ID L5KKG4_PTEAL Unreviewed; 320 AA.
AC L5KKG4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 12 {ECO:0000313|EMBL:ELK11827.1};
DE Flags: Fragment;
GN ORFNames=PAL_GLEAN10008986 {ECO:0000313|EMBL:ELK11827.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK11827.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KB030668; ELK11827.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KKG4; -.
DR STRING; 9402.L5KKG4; -.
DR MEROPS; M12.212; -.
DR InParanoid; L5KKG4; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF112; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 12; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Integrin {ECO:0000313|EMBL:ELK11827.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 141..320
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK11827.1"
SQ SEQUENCE 320 AA; 35451 MW; 2626188ED281AC17 CRC64;
VTYQCDSTLS FLFVSHRGLI ASGFTETHYL QDGTDVSLTR NYTGHCFYHG HVQGYPGSTV
SLSTCSGLRG LITFGNKTYV LEPLKNVTNR YKLFPAETLT GVWGPCGSQA STSGLAADGS
LPSPSRTRET RHKRETLKMT KYVELVIVAD NREFQRQGKD LEKVKQRLIE IANHVDKFYR
PLNIRIVLVG VEVWNDIDKC SVSQDPFATL HEFLDWRKMK LLPRKPHDNA QLISGVYFQG
TTIGMAPIMS MCTAEQSGGV VMDHSDSPLG AAVTLAHELG HNFGMNHDTL ERGCRCTMAA
DKGGCIMNPS TGQVLMLHCF
//
