ID ADA22_XENLA Reviewed; 935 AA.
AC O42596;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22;
DE Short=ADAM 22;
DE AltName: Full=MDC11.2;
DE AltName: Full=Metalloprotease-disintegrin MDC11b;
DE Flags: Precursor;
GN Name=adam22; Synonyms=mdc11b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9882486; DOI=10.1006/dbio.1998.9017;
RA Cai H., Kraetzschmar J., Alfandari D., Hunnicutt G., Blobel C.P.;
RT "Neural crest-specific and general expression of distinct metalloprotease-
RT disintegrins in early Xenopus laevis development.";
RL Dev. Biol. 204:508-524(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 464-511.
RC TISSUE=Testis;
RX PubMed=9205136; DOI=10.1006/dbio.1997.8586;
RA Shilling F.M., Kraetzschmar J., Cai H., Weskamp G., Gayko U., Leibow J.,
RA Myles D.G., Nuccitelli R., Blobel C.P.;
RT "Identification of metalloprotease/disintegrins in Xenopus laevis testis
RT with a potential role in fertilization.";
RL Dev. Biol. 186:155-164(1997).
CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non
CC catalytic metalloprotease-like protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1V6};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Low levels in adult tissues. Not detected in
CC developing embryos.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
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DR EMBL; AF032383; AAC61847.1; -; mRNA.
DR EMBL; U78188; AAB87148.1; -; mRNA.
DR RefSeq; NP_001080913.1; NM_001087444.1.
DR AlphaFoldDB; O42596; -.
DR SMR; O42596; -.
DR MEROPS; M12.978; -.
DR GlyCosmos; O42596; 6 sites, No reported glycans.
DR GeneID; 386621; -.
DR KEGG; xla:386621; -.
DR AGR; Xenbase:XB-GENE-957020; -.
DR CTD; 386621; -.
DR Xenbase; XB-GENE-957020; adam22.L.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 386621; Expressed in brain and 12 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..227
FT /evidence="ECO:0000250"
FT /id="PRO_0000029116"
FT CHAIN 228..935
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 22"
FT /id="PRO_0000029117"
FT TOPO_DOM 228..736
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 758..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 241..440
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 446..533
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 677..713
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 850..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 351..435
FT /evidence="ECO:0000250"
FT DISULFID 394..419
FT /evidence="ECO:0000250"
FT DISULFID 396..403
FT /evidence="ECO:0000250"
FT DISULFID 449..479
FT /evidence="ECO:0000250"
FT DISULFID 460..476
FT /evidence="ECO:0000250"
FT DISULFID 462..468
FT /evidence="ECO:0000250"
FT DISULFID 475..496
FT /evidence="ECO:0000250"
FT DISULFID 487..493
FT /evidence="ECO:0000250"
FT DISULFID 492..518
FT /evidence="ECO:0000250"
FT DISULFID 505..525
FT /evidence="ECO:0000250"
FT DISULFID 512..544
FT /evidence="ECO:0000250"
FT DISULFID 537..549
FT /evidence="ECO:0000250"
FT DISULFID 556..607
FT /evidence="ECO:0000250"
FT DISULFID 571..637
FT /evidence="ECO:0000250"
FT DISULFID 585..595
FT /evidence="ECO:0000250"
FT DISULFID 602..665
FT /evidence="ECO:0000250"
FT DISULFID 659..670
FT /evidence="ECO:0000250"
FT DISULFID 681..695
FT /evidence="ECO:0000250"
FT DISULFID 689..701
FT /evidence="ECO:0000250"
FT DISULFID 703..712
FT /evidence="ECO:0000250"
SQ SEQUENCE 935 AA; 104161 MW; 77B7AFDCC5C77C90 CRC64;
MHINGGPLAS WICCVIGSIH LAHASTRPEN GGTSGMQRKK ENSVLGMEDT VPLRLIFSNE
EDNQTTQGLL STRVRAGSPQ HQDQLTHVAQ ASFQIDAFGS SFILDVELNH DLLSSDYRER
HVTQDGKTVE VKGGEHCYYQ GQIRGKAKSF VALSTCNGLH GMFCDGNHTY LIEPGEKYNP
NEDYQFHSVY KSKVLEFPLD ELPSEFWALN DTSVRLSQQT RSQRKKRQTR RYPRNVEDET
KYVELMIVND HLMYKKHRLS VGHTNSYAKS VVNMADLIYK EQLNTRIVLV AMETWATDNK
FSISENPLLT LKEFMKYRRD FIKDKSDAVH LFSGSQLRVA AVVLRILVEW CSLLKGGGVN
EFGKPDVMAV TLAQSLAHNL GIFSDKKKLL SGECKCEDTW SGCIMGDIGY YLPSKFSVCN
IEEYHEFLNN GGGACLFNKP LKLLDPPECG NGFVETGEEC DCGTIAECAM EGEECCKKCT
LTQDSECSDG LCCSNCKFNP KEMLCREAVN DCDIPETCTG NTSQCPANIH KLDGYSCESM
QGLCFGGRCK TRDRQCKYIW GEKVSAADRY CYEKLNIEGT EKGNCGRNKE TWIQCNKQDV
LCGYLLCTNI SNVPRLGELD GDVTSSSIVN QGKLYNCSGG HVKLDEDTDL GYVEDGTPCG
TGMMCLEHRC LPIDSFNFST CLGSTNKICS GHGVCSNEVR CICDRFWTGE DCSSYLHYDH
IKPEGDNRDE GVISTNIIIG AIAGTILVLA LVLGITAWGY KNYRRERQIP QGDYVKKPGD
ADSFYSDLPP GVSSNSASSS KKRSAILSHF QISACSIPHY SISQNISLFC RRSNGLSHSW
SERIPDTKHV SDVCENGRPR SNSWQGNVTS SRKKLRGKRF RPRSNSTETL SPAKSPSSST
GSIASSRRYP YPMPPLPDEE RKASKQSARL WETSI
//
