromosomal mapping of
RT   ameloblastin. A novel tooth-specific gene.";
RL   J. Biol. Chem. 271:4431-4435(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Tooth;
RX   PubMed=8797107; DOI=10.1002/jbmr.5650110703;
RA   Cerny R., Slaby I., Hammarstrom L., Wurtz T.;
RT   "A novel gene expressed in rat ameloblasts codes for proteins with cell
RT   binding domains.";
RL   J. Bone Miner. Res. 11:883-891(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RA   Lee S.K., Kim S.M., Lee Y.J., Yamada K.M., Yamada Y., Chi J.G.;
RT   "Gene structure of rat ameloblastin and specific expression in
RT   amelogenesis.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the mineralization and structural organization of
CC       enamel.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62840-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62840-2; Sequence=VSP_000226;
CC   -!- TISSUE SPECIFICITY: Ameloblast-specific.
CC   -!- SIMILARITY: Belongs to the ameloblastin family. {ECO:0000305}.
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DR   EMBL; U35097; AAC52428.1; -; mRNA.
DR   EMBL; Z50083; CAA90414.1; -; mRNA.
DR   EMBL; AY159302; AAN71737.1; -; Genomic_DNA.
DR   EMBL; AY159295; AAN71737.1; JOINED; Genomic_DNA.
DR   EMBL; AY159296; AAN71737.1; JOINED; Genomic_DNA.
DR   EMBL; AY159297; AAN71737.1; JOINED; Genomic_DNA.
DR   EMBL; AY159298; AAN71737.1; JOINED; Genomic_DNA.
DR   EMBL; AY159299; AAN71737.1; JOINED; Genomic_DNA.
DR   EMBL; AY159300; AAN71737.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_037032.1; NM_012900.1. [Q62840-1]
DR   AlphaFoldDB; Q62840; -.
DR   IntAct; Q62840; 8.
DR   STRING; 10116.ENSRNOP00000005003; -.
DR   GlyGen; Q62840; 1 site.
DR   PaxDb; Q62840; -.
DR   Ensembl; ENSRNOT00000105630; ENSRNOP00000087626; ENSRNOG00000003718. [Q62840-2]
DR   GeneID; 25376; -.
DR   KEGG; rno:25376; -.
DR   UCSC; RGD:2101; rat. [Q62840-1]
DR   CTD; 258; -.
DR   RGD; 2101; Ambn.
DR   VEuPathDB; HostDB:ENSRNOG00000003718; -.
DR   eggNOG; ENOG502QWCP; Eukaryota.
DR   GeneTree; ENSGT00390000018227; -.
DR   HOGENOM; CLU_051782_0_0_1; -.
DR   InParanoid; Q62840; -.
DR   OMA; KPAMGGD; -.
DR   OrthoDB; 1189806at2759; -.
DR   PhylomeDB; Q62840; -.
DR   TreeFam; TF337860; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:Q62840; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; ISO:RGD.
DR   GO; GO:0030345; F:structural constituent of tooth enamel; TAS:RGD.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   InterPro; IPR007798; Amelin.
DR   PANTHER; PTHR14115; PTHR14115; 1.
DR   Pfam; PF05111; Amelin; 1.
DR   SMART; SM00817; Amelin; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Biomineralization; Extracellular matrix;
KW   Glycoprotein; Hydroxylation; Phosphoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..422
FT                   /note="Ameloblastin"
FT                   /id="PRO_0000001195"
FT   REGION          271..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28989"
FT   CARBOHYD        117
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         104..118
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8797107"
FT                   /id="VSP_000226"
FT   CONFLICT        324
FT                   /note="M -> I (in Ref. 2; CAA90414)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  45206 MW;  0F983772E9082A89 CRC64;
     MSASKIPLFK MKGLLLFLSL VKMSLAVPAF PQQPGAQGMA PPGMASLSLE TMRQLGSLQG
     LNALSQYSRL GFGKALNSLW LHGLLPPHNS FPWIGPREHE TQQYEYSLPV HPPPLPSQPS
     LQPHQPGLKP FLQPTAATGV QVTPQKPGPH PPMHPGQLPL QEGELIAPDE PQVAPSENPP
     TPEVPIMDFA DPQFPTVFQI AHSLSRGPMA HNKVPTFYPG MFYMSYGANQ LNAPARIGFM
     SSEEMPGERG SPMAYGTLFP GYGGFRQTLR GLNQNSPKGG DFTVEVDSPV SVTKGPEKGE
     GPEGSPLQEA SPDKGENPAL LSQMAPGAHA GLLAFPNDHI PNMARGPAGQ RLLGVTPAAA
     DPLITPELAE VYETYGADVT TPLGDGEATM DITMSPDTQQ PPMPGNKVHQ PQVHNAWRFQ
     EP
 
 
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