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 03-APR-2013, entry version 79.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 to membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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; Disintegrin; 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; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG.
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
//
