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Q9H013 (ADA19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 19

Short name=ADAM 19
EC=3.4.24.-
Alternative name(s):
Meltrin-beta
Metalloprotease and disintegrin dendritic antigen marker
Short name=MADDAM
Gene names
Name:ADAM19
Synonyms:MLTNB
ORF Names:FKSG34
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length955 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in the proteolytic processing of beta-type neuregulin isoforms which are involved in neurogenesis and synaptogenesis, suggesting a regulatory role in glial cell. Also cleaves alpha-2 macroglobulin. May be involved in osteoblast differentiation and/or osteoblast activity in bone By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with SH3PXD2A. Ref.6

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in many normal organ tissues and several cancer cell lines.

Induction

By 1,25(OH)2VD3 in monocytes.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9H013-1)

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 B (identifier: Q9H013-2)

The sequence of this isoform differs from the canonical sequence as follows:
     902-955: VSPREALKVKAGTRGLQGGRCRVEKTKQFMLLVVWTELPEQKPRAKHSCFLVPA → FPEYRSQRAGGMISSKI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 202177 By similarity
PRO_0000029102
Chain203 – 955753Disintegrin and metalloproteinase domain-containing protein 19
PRO_0000029103

Regions

Topological domain203 – 699497Extracellular Potential
Transmembrane700 – 72021Helical; Potential
Topological domain721 – 955235Cytoplasmic Potential
Domain210 – 408199Peptidase M12B
Domain416 – 50287Disintegrin
Domain650 – 68233EGF-like
Motif130 – 1378Cysteine switch By similarity
Motif833 – 84412SH3-binding Potential
Compositional bias434 – 4374Poly-Glu
Compositional bias502 – 649148Cys-rich

Sites

Active site3461 By similarity
Metal binding1321Zinc; in inhibited form By similarity
Metal binding3451Zinc; catalytic By similarity
Metal binding3491Zinc; catalytic By similarity
Metal binding3551Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Disulfide bond320 ↔ 403 By similarity
Disulfide bond360 ↔ 387 By similarity
Disulfide bond361 ↔ 370 By similarity
Disulfide bond474 ↔ 494 By similarity
Disulfide bond654 ↔ 664 By similarity
Disulfide bond658 ↔ 670 By similarity
Disulfide bond672 ↔ 681 By similarity

Natural variations

Alternative sequence902 – 95554VSPRE…FLVPA → FPEYRSQRAGGMISSKI in isoform B.
VSP_005481
Natural variant41G → S. Ref.2
Corresponds to variant rs11465228 [ dbSNP | Ensembl ].
VAR_057066
Natural variant1331R → Q in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036146
Natural variant2981A → T in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036147
Natural variant6091H → Q in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.8
VAR_062670

Experimental info

Sequence conflict321R → SK in AAG50282. Ref.1
Sequence conflict5571D → V in AAG50282. Ref.1
Sequence conflict5571D → V in AAF22162. Ref.5
Sequence conflict6221D → N in AAG50282. Ref.1
Sequence conflict6221D → N in AAF22162. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified August 10, 2010. Version 3.
Checksum: 9C9D42BED18BF7F9

FASTA955104,997
        10         20         30         40         50         60 
MPGGAGAARL CLLAFALQPL RPRAAREPGW TRGSEEGSPK LQHELIIPQW KTSESPVREK 

        70         80         90        100        110        120 
HPLKAELRVM AEGRELILDL EKNEQLFAPS YTETHYTSSG NPQTTTRKLE DHCFYHGTVR 

       130        140        150        160        170        180 
ETELSSVTLS TCRGIRGLIT VSSNLSYVIE PLPDSKGQHL IYRSEHLKPP PGNCGFEHSK 

       190        200        210        220        230        240 
PTTRDWALQF TQQTKKRPRR MKREDLNSMK YVELYLVADY LEFQKNRRDQ DATKHKLIEI 

       250        260        270        280        290        300 
ANYVDKFYRS LNIRIALVGL EVWTHGNMCE VSENPYSTLW SFLSWRRKLL AQKYHDNAQL 

       310        320        330        340        350        360 
ITGMSFHGTT IGLAPLMAMC SVYQSGGVNM DHSENAIGVA ATMAHEMGHN FGMTHDSADC 

       370        380        390        400        410        420 
CSASAADGGC IMAAATGHPF PKVFNGCNRR ELDRYLQSGG GMCLSNMPDT RMLYGGRRCG 

       430        440        450        460        470        480 
NGYLEDGEEC DCGEEEECNN PCCNASNCTL RPGAECAHGS CCHQCKLLAP GTLCREQARQ 

       490        500        510        520        530        540 
CDLPEFCTGK SPHCPTNFYQ MDGTPCEGGQ AYCYNGMCLT YQEQCQQLWG PGARPAPDLC 

       550        560        570        580        590        600 
FEKVNVAGDT FGNCGKDMNG EHRKCNMRDA KCGKIQCQSS EARPLESNAV PIDTTIIMNG 

       610        620        630        640        650        660 
RQIQCRGTHV YRGPEEEGDM LDPGLVMTGT KCGYNHICFE GQCRNTSFFE TEGCGKKCNG 

       670        680        690        700        710        720 
HGVCNNNQNC HCLPGWAPPF CNTPGHGGSI DSGPMPPESV GPVVAGVLVA ILVLAVLMLM 

       730        740        750        760        770        780 
YYCCRQNNKL GQLKPSALPS KLRQQFSCPF RVSQNSGTGH ANPTFKLQTP QGKRKVINTP 

       790        800        810        820        830        840 
EILRKPSQPP PRPPPDYLRG GSPPAPLPAH LSRAARNSPG PGSQIERTES SRRPPPSRPI 

       850        860        870        880        890        900 
PPAPNCIVSQ DFSRPRPPQK ALPANPVPGR RSLPRPGGAS PLRPPGAGPQ QSRPLAALAP 

       910        920        930        940        950 
KVSPREALKV KAGTRGLQGG RCRVEKTKQF MLLVVWTELP EQKPRAKHSC FLVPA 

« Hide

Isoform B [UniParc].

Checksum: 048EA0189D3D126A
Show »

FASTA918100,848

References

« Hide 'large scale' references
[1]"Identification of FKSG34, a novel human gene encoding for metalloprotease-disintegrin meltrin beta."
Wang Y.-G., Gong L.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Molecular cloning and characterization of a human metalloprotease disintegrin a novel marker for dendritic cell differentiation."
Fritsche J., Moser M., Faust S., Peuker A., Buettner R., Andreesen R., Kreutz M.
Blood 96:732-739(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT SER-4.
Tissue: Lymph node.
[3]"Expression and enzymatic activity of human disintegrin and metalloproteinase ADAM19/meltrin beta."
Wei P., Zhao Y.-G., Zhuang L., Ruben S., Sang Q.-X.A.
Biochem. Biophys. Res. Commun. 280:744-755(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tissue: Dendritic cell.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Partial sequence of Homo sapiens ADAM19."
Xu R., Cai J., Ying B., Wang F., Xu T., Zhao S., Li C.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 99-955 (ISOFORM A).
[6]"The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3PXD2A.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-133 AND THR-298.
[8]"Core signaling pathways in human pancreatic cancers revealed by global genomic analyses."
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y. expand/collapse author list , Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.
Science 321:1801-1806(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-609.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF326918 mRNA. Translation: AAG50282.1.
Y13786 mRNA. Translation: CAC20585.1.
AF311317 mRNA. Translation: AAK07852.1.
AC008676 Genomic DNA. No translation available.
AC008694 Genomic DNA. No translation available.
AC106801 Genomic DNA. No translation available.
AF134707 mRNA. Translation: AAF22162.1.
CCDSCCDS4338.1. [Q9H013-2]
RefSeqNP_150377.1. NM_033274.4. [Q9H013-2]
XP_005266060.1. XM_005266003.1. [Q9H013-1]
UniGeneHs.483944.

3D structure databases

ProteinModelPortalQ9H013.
SMRQ9H013. Positions 206-685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114267. 4 interactions.
IntActQ9H013. 3 interactions.
MINTMINT-246384.
STRING9606.ENSP00000257527.

Protein family/group databases

MEROPSM12.214.

PTM databases

PhosphoSiteQ9H013.

Polymorphism databases

DMDM302393821.

Proteomic databases

MaxQBQ9H013.
PaxDbQ9H013.
PRIDEQ9H013.

Protocols and materials databases

DNASU8728.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257527; ENSP00000257527; ENSG00000135074. [Q9H013-2]
ENST00000517905; ENSP00000428654; ENSG00000135074. [Q9H013-1]
GeneID8728.
KEGGhsa:8728.
UCSCuc003lwy.3. human. [Q9H013-1]
uc003lwz.4. human. [Q9H013-2]

Organism-specific databases

CTD8728.
GeneCardsGC05M156836.
HGNCHGNC:197. ADAM19.
HPAHPA055537.
MIM603640. gene.
neXtProtNX_Q9H013.
PharmGKBPA24514.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294463.
HOGENOMHOG000230883.
HOVERGENHBG006978.
InParanoidQ9H013.
KOK08608.
OMAFQKNRRD.
OrthoDBEOG7F7W89.
PhylomeDBQ9H013.
TreeFamTF314733.

Enzyme and pathway databases

SABIO-RKQ9H013.

Gene expression databases

ArrayExpressQ9H013.
BgeeQ9H013.
CleanExHS_ADAM19.
GenevestigatorQ9H013.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiADAM19.
GenomeRNAi8728.
NextBio32743.
PROQ9H013.
SOURCESearch...

Entry information

Entry nameADA19_HUMAN
AccessionPrimary (citable) accession number: Q9H013
Secondary accession number(s): Q9BZL5, Q9UHP2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM