Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Disintegrin and metalloproteinase domain-containing protein 22

Gene

adam22

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (By similarity).By similarity

GO - Molecular functioni

Protein family/group databases

MEROPSiM12.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 22
Short name:
ADAM 22
Alternative name(s):
MDC11.2
Metalloprotease-disintegrin MDC11b
Gene namesi
Name:adam22
Synonyms:mdc11b
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-957020. adam22.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini228 – 736ExtracellularSequence analysisAdd BLAST509
Transmembranei737 – 757HelicalSequence analysisAdd BLAST21
Topological domaini758 – 935CytoplasmicSequence analysisAdd BLAST178

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002911625 – 227By similarityAdd BLAST203
ChainiPRO_0000029117228 – 935Disintegrin and metalloproteinase domain-containing protein 22Add BLAST708

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi167N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi210N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi351 ↔ 435By similarity
Disulfide bondi394 ↔ 419By similarity
Disulfide bondi396 ↔ 403By similarity
Disulfide bondi449 ↔ 479By similarity
Disulfide bondi460 ↔ 476By similarity
Disulfide bondi462 ↔ 468By similarity
Disulfide bondi475 ↔ 496By similarity
Disulfide bondi487 ↔ 493By similarity
Disulfide bondi492 ↔ 518By similarity
Disulfide bondi505 ↔ 525By similarity
Disulfide bondi512 ↔ 544By similarity
Glycosylationi521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi537 ↔ 549By similarity
Disulfide bondi556 ↔ 607By similarity
Disulfide bondi571 ↔ 637By similarity
Disulfide bondi585 ↔ 595By similarity
Disulfide bondi602 ↔ 665By similarity
Glycosylationi609N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi636N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi659 ↔ 670By similarity
Glycosylationi677N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi681 ↔ 695By similarity
Disulfide bondi689 ↔ 701By similarity
Disulfide bondi703 ↔ 712By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Low levels in adult tissues. Not detected in developing embryos.

Structurei

3D structure databases

ProteinModelPortaliO42596.
SMRiO42596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini241 – 440Peptidase M12BPROSITE-ProRule annotationAdd BLAST200
Domaini446 – 533DisintegrinPROSITE-ProRule annotationAdd BLAST88
Domaini677 – 713EGF-likePROSITE-ProRule annotationAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi536 – 670Cys-richAdd BLAST135

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG050456.
KOiK16068.

Family and domain databases

CDDicd04269. ZnMc_adamalysin_II_like. 1 hit.
Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiView protein in InterPro
IPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR036436. Disintegrin_dom_sf.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom_sf.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
IPR034027. Reprolysin_adamalysin.
PfamiView protein in Pfam
PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PRINTSiPR00289. DISINTEGRIN.
SMARTiView protein in SMART
SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiView protein in PROSITE
PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O42596-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHINGGPLAS WICCVIGSIH LAHASTRPEN GGTSGMQRKK ENSVLGMEDT
60 70 80 90 100
VPLRLIFSNE EDNQTTQGLL STRVRAGSPQ HQDQLTHVAQ ASFQIDAFGS
110 120 130 140 150
SFILDVELNH DLLSSDYRER HVTQDGKTVE VKGGEHCYYQ GQIRGKAKSF
160 170 180 190 200
VALSTCNGLH GMFCDGNHTY LIEPGEKYNP NEDYQFHSVY KSKVLEFPLD
210 220 230 240 250
ELPSEFWALN DTSVRLSQQT RSQRKKRQTR RYPRNVEDET KYVELMIVND
260 270 280 290 300
HLMYKKHRLS VGHTNSYAKS VVNMADLIYK EQLNTRIVLV AMETWATDNK
310 320 330 340 350
FSISENPLLT LKEFMKYRRD FIKDKSDAVH LFSGSQLRVA AVVLRILVEW
360 370 380 390 400
CSLLKGGGVN EFGKPDVMAV TLAQSLAHNL GIFSDKKKLL SGECKCEDTW
410 420 430 440 450
SGCIMGDIGY YLPSKFSVCN IEEYHEFLNN GGGACLFNKP LKLLDPPECG
460 470 480 490 500
NGFVETGEEC DCGTIAECAM EGEECCKKCT LTQDSECSDG LCCSNCKFNP
510 520 530 540 550
KEMLCREAVN DCDIPETCTG NTSQCPANIH KLDGYSCESM QGLCFGGRCK
560 570 580 590 600
TRDRQCKYIW GEKVSAADRY CYEKLNIEGT EKGNCGRNKE TWIQCNKQDV
610 620 630 640 650
LCGYLLCTNI SNVPRLGELD GDVTSSSIVN QGKLYNCSGG HVKLDEDTDL
660 670 680 690 700
GYVEDGTPCG TGMMCLEHRC LPIDSFNFST CLGSTNKICS GHGVCSNEVR
710 720 730 740 750
CICDRFWTGE DCSSYLHYDH IKPEGDNRDE GVISTNIIIG AIAGTILVLA
760 770 780 790 800
LVLGITAWGY KNYRRERQIP QGDYVKKPGD ADSFYSDLPP GVSSNSASSS
810 820 830 840 850
KKRSAILSHF QISACSIPHY SISQNISLFC RRSNGLSHSW SERIPDTKHV
860 870 880 890 900
SDVCENGRPR SNSWQGNVTS SRKKLRGKRF RPRSNSTETL SPAKSPSSST
910 920 930
GSIASSRRYP YPMPPLPDEE RKASKQSARL WETSI
Length:935
Mass (Da):104,161
Last modified:May 1, 1999 - v2
Checksum:i77B7AFDCC5C77C90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032383 mRNA. Translation: AAC61847.1.
U78188 mRNA. Translation: AAB87148.1.
RefSeqiNP_001080913.1. NM_001087444.1.
UniGeneiXl.401.

Genome annotation databases

GeneIDi386621.
KEGGixla:386621.

Similar proteinsi

Entry informationi

Entry nameiADA22_XENLA
AccessioniPrimary (citable) accession number: O42596
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1999
Last modified: November 22, 2017
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program