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Q60718 (ADAM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 2

Short name=ADAM 2
Alternative name(s):
Fertilin subunit beta
PH-30
Short name=PH30
PH30-beta
Gene names
Name:Adam2
Synonyms:Ftnb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length735 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein By similarity.

Subunit structure

Heterodimer with ADAM1/fertilin subunit alpha.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed specifically in testis.

Domain

A tripeptide motif (QDE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding By similarity.

Post-translational modification

The signal and the metalloprotease domain are cleaved during the epididymal maturation of the spermatozoa.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 180162 By similarity
PRO_0000029046
Chain181 – 735555Disintegrin and metalloproteinase domain-containing protein 2
PRO_0000029047

Regions

Topological domain19 – 686668Extracellular Potential
Transmembrane687 – 70721Helical; Potential
Topological domain708 – 73528Cytoplasmic Potential
Domain184 – 381198Peptidase M12B
Domain389 – 47688Disintegrin
Domain615 – 64834EGF-like
Compositional bias480 – 611132Cys-rich

Amino acid modifications

Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Potential
Disulfide bond293 ↔ 376 By similarity
Disulfide bond335 ↔ 360 By similarity
Disulfide bond337 ↔ 342 By similarity
Disulfide bond449 ↔ 469 By similarity
Disulfide bond619 ↔ 630 By similarity
Disulfide bond624 ↔ 636 By similarity
Disulfide bond638 ↔ 647 By similarity

Experimental info

Sequence conflict21W → R in AAD04207. Ref.2
Sequence conflict17 – 204LSQS → IRHE in AAA74921. Ref.4
Sequence conflict24 – 252GT → A in AAA74921. Ref.4
Sequence conflict1131I → M in AAA90980. Ref.1
Sequence conflict234 – 2429LEFWMDENK → WNFGWMKQ in AAA74921. Ref.4
Sequence conflict246 – 2472TG → QA in AAA74921. Ref.4
Sequence conflict2861A → L in AAA74921. Ref.4
Sequence conflict331 – 3322DV → RRL in AAA74921. Ref.4
Sequence conflict3821R → T in AAD04207. Ref.2
Sequence conflict6581S → T in AAA74921. Ref.4
Sequence conflict6791A → R in AAD04207. Ref.2
Sequence conflict7121Q → P in AAA90980. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60718 [UniParc].

Last modified February 1, 2003. Version 2.
Checksum: 75EC8529CF5B8E2B

FASTA73582,375
        10         20         30         40         50         60 
MWLILLLLSG LSELGGLSQS QTEGTREKLH VQVTVPEKIR SVTSNGYETQ VTYNLKIEGK 

        70         80         90        100        110        120 
TYTLDLMQKP FLPPNFRVYS YDNAGIMRSL EQKFQNICYF QGYIEGYPNS MVIVSTCTGL 

       130        140        150        160        170        180 
RGFLQFGNVS YGIEPLESSS GFEHVIYQVE PEKGGALLYA EKDIDLRDSQ YKIRSIKPQR 

       190        200        210        220        230        240 
IVSHYLEIHI VVEKQMFEHI GADTAIVTQK IFQLIGLANA IFAPFNLTVI LSSLEFWMDE 

       250        260        270        280        290        300 
NKILTTGDAN KLLYRFLKWK QSYLVLRPHD MAFLLVYRNT TDYVGATYQG KMCDKNYAGG 

       310        320        330        340        350        360 
VALHPKAVTL ESLAIILVQL LSLSMGLAYD DVNKCQCGVP VCVMNPEAPH SSGVRAFSNC 

       370        380        390        400        410        420 
SMEDFSKFIT SQSSHCLQNQ PRLQPSYKMA VCGNGEVEED EICDCGKKGC AEMPPPCCNP 

       430        440        450        460        470        480 
DTCKLSDGSE CSSGICCNSC KLKRKGEVCR LAQDECDVTE YCNGTSEVCE DFFVQNGHPC 

       490        500        510        520        530        540 
DNRKWICING TCQSGEQQCQ DLFGIDAGFG SSECFWELNS KSDISGSCGI SAGGYKECPP 

       550        560        570        580        590        600 
NDRMCGKIIC KYQSENILKL RSATVIYANI SGHVCVSLEY PQGHNESQKM WVRDGTVCGS 

       610        620        630        640        650        660 
NKVCQNQKCV ADTFLGYDCN LEKCNHHGVC NNKKNCHCDP TYLPPDCKRM KDSYPGGSID 

       670        680        690        700        710        720 
SGNKERAEPI PVRPYIASAY RSKSPRWPFF LIIPFYVVIL VLIGMLVKVY SQRMKWRMDD 

       730 
FSSEEQFESE SESKD 

« Hide

References

« Hide 'large scale' references
[1]"Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta."
Evans J.P., Schultz R.M., Kopf G.S.
J. Cell Sci. 108:3267-3278(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]Gupta S.K., Alves K., Palladino L.O., Mark G.E., Hollis G.F.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[4]"ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain."
Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.-P., Primakoff P., Myles D.G., White J.M.
Dev. Biol. 169:378-383(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-735.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16242 mRNA. Translation: AAA90980.1.
U38806 mRNA. Translation: AAD04207.1.
AK016550 mRNA. Translation: BAB30298.1.
U22057 mRNA. Translation: AAA74921.1.
CCDSCCDS36959.1.
RefSeqNP_033748.2. NM_009618.2.
UniGeneMm.422850.

3D structure databases

ProteinModelPortalQ60718.
SMRQ60718. Positions 185-610.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.950.

PTM databases

PhosphoSiteQ60718.

Proteomic databases

PaxDbQ60718.
PRIDEQ60718.

Protocols and materials databases

DNASU11495.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022618; ENSMUSP00000022618; ENSMUSG00000022039.
GeneID11495.
KEGGmmu:11495.
UCSCuc007uju.1. mouse.

Organism-specific databases

CTD2515.
MGIMGI:1340894. Adam2.

Phylogenomic databases

eggNOGNOG242228.
GeneTreeENSGT00750000117474.
HOGENOMHOG000230883.
HOVERGENHBG103628.
InParanoidQ60718.
KOK06833.
OMACGKLICK.
OrthoDBEOG7HB58N.
PhylomeDBQ60718.
TreeFamTF314733.

Gene expression databases

BgeeQ60718.
CleanExMM_ADAM2.
GenevestigatorQ60718.

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.
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]
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.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278874.
PROQ60718.
SOURCESearch...

Entry information

Entry nameADAM2_MOUSE
AccessionPrimary (citable) accession number: Q60718
Secondary accession number(s): Q60814, Q9D4G3, Q9QWJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot