GenomeNet

Database: UniProt
Entry: Q9PSZ3
LinkDB: Q9PSZ3
Original site: Q9PSZ3 
ID   ADA11_XENLA             Reviewed;         452 AA.
AC   Q9PSZ3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   14-MAY-2014, entry version 82.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 11;
DE            Short=ADAM 11;
DE   AltName: Full=MDC11.1;
DE   AltName: Full=Metalloprotease-disintegrin MDC11a;
DE   AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein;
DE            Short=MDC;
DE   Flags: Fragment;
GN   Name=adam11; Synonyms=mdc11a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
RT   metalloprotease-disintegrins in early Xenopus laevis development.";
RL   Dev. Biol. 204:508-524(1998).
CC   -!- FUNCTION: Probable ligand for integrin in the brain. This is a
CC       non-catalytic metalloprotease-like protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Detected in testis and barely expressed in
CC       heart and muscle. Not detectable in liver.
CC   -!- DEVELOPMENTAL STAGE: Could not be detected in embryos until
CC       neurulation. In developing embryos, the expression is restricted
CC       to neural crest derivatives.
CC   -!- DOMAIN: A conserved motif [AVN[ED]CD] within the disintegrin-like
CC       domain could be involved in the binding to the integrin receptor.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
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DR   EMBL; AF032384; AAC61848.1; -; mRNA.
DR   UniGene; Xl.21440; -.
DR   ProteinModelPortal; Q9PSZ3; -.
DR   Xenbase; XB-GENE-966542; adam11.
DR   HOVERGEN; HBG050456; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 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   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN        <1    452       Disintegrin and metalloproteinase domain-
FT                                containing protein 11.
FT                                /FTId=PRO_0000078206.
FT   TOPO_DOM     <1    417       Extracellular (Potential).
FT   TRANSMEM    418    438       Helical; (Potential).
FT   TOPO_DOM    439    452       Cytoplasmic (Potential).
FT   DOMAIN       <1    120       Peptidase M12B.
FT   DOMAIN      126    214       Disintegrin.
FT   DOMAIN      360    416       EGF-like.
FT   COMPBIAS    215    359       Cys-rich.
FT   CARBOHYD    149    149       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    288    288       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    356    356       N-linked (GlcNAc...) (Potential).
FT   DISULFID     31    115       By similarity.
FT   DISULFID     74     99       By similarity.
FT   DISULFID     76     83       By similarity.
FT   DISULFID    186    206       By similarity.
FT   DISULFID    360    375       By similarity.
FT   DISULFID    369    381       By similarity.
FT   DISULFID    383    392       By similarity.
FT   NON_TER       1      1
SQ   SEQUENCE   452 AA;  48577 MW;  DF1F66C24CCD6847 CRC64;
     RRHHSPLLVS LIGGQTFKSS HSGAAYFGGI CSPTHGGGVN EYGNIGAMAI TLAQTLGQNL
     GMMWNKPRTT TGDCKCPDLW RGCIMEDTGF YLPQKFSRCS VDEYSKFLQD GGGSCLFNKP
     LKLLDPPSCG NGFIEIGEEC DCGSPAECNK SRAGNCCKKC TLSHDAMCSD GLCCRGCKYE
     PRGTVCRESL NECDVPEACP GDSSACPANL HKQDGYFCDN EQGRCFGGRC KTRDRQCHAL
     WGRGASDRFC YEKLNIEGTE KGNCGRDRQN WIQCSKQDVL CGYLLCSNIS GIPQIGELNG
     DITSMSFYHQ NRYLDCRGGQ VTLPDGSCLG YVEDGTPCGP NMICLDRRCL PASAFNFSTC
     PGSWNGVICS DHGVCSNEGK CICHPEWTGK DCSVYDPLPV PKPTGVVEKY KGPSGTNIII
     GSIAGAVLIA AIVLGGTGWG FKNIRRGRSG GG
//
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