ID ADA22_HUMAN STANDARD; PRT; 906 AA. AC Q9P0K1; O75075; O75076; Q9P0K2; Q9UIA1; Q9UKK2; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE ADAM 22 precursor (A disintegrin and metalloproteinase domain 22) DE (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein DE 2) (Metalloproteinase-disintegrin ADAM22-3). GN Name=ADAM22; Synonyms=MDC2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2). RX MEDLINE=20504287; PubMed=11050470; RA Harada T., Nishie A., Torigoe K., Ikezaki K., Shono T., Maehara Y., RA Kuwano M., Wada M.; RT "The specific expression of three novel splice variant forms of human RT metalloprotease-like disintegrin-like cysteine-rich protein 2 gene in RT brain tissues and gliomas."; RL Jpn. J. Cancer Res. 91:1001-1006(2000). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS 3 AND 4). RC TISSUE=Brain; RX MEDLINE=98359734; PubMed=9693107; RA Sagane K., Ohya Y., Hasegawa Y., Tanaka I.; RT "Metalloproteinase-like, disintegrin-like, cysteine-rich proteins MDC2 RT and MDC3: novel human cellular disintegrins highly expressed in the RT brain."; RL Biochem. J. 334:93-98(1998). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 5), AND VARIANT ARG-81. RC TISSUE=Brain; RA Wada M., Torigoe K., Harada T., Kuwano M.; RT "Isolation and tissue specific expression of novel ADAM family from RT 7q21.1 region."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE OF 40-906 (ISOFORM 1), AND VARIANT ARG-81. RC TISSUE=Cerebellum; RX MEDLINE=99453762; PubMed=10524237; DOI=10.1016/S0378-1119(99)00302-9; RA Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.; RT "The identification of seven metalloproteinase-disintegrin (ADAM) RT genes from genomic libraries."; RL Gene 237:61-70(1999). RN [5] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004). CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non CC catalytic metalloprotease-like protein. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=Epsilon; CC IsoId=Q9P0K1-1; Sequence=Displayed; CC Name=2; Synonyms=Delta; CC IsoId=Q9P0K1-2; Sequence=VSP_005482, VSP_005484; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay; CC Name=3; Synonyms=Alpha; CC IsoId=Q9P0K1-3; Sequence=VSP_005483; CC Name=4; Synonyms=Beta; CC IsoId=Q9P0K1-4; Sequence=VSP_005482, VSP_005483; CC Name=5; CC IsoId=Q9P0K1-5; Sequence=VSP_005482; CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. Detected CC slighly or not at all in other tissues. CC -!- PTM: The precursor is cleaved by a furin endopeptidase (By CC similarity). CC -!- SIMILARITY: Belongs to the peptidase M12B family. CC -!- SIMILARITY: Contains 1 disintegrin domain. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF155382; AAF73289.1; -. DR EMBL; AF155381; AAF73288.1; -. DR EMBL; AB009671; BAA32349.1; -. DR EMBL; AB009671; BAA32350.1; -. DR EMBL; AF073291; AAF22476.2; -. DR EMBL; AF158637; AAD55251.1; -. DR HSSP; P18619; 1FVL. DR MEROPS; M12.978; -. DR Ensembl; ENSG00000008277; Homo sapiens. DR Genew; HGNC:201; ADAM22. DR MIM; 603709; -. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0005178; F:integrin binding; NAS. DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS. DR InterPro; IPR006586; ADAM_cysteine. DR InterPro; IPR001762; Disintegrin. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR006210; IEGF. DR InterPro; IPR006025; Pept_M_Zn_BS. DR InterPro; IPR001590; Peptidase_M12B. DR InterPro; IPR002870; Peptidase_M12B_N. DR Pfam; PF00200; Disintegrin; 1. DR Pfam; PF01562; Pep_M12B_propep; 1. DR Pfam; PF01421; Reprolysin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR ProDom; PD000664; Disintegrin; 1. DR SMART; SM00608; ACR; 1. DR SMART; SM00050; DISIN; 1. DR SMART; SM00181; EGF; 1. DR PROSITE; PS50215; ADAM_MEPRO; 1. DR PROSITE; PS00427; DISINTEGRIN_1; FALSE_NEG. DR PROSITE; PS50214; DISINTEGRIN_2; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; FALSE_NEG. DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG. KW Alternative splicing; EGF-like domain; Glycoprotein; Polymorphism; KW Signal; Transmembrane. FT SIGNAL 1 25 Potential. FT PROPEP 26 222 By similarity. FT CHAIN 223 906 ADAM 22. FT DOMAIN 223 736 Extracellular (Potential). FT TRANSMEM 737 757 Potential. FT DOMAIN 758 906 Cytoplasmic (Potential). FT DOMAIN 223 438 Metalloprotease-like. FT DOMAIN 444 531 Disintegrin. FT DOMAIN 532 678 Cys-rich. FT DOMAIN 675 712 EGF-like. FT DISULFID 349 433 By similarity. FT DISULFID 503 516 Potential. FT DISULFID 679 694 By similarity. FT DISULFID 688 700 By similarity. FT DISULFID 702 711 By similarity. FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 519 519 N-linked (GlcNAc...) (Potential). FT CARBOHYD 634 634 N-linked (GlcNAc...) (Potential). FT CARBOHYD 675 675 N-linked (GlcNAc...) (Potential). FT VARSPLIC 768 803 Missing (in isoform 2, isoform 4 and FT isoform 5). FT /FTId=VSP_005482. FT VARSPLIC 860 906 Missing (in isoform 3 and isoform 4). FT /FTId=VSP_005483. FT VARSPLIC 859 859 E -> EYLNPWFKRDYNVAKWVEDVNKNTEEPYFR (in FT isoform 2). FT /FTId=VSP_005484. FT VARIANT 81 81 P -> R (in dbSNP:2279542). FT /FTId=VAR_020057. SQ SEQUENCE 906 AA; 100433 MW; 265ECCD0FA6C088B CRC64; MQAAVAVSVP FLLLCVLGTC PPARCGQAGD ASLMELEKRK ENRFVERQSI VPLRLIYRSG GEDESRHDAL DTRVRGDLGG PQLTHVDQAS FQVDAFGTSF ILDVVLNHDL LSSEYIERHI EHGGKTVEVK GGEHCYYQGH IRGNPDSFVA LSTCHGLHGM FYDGNHTYLI EPEENDTTQE DFHFHSVYKS RLFEFSLDDL PSEFQQVNIT PSKFILKPRP KRSKRQLRRY PRNVEEETKY IELMIVNDHL MFKKHRLSVV HTNTYAKSVV NMADLIYKDQ LKTRIVLVAM ETWATDNKFA ISENPLITLR EFMKYRRDFI KEKSDAVHLF SGSQFESSRS GAAYIGGICS LLKGGGVNEF GKTDLMAVTL AQSLAHNIGI ISDKRKLASG ECKCEDTWSG CIMGDTGYYL PKKFTQCNIE EYHDFLNSGG GACLFNKPSK LLDPPECGNG FIETGEECDC GTPAECVLEG AECCKKCTLT QDSQCSDGLC CKKCKFQPMG TVCREAVNDC DIRETCSGNS SQCAPNIHKM DGYSCDGVQG ICFGGRCKTR DRQCKYIWGQ KVTASDKYCY EKLNIEGTEK GNCGKDKDTW IQCNKRDVLC GYLLCTNIGN IPRLGELDGE ITSTLVVQQG RTLNCSGGHV KLEEDVDLGY VEDGTPCGPQ MMCLEHRCLP VASFNFSTCL SSKEGTICSG NGVCSNELKC VCNRHWIGSD CNTYFPHNDD AKTGITLSGN GVAGTNIIIG IIAGTILVLA LILGITAWGY KNYREQRQLP QGDYVKKPGD GDSFYSDIPP GVSTNSASSS KKRSNGLSHS WSERIPDTKH ISDICENGRP RSNSWQGNLG GNKKKIRGKR FRPRSNSTET LSPAKSPSSS TGSIASSRKY PYPMPPLPDE DKKVNRQSAR LWETSI //