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Protein

Disintegrin and metalloproteinase domain-containing protein 2

Gene

Adam2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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

  • cell adhesion Source: UniProtKB-KW
  • male gonad development Source: RGD
  • spermatogenesis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69299. Adam2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 688670ExtracellularSequence analysisAdd
BLAST
Transmembranei689 – 70921HelicalSequence analysisAdd
BLAST
Topological domaini710 – 73728CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • 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_0000029050Add
BLAST
Chaini181 – 737557Disintegrin and metalloproteinase domain-containing protein 2PRO_0000029051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi293 ↔ 376By similarity
Disulfide bondi335 ↔ 360By similarity
Disulfide bondi337 ↔ 342By similarity
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence analysis
Disulfide bondi450 ↔ 470By similarity
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence analysis
Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence analysis
Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi621 ↔ 632By similarity
Disulfide bondi626 ↔ 638By similarity
Disulfide bondi640 ↔ 649By similarity
Modified residuei731 – 7311PhosphoserineCombined sources

Post-translational modificationi

The prodomain and the metalloprotease domain are cleaved during the epididymal maturation of the spermatozoa.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63202.
PRIDEiQ63202.

PTM databases

iPTMnetiQ63202.
PhosphoSiteiQ63202.

Interactioni

Subunit structurei

Heterodimer with ADAM1/fertilin subunit alpha.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061122.

Structurei

3D structure databases

ProteinModelPortaliQ63202.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini184 – 381198Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 47890DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini617 – 65034EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi482 – 616135Cys-richAdd
BLAST

Domaini

A tripeptide motif (NQE) 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

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
HOGENOMiHOG000230883.
HOVERGENiHBG103628.
InParanoidiQ63202.
KOiK06833.
PhylomeDBiQ63202.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR000742. EGF-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.

Q63202-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLLLLLLSG LSRLGGLSEP QTEGTREKLH VQVTVPEKIR SITSEGYETQ
60 70 80 90 100
VTYSLKIEGK TYILNLMQKA FLPPNFRVYS YDSTGIMRPL EQKFQNICYF
110 120 130 140 150
QGYIEGYPNS MVIVSTCTGL RGVLQFGNVS YGIEPLESSS GFEHVIYQVE
160 170 180 190 200
PKKGDTLLYA EKDMDLRDPQ YKIRSIKPQR TVSHYLEIHI VVEKQMFEHI
210 220 230 240 250
GADTAVVTQK IFQLIGLTNA IFAPFNLTVI LSSLEFWMDE NKISTTGDAN
260 270 280 290 300
KLLYRFLKWK QSYLVLRPHD MAFLLVYRDT TDYVGATYQG KMCDKNYAGG
310 320 330 340 350
VALHPKAVTL ESLAIILVQL LSLSMGVAYD DVNTCQCGVP ICVMNPEALH
360 370 380 390 400
SSGVRSFSNC SMEDFSKFIV SQSSHCLQNQ PHLQPSYKMA VCGNGELEEG
410 420 430 440 450
EVCDCGQEGC DDKPPPCCNP TTCQLSEGST CSTGSCCDAS CNLKAKGELC
460 470 480 490 500
RPANQECDVT EYCNGTSEVC EEDFFVQDGH PCAEQKWICI NGTCQSGAQQ
510 520 530 540 550
CRDLFGTDAD YGTKECYSEL NSKSDISGSC GITPTGYKDC APNDRMCGKL
560 570 580 590 600
ICIYQSEDIL KMRSAIVIYA NISGQICISL EYPPGHKESK KMCVRDGTVC
610 620 630 640 650
GSGKVCLNQE CVEDTFLNYD CTPEKCNHHG VCNNKKHCHC EPTYLPPDCK
660 670 680 690 700
NTEDTWPGGS VDSGNQQRAE SIPARSYVAS AYRSKSARWP FFLIIPFYVV
710 720 730
ILVLIGMLVK VYSQRKKWRM DDFSSEEQFE SESESKD
Length:737
Mass (Da):82,311
Last modified:February 1, 2003 - v2
Checksum:i647E92A90D7CC1D1
GO

Sequence cautioni

The sequence CAA68127.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99794 mRNA. Translation: CAA68127.1. Different initiation.
RefSeqiNP_064462.1. NM_020077.1.
UniGeneiRn.42917.

Genome annotation databases

GeneIDi56806.
KEGGirno:56806.
UCSCiRGD:69299. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99794 mRNA. Translation: CAA68127.1. Different initiation.
RefSeqiNP_064462.1. NM_020077.1.
UniGeneiRn.42917.

3D structure databases

ProteinModelPortaliQ63202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061122.

Protein family/group databases

MEROPSiM12.950.

PTM databases

iPTMnetiQ63202.
PhosphoSiteiQ63202.

Proteomic databases

PaxDbiQ63202.
PRIDEiQ63202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56806.
KEGGirno:56806.
UCSCiRGD:69299. rat.

Organism-specific databases

CTDi2515.
RGDi69299. Adam2.

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
HOGENOMiHOG000230883.
HOVERGENiHBG103628.
InParanoidiQ63202.
KOiK06833.
PhylomeDBiQ63202.

Miscellaneous databases

PROiQ63202.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR000742. EGF-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. "Cloning and sequence analysis of rat fertilin alpha and beta - developmental expression, processing and immunolocalization."
    McLaughlin E.A., Frayne J., Barker H.L., Jury J.A., Jones R., Ford W.C.L., Hall L.
    Mol. Hum. Reprod. 3:801-809(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiADAM2_RAT
AccessioniPrimary (citable) accession number: Q63202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: June 8, 2016
This is version 118 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.