ID A0A2K5DYU5_AOTNA Unreviewed; 755 AA.
AC A0A2K5DYU5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ADAM metallopeptidase domain 11 {ECO:0000313|Ensembl:ENSANAP00000026171.1};
GN Name=ADAM11 {ECO:0000313|Ensembl:ENSANAP00000026171.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000026171.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000026171.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A2K5DYU5; -.
DR Ensembl; ENSANAT00000044094.1; ENSANAP00000026171.1; ENSANAG00000030699.1.
DR GeneTree; ENSGT00940000159790; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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 Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
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 InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF114; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 11; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..755
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014447017"
FT TRANSMEM 731..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..438
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 444..531
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 669..706
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 503..523
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 696..705
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 755 AA; 81869 MW; EE25D32AAD533F09 CRC64;
MRLLQRWAFA ALLLPLLPTP GLGTRGPAGA LRWGGLSQLR GPEAPEVTEP SRLVRKSSGG
EVRKQQLDTR VRQEPPGGPP VHLAQVSFVI PAFNSNFTLD LELNHHLLSS QYVERHFSRE
GTTQHSTGAG DHCYYQGKLR GNAHSFAALS TCQGLHGVFS DGNVTYIVEP QEMAGPWGAP
QGPLPHLIYR TPLLPDPLRC REPGCLFAVP AQSAPPNHPR LRRKRQVRRG HPTVHSETKY
VELIVINDHQ LFEQMRQSVV LTSNFAKSVV NLADVIYKEQ LNTRIVLVAM ETWADGDKIQ
VQDDLLETLA RLMVYRREGL PEPSDATHLF SGRTFQSTSS GAAYVGGICS LSRGGGVNEY
GNMGAMAVTL AQTLGQNLGM MWNKHRSSAG DCKCPDIWLG CIMEDTGFYL PRKFSRCSID
EYNQFLQEGG GSCLFNKPLK LLDPPECGNG FVEAGEECDC GSVQECSRAG GNCCKKCTLT
HDAMCSDGLC CRRCKYEPRG VSCREAVNEC DIAETCTGDS SQCPANLHKL DGYYCDHEDP
GRQPGGQAKV DPGVCWAAAD RFCYEKLNVE GTERGSCGRK GSGWVQCSKQ DVLCGFLLCV
NISGAPRLGD LVGDISSVTF YHQGKELDCR GGHVQLADGS DLSYVEDGTA CGPNMLCLDH
RCLPASAFNF STCPGSGEHR ICSHHGVCSN EGKCICQPDW TGKDCSIHNP LPTSPPTGET
ERYKGPSGTN IIIGSIAGAV LVAAIVLGGT GWGFK
//
