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Protein

Disintegrin and metalloproteinase domain-containing protein 2

Gene

Adam2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

  • adult behavior Source: MGI
  • cell adhesion Source: MGI
  • visual learning Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_301180. Interaction With The Zona Pellucida.

Protein family/group databases

MEROPSiM12.950.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Adam2
Synonyms:Ftnb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1340894. Adam2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 686668ExtracellularSequence AnalysisAdd
BLAST
Transmembranei687 – 70721HelicalSequence AnalysisAdd
BLAST
Topological domaini708 – 73528CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 180162By similarityPRO_0000029046Add
BLAST
Chaini181 – 735555Disintegrin and metalloproteinase domain-containing protein 2PRO_0000029047Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi293 ↔ 376By similarity
Disulfide bondi335 ↔ 360By similarity
Disulfide bondi337 ↔ 342By similarity
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi449 ↔ 469By similarity
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi585 – 5851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi619 ↔ 630By similarity
Disulfide bondi624 ↔ 636By similarity
Disulfide bondi638 ↔ 647By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ60718.
PRIDEiQ60718.

PTM databases

PhosphoSiteiQ60718.

Expressioni

Tissue specificityi

Expressed specifically in testis.

Gene expression databases

BgeeiQ60718.
CleanExiMM_ADAM2.
GenevestigatoriQ60718.

Interactioni

Subunit structurei

Heterodimer with ADAM1/fertilin subunit alpha.

Structurei

3D structure databases

ProteinModelPortaliQ60718.
SMRiQ60718. Positions 185-610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini184 – 381198Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 47688DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini615 – 64834EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi480 – 611132Cys-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242228.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG103628.
InParanoidiQ60718.
KOiK06833.
OMAiCGKLICK.
OrthoDBiEOG7HB58N.
PhylomeDBiQ60718.
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.
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]
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.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLILLLLSG LSELGGLSQS QTEGTREKLH VQVTVPEKIR SVTSNGYETQ
60 70 80 90 100
VTYNLKIEGK TYTLDLMQKP FLPPNFRVYS YDNAGIMRSL EQKFQNICYF
110 120 130 140 150
QGYIEGYPNS MVIVSTCTGL RGFLQFGNVS YGIEPLESSS GFEHVIYQVE
160 170 180 190 200
PEKGGALLYA EKDIDLRDSQ YKIRSIKPQR IVSHYLEIHI VVEKQMFEHI
210 220 230 240 250
GADTAIVTQK IFQLIGLANA IFAPFNLTVI LSSLEFWMDE NKILTTGDAN
260 270 280 290 300
KLLYRFLKWK QSYLVLRPHD MAFLLVYRNT TDYVGATYQG KMCDKNYAGG
310 320 330 340 350
VALHPKAVTL ESLAIILVQL LSLSMGLAYD DVNKCQCGVP VCVMNPEAPH
360 370 380 390 400
SSGVRAFSNC SMEDFSKFIT SQSSHCLQNQ PRLQPSYKMA VCGNGEVEED
410 420 430 440 450
EICDCGKKGC AEMPPPCCNP DTCKLSDGSE CSSGICCNSC KLKRKGEVCR
460 470 480 490 500
LAQDECDVTE YCNGTSEVCE DFFVQNGHPC DNRKWICING TCQSGEQQCQ
510 520 530 540 550
DLFGIDAGFG SSECFWELNS KSDISGSCGI SAGGYKECPP NDRMCGKIIC
560 570 580 590 600
KYQSENILKL RSATVIYANI SGHVCVSLEY PQGHNESQKM WVRDGTVCGS
610 620 630 640 650
NKVCQNQKCV ADTFLGYDCN LEKCNHHGVC NNKKNCHCDP TYLPPDCKRM
660 670 680 690 700
KDSYPGGSID SGNKERAEPI PVRPYIASAY RSKSPRWPFF LIIPFYVVIL
710 720 730
VLIGMLVKVY SQRMKWRMDD FSSEEQFESE SESKD
Length:735
Mass (Da):82,375
Last modified:February 1, 2003 - v2
Checksum:i75EC8529CF5B8E2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21W → R in AAD04207 (Ref. 2) Curated
Sequence conflicti17 – 204LSQS → IRHE in AAA74921 (PubMed:7750654).Curated
Sequence conflicti24 – 252GT → A in AAA74921 (PubMed:7750654).Curated
Sequence conflicti113 – 1131I → M in AAA90980 (PubMed:7593287).Curated
Sequence conflicti234 – 2429LEFWMDENK → WNFGWMKQ in AAA74921 (PubMed:7750654).Curated
Sequence conflicti246 – 2472TG → QA in AAA74921 (PubMed:7750654).Curated
Sequence conflicti286 – 2861A → L in AAA74921 (PubMed:7750654).Curated
Sequence conflicti331 – 3322DV → RRL in AAA74921 (PubMed:7750654).Curated
Sequence conflicti382 – 3821R → T in AAD04207 (Ref. 2) Curated
Sequence conflicti658 – 6581S → T in AAA74921 (PubMed:7750654).Curated
Sequence conflicti679 – 6791A → R in AAD04207 (Ref. 2) Curated
Sequence conflicti712 – 7121Q → P in AAA90980 (PubMed:7593287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16242 mRNA. Translation: AAA90980.1.
U38806 mRNA. Translation: AAD04207.1.
AK016550 mRNA. Translation: BAB30298.1.
U22057 mRNA. Translation: AAA74921.1.
CCDSiCCDS36959.1.
RefSeqiNP_033748.2. NM_009618.2.
UniGeneiMm.422850.

Genome annotation databases

EnsembliENSMUST00000022618; ENSMUSP00000022618; ENSMUSG00000022039.
GeneIDi11495.
KEGGimmu:11495.
UCSCiuc007uju.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16242 mRNA. Translation: AAA90980.1.
U38806 mRNA. Translation: AAD04207.1.
AK016550 mRNA. Translation: BAB30298.1.
U22057 mRNA. Translation: AAA74921.1.
CCDSiCCDS36959.1.
RefSeqiNP_033748.2. NM_009618.2.
UniGeneiMm.422850.

3D structure databases

ProteinModelPortaliQ60718.
SMRiQ60718. Positions 185-610.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.950.

PTM databases

PhosphoSiteiQ60718.

Proteomic databases

PaxDbiQ60718.
PRIDEiQ60718.

Protocols and materials databases

DNASUi11495.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022618; ENSMUSP00000022618; ENSMUSG00000022039.
GeneIDi11495.
KEGGimmu:11495.
UCSCiuc007uju.1. mouse.

Organism-specific databases

CTDi2515.
MGIiMGI:1340894. Adam2.

Phylogenomic databases

eggNOGiNOG242228.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG103628.
InParanoidiQ60718.
KOiK06833.
OMAiCGKLICK.
OrthoDBiEOG7HB58N.
PhylomeDBiQ60718.
TreeFamiTF314733.

Enzyme and pathway databases

ReactomeiREACT_301180. Interaction With The Zona Pellucida.

Miscellaneous databases

NextBioi278874.
PROiQ60718.
SOURCEiSearch...

Gene expression databases

BgeeiQ60718.
CleanExiMM_ADAM2.
GenevestigatoriQ60718.

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

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiADAM2_MOUSE
AccessioniPrimary (citable) accession number: Q60718
Secondary accession number(s): Q60814, Q9D4G3, Q9QWJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: May 27, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.