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Q9UKF2

- ADA30_HUMAN

UniProt

Q9UKF2 - ADA30_HUMAN

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Protein
Disintegrin and metalloproteinase domain-containing protein 30
Gene
ADAM30, UNQ2509/PRO5997
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

May be involved in spermatogenesis and fertilization.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Zinc; in inhibited form By similarity
Metal bindingi338 – 3381Zinc; catalytic By similarity
Active sitei339 – 3391 By similarity
Metal bindingi342 – 3421Zinc; catalytic By similarity
Metal bindingi348 – 3481Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: ProtInc
  3. zinc ion binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. binding of sperm to zona pellucida Source: Reactome
  2. multicellular organism reproduction Source: Reactome
  3. single fertilization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_163933. Interaction With The Zona Pellucida.

Protein family/group databases

MEROPSiM12.232.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 30 (EC:3.4.24.-)
Short name:
ADAM 30
Gene namesi
Name:ADAM30
ORF Names:UNQ2509/PRO5997
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:208. ADAM30.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini199 – 687489Extracellular Reviewed prediction
Add
BLAST
Transmembranei688 – 70821Helical; Reviewed prediction
Add
BLAST
Topological domaini709 – 79082Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: ProtInc
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Propeptidei28 – 198171 By similarity
PRO_0000029136Add
BLAST
Chaini199 – 790592Disintegrin and metalloproteinase domain-containing protein 30
PRO_0000029137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi222 – 2221N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi313 ↔ 388 By similarity
Disulfide bondi353 ↔ 373 By similarity
Disulfide bondi355 ↔ 361 By similarity
Glycosylationi372 – 3721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi438 – 4381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi457 ↔ 477 By similarity
Glycosylationi473 – 4731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi625 – 6251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi633 ↔ 644 By similarity
Disulfide bondi638 ↔ 650 By similarity
Disulfide bondi652 ↔ 661 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9UKF2.
PRIDEiQ9UKF2.

PTM databases

PhosphoSiteiQ9UKF2.

Expressioni

Tissue specificityi

Expressed specifically in testis.

Gene expression databases

BgeeiQ9UKF2.
CleanExiHS_ADAM30.
GenevestigatoriQ9UKF2.

Organism-specific databases

HPAiHPA026080.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000358407.

Structurei

3D structure databases

ProteinModelPortaliQ9UKF2.
SMRiQ9UKF2. Positions 199-625.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini203 – 393191Peptidase M12B
Add
BLAST
Domaini399 – 48587Disintegrin
Add
BLAST
Domaini629 – 66335EGF-like
Add
BLAST
Repeati732 – 74091
Repeati741 – 74992
Repeati750 – 75893
Repeati759 – 76794
Repeati768 – 77695

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni732 – 776455 X 9 AA approximate repeats
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi170 – 1778Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi486 – 632147Cys-rich
Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 disintegrin domain.
Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG276852.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9UKF2.
KOiK08615.
OMAiLQCINVK.
OrthoDBiEOG7FFMR2.
PhylomeDBiQ9UKF2.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. 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]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q9UKF2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRSVQIFLSQ CRLLLLLVPT MLLKSLGEDV IFHPEGEFDS YEVTIPEKLS    50
FRGEVQGVVS PVSYLLQLKG KKHVLHLWPK RLLLPRHLRV FSFTEHGELL 100
EDHPYIPKDC NYMGSVKESL DSKATISTCM GGLRGVFNID AKHYQIEPLK 150
ASPSFEHVVY LLKKEQFGNQ VCGLSDDEIE WQMAPYENKA RLRDFPGSYK 200
HPKYLELILL FDQSRYRFVN NNLSQVIHDA ILLTGIMDTY FQDVRMRIHL 250
KALEVWTDFN KIRVGYPELA EVLGRFVIYK KSVLNARLSS DWAHLYLQRK 300
YNDALAWSFG KVCSLEYAGS VSTLLDTNIL APATWSAHEL GHAVGMSHDE 350
QYCQCRGRLN CIMGSGRTGF SNCSYISFFK HISSGATCLN NIPGLGYVLK 400
RCGNKIVEDN EECDCGSTEE CQKDRCCQSN CKLQPGANCS IGLCCHDCRF 450
RPSGYVCRQE GNECDLAEYC DGNSSSCPND VYKQDGTPCK YEGRCFRKGC 500
RSRYMQCQSI FGPDAMEAPS ECYDAVNLIG DQFGNCEITG IRNFKKCESA 550
NSICGRLQCI NVETIPDLPE HTTIISTHLQ AENLMCWGTG YHLSMKPMGI 600
PDLGMINDGT SCGEGRVCFK KNCVNSSVLQ FDCLPEKCNT RGVCNNRKNC 650
HCMYGWAPPF CEEVGYGGSI DSGPPGLLRG AIPSSIWVVS IIMFRLILLI 700
LSVVFVFFRQ VIGNHLKPKQ EKMPLSKAKT EQEESKTKTV QEESKTKTGQ 750
EESEAKTGQE ESKAKTGQEE SKANIESKRP KAKSVKKQKK 790
Length:790
Mass (Da):88,940
Last modified:May 10, 2004 - v2
Checksum:i42EC8A5F6B5ACDA3
GO
Isoform Beta (identifier: Q9UKF2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     763-771: Missing.

Show »
Length:781
Mass (Da):87,981
Checksum:iEC875E91BA95B28F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti359 – 3591L → P.2 Publications
Corresponds to variant rs2641348 [ dbSNP | Ensembl ].
VAR_024597
Natural varianti737 – 7371T → A.
Corresponds to variant rs35273427 [ dbSNP | Ensembl ].
VAR_061738

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei763 – 7719Missing in isoform Beta.
VSP_005494

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361S → P in AAF03781. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171932 mRNA. Translation: AAF03780.1.
AF171933 mRNA. Translation: AAF03781.1.
AY358734 mRNA. Translation: AAQ89096.1.
AK292483 mRNA. Translation: BAF85172.1.
AL359752 Genomic DNA. Translation: CAI18978.1.
CCDSiCCDS907.1. [Q9UKF2-1]
RefSeqiNP_068566.2. NM_021794.3. [Q9UKF2-1]
UniGeneiHs.283011.

Genome annotation databases

EnsembliENST00000369400; ENSP00000358407; ENSG00000134249. [Q9UKF2-1]
GeneIDi11085.
KEGGihsa:11085.
UCSCiuc001eij.3. human. [Q9UKF2-1]

Polymorphism databases

DMDMi47117918.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF171932 mRNA. Translation: AAF03780.1 .
AF171933 mRNA. Translation: AAF03781.1 .
AY358734 mRNA. Translation: AAQ89096.1 .
AK292483 mRNA. Translation: BAF85172.1 .
AL359752 Genomic DNA. Translation: CAI18978.1 .
CCDSi CCDS907.1. [Q9UKF2-1 ]
RefSeqi NP_068566.2. NM_021794.3. [Q9UKF2-1 ]
UniGenei Hs.283011.

3D structure databases

ProteinModelPortali Q9UKF2.
SMRi Q9UKF2. Positions 199-625.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000358407.

Protein family/group databases

MEROPSi M12.232.

PTM databases

PhosphoSitei Q9UKF2.

Polymorphism databases

DMDMi 47117918.

Proteomic databases

PaxDbi Q9UKF2.
PRIDEi Q9UKF2.

Protocols and materials databases

DNASUi 11085.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369400 ; ENSP00000358407 ; ENSG00000134249 . [Q9UKF2-1 ]
GeneIDi 11085.
KEGGi hsa:11085.
UCSCi uc001eij.3. human. [Q9UKF2-1 ]

Organism-specific databases

CTDi 11085.
GeneCardsi GC01M120436.
HGNCi HGNC:208. ADAM30.
HPAi HPA026080.
MIMi 604779. gene.
neXtProti NX_Q9UKF2.
PharmGKBi PA24525.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG276852.
HOGENOMi HOG000230883.
HOVERGENi HBG006978.
InParanoidi Q9UKF2.
KOi K08615.
OMAi LQCINVK.
OrthoDBi EOG7FFMR2.
PhylomeDBi Q9UKF2.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_163933. Interaction With The Zona Pellucida.

Miscellaneous databases

GenomeRNAii 11085.
NextBioi 42148.
PROi Q9UKF2.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKF2.
CleanExi HS_ADAM30.
Genevestigatori Q9UKF2.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProi 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 ]
Pfami PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view ]
PRINTSi PR00289. DISINTEGRIN.
SMARTi SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression."
    Cerretti D.P., DuBose R.F., Black R.A., Nelson N.
    Biochem. Biophys. Res. Commun. 263:810-815(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), VARIANT PRO-359.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT PRO-359.
    Tissue: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiADA30_HUMAN
AccessioniPrimary (citable) accession number: Q9UKF2
Secondary accession number(s): A8K8W8, Q5T3X6, Q9UKF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 10, 2004
Last modified: September 3, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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