ID A0A1S3F034_DIPOR Unreviewed; 751 AA.
AC A0A1S3F034;
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 20-like {ECO:0000313|RefSeq:XP_012869097.1};
GN Name=LOC105983678 {ECO:0000313|RefSeq:XP_012869097.1};
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_012869097.1};
RN [1] {ECO:0000313|RefSeq:XP_012869097.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012869097.1};
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_012869097.1; XM_013013643.1.
DR AlphaFoldDB; A0A1S3F034; -.
DR GeneID; 105983678; -.
DR KEGG; dord:105983678; -.
DR InParanoid; A0A1S3F034; -.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; 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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 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; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR PANTHER; PTHR11905:SF167; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 4-RELATED; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 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; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..751
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010215450"
FT TRANSMEM 705..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 206..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 409..495
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 641..674
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 467..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 664..673
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 751 AA; 84780 MW; 1961E1B20EF0ADCE CRC64;
MRAAWAQGLL PGALWLPVLW TLLSPACCSY GPPGWRFTSS EIVIPRKVPH RKGGIKMPDQ
LAYSMRFRGQ RHVFHMKLKK NLLPRHLPVI TDSNQEGMQE DYPFLPGDCY YYSYLEGVPG
SLATLDTCHG GLRGRIQVDD FTYEIKPLET SSTFEHVISL LVVEERGEAS QRCDIGEEET
KPVFEDLELL GSPRAGTYYL WRKHPKDTRV MYIVSYSYIN HFKNQTLVLE HVMIINSIID
TIYKPTGFNI RVRFVLLWDT TDAVSLEINN AFAFLRNFGR WMHSTWQHRV SHSISVLIAG
QLIAEKNHYA VQGAICNDRW AVLFVAARRF HVFLASTMIA HTLGHQFNMA HDSPHCLCFR
RTHCLMTPVP NLQDTISNCS YPATHQWVLK WDTCMWQLNV PYESFRYVAP RCGDKIINQL
EDCDCGSFKE CASDKCCGTD CMFTPGSKCN EGDCCQDCKF SPPGTICRDI GGICDLTEYC
DGQSEKCPND TYIQDGTPCS PRAVCMRGNC SDRETQCQAL FGRNIKDGAA ECYKQLNMIG
DRFGNCGMKS QRGGPRIVKC SKENFMCGML HCSGLSNIPG GGEHTAFRHL SVRYEQVEHH
CFGYDAHFGT ELPQMGMVVD GAMCAPGRFC FEKNCTSHVD LNFDCDVRRC NYKGVCNNNH
NCHCMPGWKP PTCEEKGQGG SEDSGPPGGR QQRLRTYIHV DMHRIIPLML ARLILYLLSI
LAGAIPAIKS AVTNRLFKVV PEAKPPKKPP K
//
