ID A0A1S3GFA8_DIPOR Unreviewed; 755 AA.
AC A0A1S3GFA8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 11 isoform X2 {ECO:0000313|RefSeq:XP_012887506.1};
GN Name=Adam11 {ECO:0000313|RefSeq:XP_012887506.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012887506.1};
RN [1] {ECO:0000313|RefSeq:XP_012887506.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012887506.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012887506.1; XM_013032052.1.
DR AlphaFoldDB; A0A1S3GFA8; -.
DR STRING; 10020.ENSDORP00000002702; -.
DR GeneID; 105997575; -.
DR CTD; 4185; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000081671; 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:UP000081671};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 721..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 225..424
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 430..517
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 659..696
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 489..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 686..695
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 755 AA; 81843 MW; 4158092734A18337 CRC64;
MALSPPGLGA QGPSGALHWR GSPQVGSPEA PEVTEPSRLV RESSGGEVRK QQLDTRVRQE
RPGGPPVHLA QVSFVIPAFN SNFTLDLELN HHLLSSQYVE RHFSREGTTQ HSTGAGDHCY
YQGKLRGNPH SFAALSTCQG LHGVFSDGNL TYIVEPQEMA GPWGAPHGPL PHLIYRTPLL
PAPLGCREPG CLFAASAHSA LPNLPRLRRK RQVRRGHATV HSETKYVELI VINDHQLFEQ
MRQSVVLTSN FAKSVVNLAD VIYKEQLNTR IVLVAMETWA DGDKIQVQDD LLETLSRLMV
YRREGLPEPS DATHLFSGRT FQSTSSGAAY VGGICSLSRG GGVNEYGNMG AMAVTLAQTL
GQNLGMMWNK HRSSAGDCKC PDIWLGCIME DTGFYLPRKF SRCSIDEYNQ FLQEGGGSCL
FNKPLKLLDP PECGNGFVEA GEECDCGSVQ ECSRAGGNCC KKCTLTHDAM CSDGLCCRRC
KYEPRGVSCR EAVNECDIAE TCTGDSSQCP PNLHKLDGYY CDHEQGRCYG GRCKTRDRQC
QALWGHVAAD RFCYEKLNVE GTERGNCGRK GSGWVQCNKQ DVLCGFLLCV NISGAPRLGD
LGGDISSVTF YHQGKELDCR GGHVQLADGS DLSYVEDGTA CGPNMLCLDH RCLPASAFNF
STCPGSGERR ICSHHGVCSN EGKCICQPDW TGKDCSIHNP LPTSPPTGET ERYKGPSGTN
IIIGSIAGAV LVAAIVLGGT GWGFKNIRRG RSGGA
//
