ID   AD22_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   28-FEB-2003 (Rel. 41, 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   ADAM22 OR MDC2.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A. (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
RT   in brain tissues and gliomas.";
RL   Jpn. J. Cancer Res. 91:1001-1006(2000).
RN   [2]
RP   SEQUENCE FROM N.A. (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   SEQUENCE FROM N.A. (ISOFORM 5).
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   SEQUENCE OF 40-906 FROM N.A. (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   MEDLINE=99453762; PubMed=10524237;
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).
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       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: HIGLY EXPRESSED IN THE BRAIN. DETECTED SLIGHLY
CC       OR NOT AT ALL IN OTHER TISSUES.
CC   -!- PTM: THE PRECURSOR IS CLEAVED BY A FURIN ENDOPEPTIDASE (BY
CC       SIMILARITY).
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY M12B.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
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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   Genew; HGNC:201; ADAM22.
DR   MIM; 603709; -.
DR   GO; GO:0016021; C:integral to membrane; NAS.
DR   GO; GO:0005178; F:integrin binding activity; 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; IPR002870; Pep_M12B_propep.
DR   InterPro; IPR001590; Reprolysin.
DR   InterPro; IPR006025; Zn_MTpeptdse.
DR   Pfam; PF00200; disintegrin; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   ProDom; PD000664; Disintegrin; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 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; PS00142; ZINC_PROTEASE; FALSE_NEG.
KW   Signal; Glycoprotein; Transmembrane; EGF-like domain;
KW   Alternative splicing.
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-LIKE.
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   CONFLICT     81     81       P -> R (IN REF. 3 AND 4).
SQ   SEQUENCE   906 AA;  100432 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
//