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-AUG-2022, entry version 103.
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; 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).
CC   -!- FUNCTION: Probable ligand for integrin in the brain. This is a non-
CC       catalytic metalloprotease-like protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in testis and barely expressed in heart
CC       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 to
CC       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. {ECO:0000250}.
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DR   EMBL; AF032384; AAC61848.1; -; mRNA.
DR   AlphaFoldDB; Q9PSZ3; -.
DR   SMR; Q9PSZ3; -.
DR   MEROPS; M12.976; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0016021; C:integral component of 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; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           <1..452
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 11"
FT                   /id="PRO_0000078206"
FT   TOPO_DOM        <1..417
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        439..452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..120
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          126..214
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          360..416
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..99
FT                   /evidence="ECO:0000250"
FT   DISULFID        76..83
FT                   /evidence="ECO:0000250"
FT   DISULFID        186..206
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..375
FT                   /evidence="ECO:0000250"
FT   DISULFID        369..381
FT                   /evidence="ECO:0000250"
FT   DISULFID        383..392
FT                   /evidence="ECO:0000250"
FT   NON_TER         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