Q9BZ11 (ADA33_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Disintegrin and metalloproteinase domain-containing protein 33
Short name=ADAM 33
EC=3.4.24.-

Gene names

Name:	ADAM33
Synonyms:	C20orf153
ORF Names:	UNQ873/PRO1891

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	813 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)

Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in all tissues, except liver, with high expression in placenta, lung, spleen and veins. Ref.1
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.
Involvement in disease	Asthma (ASTHMA) [MIM:600807]: The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with weezing due to spasmodic contraction of the bronchi. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.2 Ref.6 Ref.7
Sequence similarities	Contains 1 disintegrin domain. Contains 1 EGF-like domain. Contains 1 peptidase M12B domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Asthma
Domain	EGF-like domain Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	integral to membrane Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	metalloendopeptidase activity Non-traceable author statement Ref.1. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9BZ11-1)

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: Q9BZ11-2)

The sequence of this isoform differs from the canonical sequence as follows:
     636-661: Missing.

Isoform 3 (identifier: Q9BZ11-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-478: Missing.
     636-661: Missing.

Note: No experimental confirmation available. By similarity with mouse isoform.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 203

174

By similarity

PRO_0000029142

Chain

204 – 813

610

Disintegrin and metalloproteinase domain-containing protein 33

PRO_0000029143

Regions

Topological domain

30 – 701

672

Extracellular Potential

Transmembrane

702 – 722

21

Helical; Potential

Topological domain

723 – 813

91

Cytoplasmic Potential

Domain

210 – 409

200

Peptidase M12B

Domain

417 – 503

87

Disintegrin

Domain

649 – 681

33

EGF-like

Motif

131 – 138

8

Cysteine switch By similarity

Compositional bias

503 – 648

146

Cys-rich

Sites

Active site

346

1

By similarity

Metal binding

133

1

Zinc; in inhibited form By similarity

Metal binding

345

1

Zinc; catalytic

Metal binding

349

1

Zinc; catalytic

Metal binding

355

1

Zinc; catalytic

Amino acid modifications

Glycosylation

109

1

N-linked (GlcNAc...) Potential

Glycosylation

145

1

N-linked (GlcNAc...) Potential

Glycosylation

231

1

N-linked (GlcNAc...)

Glycosylation

276

1

N-linked (GlcNAc...)

Glycosylation

448

1

N-linked (GlcNAc...) Potential

Disulfide bond

320 ↔ 404

Disulfide bond

360 ↔ 388

Disulfide bond

361 ↔ 371

Disulfide bond

475 ↔ 495

By similarity

Disulfide bond

653 ↔ 663

By similarity

Disulfide bond

657 ↔ 669

By similarity

Disulfide bond

671 ↔ 680

By similarity

Natural variations

Alternative sequence

1 – 478

478

Missing in isoform 3.

VSP_015421

Alternative sequence

636 – 661

26

Missing in isoform 2 and isoform 3.

VSP_005495

Natural variant

109

1

N → S. Ref.4
Corresponds to variant rs41467948 [ dbSNP | Ensembl ].

VAR_030512

Natural variant

178

1

T → A. Ref.4
Corresponds to variant rs3918392 [ dbSNP | Ensembl ].

VAR_029143

Natural variant

272

1

T → M. Ref.4
Corresponds to variant rs41534847 [ dbSNP | Ensembl ].

VAR_030513

Natural variant

305

1

A → V in a cutaneous metastatic melanoma sample; somatic mutation. Ref.9

VAR_066337

Natural variant

316

1

V → I. Ref.4
Corresponds to variant rs41459049 [ dbSNP | Ensembl ].

VAR_030514

Natural variant

336

1

P → S. Ref.4
Corresponds to variant rs41483049 [ dbSNP | Ensembl ].

VAR_030515

Natural variant

365

1

A → S. Ref.4
Corresponds to variant rs41419248 [ dbSNP | Ensembl ].

VAR_030516

Natural variant

441

1

D → E. Ref.4
Corresponds to variant rs41382144 [ dbSNP | Ensembl ].

VAR_030517

Natural variant

515

1

W → R. Ref.4
Corresponds to variant rs615436 [ dbSNP | Ensembl ].

VAR_030518

Natural variant

612

1

L → H. Ref.4
Corresponds to variant rs41453444 [ dbSNP | Ensembl ].

VAR_030519

Natural variant

710

1

V → I. Ref.4
Corresponds to variant rs3918396 [ dbSNP | Ensembl ].

VAR_030520

Natural variant

739

1

C → G. Ref.4
Corresponds to variant rs41434648 [ dbSNP | Ensembl ].

VAR_030521

Natural variant

742

1

D → Y. Ref.4
Corresponds to variant rs41462450 [ dbSNP | Ensembl ].

VAR_030522

Natural variant

764

1

M → T. Ref.4
Corresponds to variant rs2280091 [ dbSNP | Ensembl ].

VAR_021847

Natural variant

774

1

P → S. Ref.4
Corresponds to variant rs2280090 [ dbSNP | Ensembl ].

VAR_029144

Experimental info

Sequence conflict

802

1

Missing in AAM80482. Ref.2

Sequence conflict

802

1

Missing in AAM80483. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

813

Helix Strand Turn

Details...

Beta strand

210 – 218

9

Helix

220 – 225

6

Turn

226 – 228

3

Helix

230 – 248

19

Helix

249 – 251

3

Beta strand

253 – 262

10

Beta strand

264 – 266

3

Helix

275 – 292

18

Beta strand

296 – 303

8

Helix

307 – 309

3

Turn

322 – 324

3

Beta strand

326 – 330

5

Beta strand

333 – 335

3

Helix

336 – 350

15

Helix

366 – 368

3

Helix

387 – 398

12

Turn

399 – 402

4

Helix

403 – 406

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: 90713A99668D5569	FASTA	813	87,739
	10 20 30 40 50 60 MGWRPRRARG TPLLLLLLLL LLWPVPGAGV LQGHIPGQPV TPHWVLDGQP WRTVSLEEPV 70 80 90 100 110 120 SKPDMGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD GQPVVLAPNH TDHCHYQGRV 130 140 150 160 170 180 RGFPDSWVVL CTCSGMSGLI TLSRNASYYL RPWPPRGSKD FSTHEIFRME QLLTWKGTCG 190 200 210 220 230 240 HRDPGNKAGM TSLPGGPQSR GRREARRTRK YLELYIVADH TLFLTRHRNL NHTKQRLLEV 250 260 270 280 290 300 ANYVDQLLRT LDIQVALTGL EVWTERDRSR VTQDANATLW AFLQWRRGLW AQRPHDSAQL 310 320 330 340 350 360 LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS LGLSHDPDGC 370 380 390 400 410 420 CVEAAAESGG CVMAAATGHP FPRVFSACSR RQLRAFFRKG GGACLSNAPD PGLPVPPALC 430 440 450 460 470 480 GNGFVEAGEE CDCGPGQECR DLCCFAHNCS LRPGAQCAHG DCCVRCLLKP AGALCRQAMG 490 500 510 520 530 540 DCDLPEFCTG TSSHCPPDVY LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA 550 560 570 580 590 600 CFQVVNSAGD AHGNCGQDSE GHFLPCAGRD ALCGKLQCQG GKPSLLAPHM VPVDSTVHLD 610 620 630 640 650 660 GQEVTCRGAL ALPSAQLDLL GLGLVEPGTQ CGPRMVCQSR RCRKNAFQEL QRCLTACHSH 670 680 690 700 710 720 GVCNSNHNCH CAPGWAPPFC DKPGFGGSMD SGPVQAENHD TFLLAMLLSV LLPLLPGAGL 730 740 750 760 770 780 AWCCYRLPGA HLQRCSWGCR RDPACSGPKD GPHRDHPLGG VHPMELGPTA TGQPWPLDPE 790 800 810 NSHEPSSHPE KPLPAVSPDP QADQVQMPRS CLW
	Isoform 2 [UniParc]. Checksum: CBAF1B08B263A890	FASTA	787	84,724
	10 20 30 40 50 60 MGWRPRRARG TPLLLLLLLL LLWPVPGAGV LQGHIPGQPV TPHWVLDGQP WRTVSLEEPV 70 80 90 100 110 120 SKPDMGLVAL EAEGQELLLE LEKNHRLLAP GYIETHYGPD GQPVVLAPNH TDHCHYQGRV 130 140 150 160 170 180 RGFPDSWVVL CTCSGMSGLI TLSRNASYYL RPWPPRGSKD FSTHEIFRME QLLTWKGTCG 190 200 210 220 230 240 HRDPGNKAGM TSLPGGPQSR GRREARRTRK YLELYIVADH TLFLTRHRNL NHTKQRLLEV 250 260 270 280 290 300 ANYVDQLLRT LDIQVALTGL EVWTERDRSR VTQDANATLW AFLQWRRGLW AQRPHDSAQL 310 320 330 340 350 360 LTGRAFQGAT VGLAPVEGMC RAESSGGVST DHSELPIGAA ATMAHEIGHS LGLSHDPDGC 370 380 390 400 410 420 CVEAAAESGG CVMAAATGHP FPRVFSACSR RQLRAFFRKG GGACLSNAPD PGLPVPPALC 430 440 450 460 470 480 GNGFVEAGEE CDCGPGQECR DLCCFAHNCS LRPGAQCAHG DCCVRCLLKP AGALCRQAMG 490 500 510 520 530 540 DCDLPEFCTG TSSHCPPDVY LLDGSPCARG SGYCWDGACP TLEQQCQQLW GPGSHPAPEA 550 560 570 580 590 600 CFQVVNSAGD AHGNCGQDSE GHFLPCAGRD ALCGKLQCQG GKPSLLAPHM VPVDSTVHLD 610 620 630 640 650 660 GQEVTCRGAL ALPSAQLDLL GLGLVEPGTQ CGPRMVCNSN HNCHCAPGWA PPFCDKPGFG 670 680 690 700 710 720 GSMDSGPVQA ENHDTFLLAM LLSVLLPLLP GAGLAWCCYR LPGAHLQRCS WGCRRDPACS 730 740 750 760 770 780 GPKDGPHRDH PLGGVHPMEL GPTATGQPWP LDPENSHEPS SHPEKPLPAV SPDPQADQVQ MPRSCLW
	Isoform 3 [UniParc]. Checksum: A60AC04E056CF264	FASTA	309	32,554
	10 20 30 40 50 60 MGDCDLPEFC TGTSSHCPPD VYLLDGSPCA RGSGYCWDGA CPTLEQQCQQ LWGPGSHPAP 70 80 90 100 110 120 EACFQVVNSA GDAHGNCGQD SEGHFLPCAG RDALCGKLQC QGGKPSLLAP HMVPVDSTVH 130 140 150 160 170 180 LDGQEVTCRG ALALPSAQLD LLGLGLVEPG TQCGPRMVCN SNHNCHCAPG WAPPFCDKPG 190 200 210 220 230 240 FGGSMDSGPV QAENHDTFLL AMLLSVLLPL LPGAGLAWCC YRLPGAHLQR CSWGCRRDPA 250 260 270 280 290 300 CSGPKDGPHR DHPLGGVHPM ELGPTATGQP WPLDPENSHE PSSHPEKPLP AVSPDPQADQ VQMPRSCLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of novel mouse and human ADAM33s with potential metalloprotease activity." Yoshinaka T., Nishii K., Yamada K., Sawada H., Nishiwaki E., Smith K., Yoshino K., Ishiguro H., Higashiyama S. Gene 282:227-236(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Testis.
[2]	"Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness." Van Eerdewegh P., Little R.D., Dupuis J., Del Mastro R.G., Falls K., Simon J., Torrey D., Pandit S., McKenny J., Braunschweiger K., Walsh A., Liu Z., Hayward B., Folz C., Manning S.P., Bawa A., Saracino L., Thackston M. , Benchekroun Y., Capparell N., Wang M., Adair R., Feng Y., Dubois J., FitzGerald M.G., Huang H., Gibson R., Allen K.M., Pedan A., Danzig M.R., Umland S.P., Egan R.W., Cuss F.M., Rorke S., Clough J.B., Holloway J.W., Holgate S.T., Keith T.P. Nature 418:426-430(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INVOLVEMENT IN ASTHMA. Tissue: Uterus.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	NIEHS SNPs program Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-109; ALA-178; MET-272; ILE-316; SER-336; SER-365; GLU-441; ARG-515; HIS-612; ILE-710; GLY-739; TYR-742; THR-764 AND SER-774.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"ADAM33 haplotypes are associated with asthma in a large Australian population." Kedda M.A., Duffy D.L., Bradley B., O'Hehir R.E., Thompson P.J. Eur. J. Hum. Genet. 14:1027-1036(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
[7]	"Positionally cloned asthma susceptibility gene polymorphisms and disease risk in the British 1958 Birth Cohort." Blakey J.D., Sayers I., Ring S.M., Strachan D.P., Hall I.P. Thorax 64:381-387(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
[8]	"Crystal structure of the catalytic domain of human ADAM33." Orth P., Reichert P., Wang W., Prosise W.W., Yarosh-Tomaine T., Hammond G., Ingram R.N., Xiao L., Mirza U.A., Zou J., Strickland C., Taremi S.S., Le H.V., Madison V. J. Mol. Biol. 335:129-137(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 204-410 IN COMPLEX WITH METALLOPROTEASE INHIBITOR MARIMASTAT, X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 204-410.
[9]	"Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and ADAM7 are often mutated in melanoma." Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y. Hum. Mutat. 32:E2148-E2175(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-305.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB055891 mRNA. Translation: BAB83092.1.
AF466287 mRNA. Translation: AAM80482.1.
AF466288 Genomic DNA. Translation: AAM80483.1.
AY358314 mRNA. Translation: AAQ88680.1.
DQ995342 Genomic DNA. Translation: ABI97387.1.
AL109804, AL356755 Genomic DNA. Translation: CAI18840.1.

IPI

IPI00079482.
IPI00218715.
IPI00642419.

RefSeq

NP_079496.1. NM_025220.2.
NP_694882.1. NM_153202.1.

UniGene

Hs.173716.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R54	X-ray	1.85	A	204-409	[»]
1R55	X-ray	1.58	A	204-409	[»]

ProteinModelPortal

Q9BZ11.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BZ11. 2 interactions.

MINT

MINT-2876745.

STRING

9606.ENSP00000348912.

Protein family/group databases

MEROPS

M12.244.

PTM databases

PhosphoSite

Q9BZ11.

Polymorphism databases

DMDM

20137458.

Proteomic databases

PaxDb

Q9BZ11.

PRIDE

Q9BZ11.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000350009; ENSP00000322550; ENSG00000149451.
ENST00000356518; ENSP00000348912; ENSG00000149451.

GeneID

80332.

KEGG

hsa:80332.

UCSC

uc002wis.3. human.
uc002wit.3. human.
uc002wiu.3. human.

Organism-specific databases

CTD

80332.

GeneCards

GC20M003596.

HGNC

HGNC:15478. ADAM33.

MIM

600807. phenotype.
607114. gene.

neXtProt

NX_Q9BZ11.

PharmGKB

PA24526.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG294463.

HOGENOM

HOG000230883.

HOVERGEN

HBG006978.

InParanoid

Q9BZ11.

KO

K08616.

OMA

DGSPCAR.

OrthoDB

EOG4CJVGF.

PhylomeDB

Q9BZ11.

Gene expression databases

ArrayExpress

Q9BZ11.

Bgee

Q9BZ11.

CleanEx

HS_ADAM33.

Genevestigator

Q9BZ11.

GermOnline

ENSG00000149451. Homo sapiens.

Family and domain databases

Gene3D

3.40.390.10. 1 hit.
4.10.70.10. 1 hit.

InterPro

IPR006586. 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]

Pfam

PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]

PRINTS

PR00289. DISINTEGRIN.

SMART

SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF57552. Disintegrin. 1 hit.

PROSITE

PS50215. ADAM_MEPRO. 1 hit.
PS00546. CYSTEINE_SWITCH. False negative.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9BZ11.

ChEMBL

CHEMBL6121.

EvolutionaryTrace

Q9BZ11.

GenomeRNAi

80332.

NextBio

70880.

SOURCE

Search...

Entry information

Entry name

ADA33_HUMAN

Accession

Primary (citable) accession number: Q9BZ11
Secondary accession number(s): A0A1K6 , Q5JT75, Q5JT76, Q8N0W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 27, 2002
Last modified:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.