Reviewed, UniProtKB/Swiss-Prot Q99217 (AMELX_HUMAN)

Names and origin

Protein names

Recommended name:
    Amelogenin, X isoform

Gene names

Name:	AMELX
Synonyms:	AMG, AMGX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location	Secreted › extracellular space › extracellular matrix.
Developmental stage	Transiently but abundantly expressed by ameloblasts during tooth development. Amelogenin is the predominant protein in developing dental enamel.
Involvement in disease	Defects in AMELX are the cause of amelogenesis imperfecta hypoplastic type 1 (AIH1) [MIM:301200]. AIH1 is a X-linked defect of dental enamel formation. Teeth have only a thin layer of enamel with normal hardness. The thinness of the enamel makes the teeth appear small. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Miscellaneous	This isoform is encoded on the X chromosome.
Sequence similarities	Belongs to the amelogenin family.

Ontologies

Keywords
Biological process	Biomineralization
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Disease	Amelogenesis imperfecta Disease mutation
Domain	Repeat Signal
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB cell proliferation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB chondrocyte differentiation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB enamel mineralization Inferred from mutant phenotype. Source: UniProtKB epithelial to mesenchymal transition Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB ion homeostasis Ref.5 Traceable author statement. Source: UniProtKB odontogenesis of dentine-containing tooth Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB osteoblast differentiation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of collagen biosynthetic process Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of tooth mineralization Ref.5 Traceable author statement. Source: UniProtKB signal transduction Traceable author statement. Source: UniProtKB
Cellular component	extracellular matrix part Inferred by curator. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA proteinaceous extracellular matrix Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	cell surface binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB growth factor activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB hydroxyapatite binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB identical protein binding Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB structural constituent of tooth enamel Ref.1 Ref.5 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q99217-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q99217-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-34: Missing.

Isoform 3 (identifier: Q99217-3)

Also known as: Rare;

The sequence of this isoform differs from the canonical sequence as follows:
     34-34: E → ENSHSQAINVDRTAL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Ref.5
	Chain	17 – 191	175	Amelogenin, X isoform		PRO_0000001199
Amino acid modifications
	Modified residue	32	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	19 – 34	16	Missing in isoform 2.		VSP_000228
	Alternative sequence	34	1	E → ENSHSQAINVDRTAL in isoform 3.		VSP_000229
	Natural variant	4	1	W → S in AIH1. Ref.13		VAR_037581
	Natural variant	5 – 8	4	ILFA → T in AIH1.		VAR_000559
	Natural variant	37	1	T → I in AIH1. Ref.10		VAR_037582
	Natural variant	56	1	P → T in AIH1. Ref.11 Ref.12		VAR_037583
Experimental info
	Sequence conflict	50 – 51	2	PS → SP AA sequence Ref.5
	Sequence conflict	173	1	D → H AA sequence Ref.8
	Sequence conflict	191	1	D → VSIF in AAA62826. Ref.7
	Sequence conflict	191	1	D → VSIF in CAA32613. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 322C88DA3F7155DC	FASTA	191	21,603
	10 20 30 40 50 60 MGTWILFACL LGAAFAMPLP PHPGHPGYIN FSYEVLTPLK WYQSIRPPYP SYGYEPMGGW 70 80 90 100 110 120 LHHQIIPVLS QQHPPTHTLQ PHHHIPVVPA QQPVIPQQPM MPVPGQHSMT PIQHHQPNLP 130 140 150 160 170 180 PPAQQPYQPQ PVQPQPHQPM QPQPPVHPMQ PLPPQPPLPP MFPMQPLPPM LPDLTLEAWP 190 STDKTKREEV D
	Isoform 2. Checksum: 214D3018D9B50F1B	FASTA	175	19,796
	10 20 30 40 50 60 MGTWILFACL LGAAFAMPVL TPLKWYQSIR PPYPSYGYEP MGGWLHHQII PVLSQQHPPT 70 80 90 100 110 120 HTLQPHHHIP VVPAQQPVIP QQPMMPVPGQ HSMTPIQHHQ PNLPPPAQQP YQPQPVQPQP 130 140 150 160 170 HQPMQPQPPV HPMQPLPPQP PLPPMFPMQP LPPMLPDLTL EAWPSTDKTK REEVD
	Isoform 3 (Rare). Checksum: 535F5454018E3D6E	FASTA	205	23,111
	10 20 30 40 50 60 MGTWILFACL LGAAFAMPLP PHPGHPGYIN FSYENSHSQA INVDRTALVL TPLKWYQSIR 70 80 90 100 110 120 PPYPSYGYEP MGGWLHHQII PVLSQQHPPT HTLQPHHHIP VVPAQQPVIP QQPMMPVPGQ 130 140 150 160 170 180 HSMTPIQHHQ PNLPPPAQQP YQPQPVQPQP HQPMQPQPPV HPMQPLPPQP PLPPMFPMQP 190 200 LPPMLPDLTL EAWPSTDKTK REEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human enamel protein gene amelogenin is expressed from both the X and the Y chromosomes." Salido E.C., Yen P.H., Koprivnikar K., Yu L.-C., Shapiro L.J. Am. J. Hum. Genet. 50:303-316(1992) [PubMed: 1734713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Tooth bud.
[2]	"A nomenclature for X-linked amelogenesis imperfecta." Hart P.S., Hart T.C., Simmer J.P., Wright J.T. Arch. Oral Biol. 47:255-260(2002) [PubMed: 11922868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Human amelogenins: sequences of 'TRAP' molecules." Fincham A.G., Hu Y., Pavlova Z., Slavkin H.C., Snead M.L. Calcif. Tissue Int. 45:243-250(1989) [PubMed: 2509010] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-60.
[6]	"Production of a monoclonal antibody against human amelogenin." Catalano-Sherman J., Laskov R., Palmon A., David S., Deutsch D. Calcif. Tissue Int. 54:76-80(1994) [PubMed: 8118759] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-37.
[7]	"A human X-Y homologous region encodes 'amelogenin'." Nakahori Y., Takenaka O., Nakagome Y. Genomics 9:264-269(1991) [PubMed: 2004775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-191 (ISOFORM 1).
[8]	"Amino acid sequence of a major human amelogenin protein employing Edman degradation and cDNA sequencing." Catalano-Sherman J., Palmon A., Burstein Y., Deutsch D. J. Dent. Res. 72:1566-1572(1993) [PubMed: 8254123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-190, PARTIAL PROTEIN SEQUENCE. Tissue: Tooth bud.
[9]	"Amelogenin signal peptide mutation: correlation between mutations in the amelogenin gene (AMGX) and manifestations of X-linked amelogenesis imperfecta." Lagerstroem-Fermer M., Nilddon M., Baeckman B., Salido E., Shapiro L., Pettersson U., Landergren U. Genomics 26:159-162(1995) [PubMed: 7782077] [Abstract] Cited for: VARIANT AIH1 5-ILE--ALA-8 DELINS THR.
[10]	"Characterisation of molecular defects in X-linked amelogenesis imperfecta (AIH1)." Lench N.J., Winter G.B. Hum. Mutat. 5:251-259(1995) [PubMed: 7599636] [Abstract] Cited for: VARIANT AIH1 ILE-37.
[11]	"Mutational analysis of X-linked amelogenesis imperfecta in multiple families." Hart S., Hart T., Gibson C., Wright J.T. Arch. Oral Biol. 45:79-86(2000) [PubMed: 10669095] [Abstract] Cited for: VARIANT AIH1 THR-56.
[12]	"An amelogenin gene defect associated with human X-linked amelogenesis imperfecta." Collier P.M., Sauk J.J., Rosenbloom S.J., Yuan Z.A., Gibson C.W. Arch. Oral Biol. 42:235-242(1997) [PubMed: 9188994] [Abstract] Cited for: VARIANT AIH1 THR-56.
[13]	"Amelogenin p.M1T and p.W4S mutations underlying hypoplastic X-linked amelogenesis imperfecta." Kim J.-W., Simmer J.P., Hu Y.Y., Lin B.P.-L., Boyd C., Wright J.T., Yamada C.J.M., Rayes S.K., Feigal R.J., Hu J.C.-C. J. Dent. Res. 83:378-383(2004) [PubMed: 15111628] [Abstract] Cited for: VARIANT AIH1 SER-4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M86932 mRNA. Translation: AAA51717.1. AF436849 mRNA. Translation: AAL30432.1. AY040206 Genomic DNA. Translation: AAK77213.1. AC002366 Genomic DNA. Translation: AAC21581.1. BC074951 mRNA. Translation: AAH74951.1. M55418 Genomic DNA. Translation: AAA62826.1. X14440 Genomic DNA. Translation: CAA32613.1. S67147 mRNA. Translation: AAB29184.1.
IPI	IPI00013959. IPI00220033. IPI00220034.
PIR	A41816. B41816.
RefSeq	NP_001133.1. NP_872621.1. NP_872622.1.
UniGene	Hs.654436
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q99217.
Proteomic databases
PRIDE	Q99217.
Genome annotation databases
Ensembl	ENST00000380714; ENSP00000370090; ENSG00000125363; Homo sapiens. [Genome view]
GeneID	265.
KEGG	hsa:265.
UCSC	uc004cus.1. human. uc004cut.1. human. uc004cuu.1. human.
Organism-specific databases
CTD	265.
GeneCards	GC0XP011221.
H-InvDB	HIX0056174.
HGNC	HGNC:461. AMELX.
HPA	HPA005988.
MIM	300391. gene. 301200. phenotype.
Orphanet	88661. Amelogenesis imperfecta. 100033. Amelogenesis imperfecta, hypomaturation type.
PharmGKB	PA24766.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q99217.
OMA	WYQNMIR.
Gene expression databases
ArrayExpress	Q99217.
Bgee	Q99217.
CleanEx	HS_AMELX.
Genevestigator	Q99217.
GermOnline	ENSG00000125363. Homo sapiens.
Family and domain databases
InterPro	IPR004116. Amelogenin. [Graphical view]
Pfam	PF02948. Amelogenin. 1 hit. [Graphical view]
PRINTS	PR01757. AMELOGENIN.
SMART	SM00818. Amelogenin. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	1037.
PMAP-CutDB	Q99217.
SOURCE	Search...

Entry information

Entry name

AMELX_HUMAN

Accession

Primary (citable) accession number: Q99217
Secondary accession number(s): Q96NW6, Q9UCA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.