ID A0A091DFJ8_FUKDA Unreviewed; 949 AA.
AC A0A091DFJ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1 {ECO:0000313|EMBL:KFO21566.1};
GN ORFNames=H920_16996 {ECO:0000313|EMBL:KFO21566.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21566.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO21566.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO21566.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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; KN124353; KFO21566.1; -; Genomic_DNA.
DR RefSeq; XP_010606873.1; XM_010608571.2.
DR AlphaFoldDB; A0A091DFJ8; -.
DR STRING; 885580.ENSFDAP00000005348; -.
DR MEROPS; M12.222; -.
DR GeneID; 104851405; -.
DR CTD; 9510; -.
DR eggNOG; KOG3538; Eukaryota.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013274; Pept_M12B_ADAM-TS1.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR613274-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:KFO21566.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..949
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001871988"
FT DOMAIN 240..449
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 180..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT DISULFID 315..367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..349
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 361..444
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 399..428
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 470..493
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 488..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 516..527
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 553..590
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 557..595
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 568..580
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 949 AA; 103557 MW; AA103510A493BDDE CRC64;
MGKAERPPRS RSSQPAPWLL LLLAATPVLL TVPGALGRPA VEDEELVLPA LERALGHETT
RLRLDAFGQQ LHLELQPDRV FLAPGFTLQT VGRKPEPEAQ RLDPTGDLAH CFYSGTVNGD
PSSAAALSLC EGVRGAFYLQ GEEFFIQPAP ASATERLAPS AAKEEPFGLP QFHLLRRRRR
GGGGSKCGVL DAETLPARGA EPEGEDAGAQ RPLRDPALPR AGQPTGTGSV RKKRFVSSPR
YVETMLVADQ SMAEFHGSGL KHYLLTLFSV AARLYKHPSI RNSVSLVVVK ILVIYEEQKG
PEVTSNAAFT LRNFCSWQKQ HNPPSDRDAE HYDTAILFTR QDLCGAQTCD TLGMADVGTV
CDPSRSCSVI EDDGLQAAFT TAHELGHVFN MPHDDAKQCA SLNGMTQDSH MMASMLSNLD
RSQPWSPCSA YMITSFLDNG HGECLMDKPQ NSIQLPSDLP GTLYDANRQC QFTFGEESKH
CPDAASTCAT LWCTGTSGGL LVCQTKHFPW ADGTSCGEGK WCVNSKCVNK TDKKHFDTPV
HGSWGPWGPW GDCSRTCGGG VQYTMRECDN PVPKNGGKYC EGKRVRYRSC NIEDCPDSNG
KTFREEQCEA HNEFSKASFG SGPAVEWTPK YAGVSPKDRC KLICQAKGIG YFFVLQPKVV
DGTPCSPDST SVCVQGQCVK AGCDRIIDSK KKFDKCGICG GNGSTCKKIS GSVTSAKPGY
HDIVTIPTGA TNIEVKQRNQ RGSRDNGSFL AIRAADGTYI LNGDFTLSTL EQDITYKGVV
LRYSGSSAAL ERIRSFSPLK EPLTIQVLTV GNALRPKIKY TYFVKKKKES FNAIPTFSEW
VIEEWSECSK SCGLGWQRRL VECKDINGQP ASECAKEVKP ASTRPCADTP CPHWQLGDWS
PCSKTCGKGY KKRTLKCLSH DGGVLSHESC DPLKKPKHYI DFCTIAECS
//
