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Database: UniProt
Entry: A0A091RCU4_MERNU
LinkDB: A0A091RCU4_MERNU
Original site: A0A091RCU4_MERNU 
ID   A0A091RCU4_MERNU        Unreviewed;       761 AA.
AC   A0A091RCU4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17 {ECO:0000313|EMBL:KFQ37077.1};
DE   Flags: Fragment;
GN   ORFNames=N331_03459 {ECO:0000313|EMBL:KFQ37077.1};
OS   Merops nubicus (Northern carmine bee-eater).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX   NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ37077.1, ECO:0000313|Proteomes:UP000052967};
RN   [1] {ECO:0000313|EMBL:KFQ37077.1, ECO:0000313|Proteomes:UP000052967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ37077.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KK717026; KFQ37077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091RCU4; -.
DR   MEROPS; M12.027; -.
DR   Proteomes; UP000052967; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; 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   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; 5.
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; IPR001590; Peptidase_M12B.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13723:SF151; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 17; 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; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Integrin {ECO:0000313|EMBL:KFQ37077.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          1..94
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          714..753
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   ACT_SITE        32
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         31
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         35
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         41
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         89
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   DISULFID        9..89
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   DISULFID        48..73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        118..142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        129..150
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        137..169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        163..174
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        197..234
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        201..239
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        212..224
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ37077.1"
FT   NON_TER         761
FT                   /evidence="ECO:0000313|EMBL:KFQ37077.1"
SQ   SEQUENCE   761 AA;  84644 MW;  80DECA3A0E615A55 CRC64;
     GIAYLGGVCS AKRKCVLAED NGLNLAFTIA HELGHNMGMS HDDDHQPCAG RSHIMSGEWV
     KGRNPSDLSW SSCSRDDLEN FLKSKVSTCL LVTDPRSQYA VRLPHKLPGM HYSADEQCQI
     LFGTNATFCK NMEHLMCAGL WCLVEGDTSC KTKLDPPLDG TECGADKWCR AGECVSKTPI
     PEHVDGDWSV WSPWSMCSRT CGTGVRFRQR KCDNPPPGPG GKNCRGASVE HTVCENLPCP
     KGVPSFRDQQ CQAHDRYTNK KKSLLTAVIV DDKPCELFCS PLGKESPVLV ADRVLDGTPC
     GPYETDLCVH GKCQKIGCDG IIGSAAKEDR CGVCSGDGKT CKVVKGDFNH TKGMGYIEAA
     VIPAGARRIR VVEDKPAHSF LALKDSSKRS INSDWKIELP GEFQIAGTTV RYVRRGLWEK
     ISAKGPTKIP LHLMVTLYPL FNYGIHYEYT IPVNYTAENR SEPEKQQDSL YIWTHSGWEG
     CSVQCGGGER RTVVSCTRIV NKSMTVVNDS DCQRATRPEP QVRKCNTHPC QSRWVTGHWS
     PCSATCEKGV QHRDVTCVYQ LQNGTYVNTR DLYCLGNKPT TVQSCEGRDC LSIWEASEWS
     KCSADCGKGI QKRTVTCTNS QGKCDAATRP RDEEECEDHT GCYEWKTGDW SKCSSTCGKG
     LQSRVVQCMH KVTGRHGSEC PVLAKPAAYR QCHQEACNEK INVNTITSPR LAALTYKCTG
     DQWTVYCRVI REKNLCQDMR WYQRCCQTCR DFYANKMQQK S
//
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