ID A0A091VJ97_NIPNI Unreviewed; 971 AA.
AC A0A091VJ97;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 17 {ECO:0000313|EMBL:KFR02568.1};
DE Flags: Fragment;
GN ORFNames=Y956_09702 {ECO:0000313|EMBL:KFR02568.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR02568.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFR02568.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR02568.1};
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; KL411013; KFR02568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VJ97; -.
DR STRING; 128390.A0A091VJ97; -.
DR MEROPS; M12.027; -.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000053283; 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 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; 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:KFR02568.1};
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:UP000053283};
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 84..304
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 924..963
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 242
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 241
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 245
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 251
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 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 160..225
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 200..207
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 219..299
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 258..283
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 328..352
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 339..360
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 347..379
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 373..384
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 407..444
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 411..449
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 422..434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR02568.1"
FT NON_TER 971
FT /evidence="ECO:0000313|EMBL:KFR02568.1"
SQ SEQUENCE 971 AA; 108860 MW; 864CDF85F06E6E3D CRC64;
GQVGYIQIGS EHMLIQPVNT SETSFSGKEH FIRRRRSTKS SHPMKSHIPD EHCKVVAEKK
RQKKMKSTSD WRERRNAIRL TNEYTVETLV VADADMVQYH GAEAAQRFIL TVMNMVYNMF
QHQSLGIKVS IRVTKLVLLR NRPAKLSIGH HGERSLESFC QWQNEEYGGA KYLGNNQVPG
ARDDTPPVDA AVFVTRTDFC VHKDEPCDTV GIAYLGGVCS AKRKCVLAED NGLNLAFTIA
HELGHNMGMS HDDDHQPCAG RSHIMSGEWV KGRNPSDLSW SSCSRDDLEN FLKSKVSTCL
LVTDPRSQYA VRLPHKLPGM HYSADEQCQI LFGTNATFCK NMEHLMCAGL WCLVEGDTSC
KTKLDPPLDG TECGADKWCR AGECVSKTPI PEHVDGDWSL WSQWSMCSRT CGTGVRFRQR
KCDNPPPGPG GKNCRGASVE HTVCENLPCP KGVPSFRDQQ CQAHDRYTNK KKSLLTAVIV
DDKPCELFCS PLGKDSPVLV TDRVLDGTPC GPYETDLCVH GKCQKIGCDG IIGSAAKEDR
CGICSGDGKT CKVVKGDFNH TKGMGYIEAA VIPAGARRIR VVEDKPAHSF LALKDSSKRS
INSDWKIELP GEFQIAGTTV RYVRRGLWEK ISAKGPTKIP LHLMVLLFHD QNYGIHYEYT
IPVNYTAENR SEPEKQQDSL YIWTHSGWEG CSVQCGGGER KTIVSCTRII NKTMTLVNDS
DCQRVNRPEP QVRKCNTHPC QSRWVTGHWS PCSATCEKGV QHREVTCVYQ LQNGTYVNTR
DLYCLGNKPT TVQSCEGRDC LSIWEASEWS KCSADCGKGI QKRTVTCTNS QGKCDAATRP
RDEEECEDHT GCYEWKTGDW SKCSSTCGKG LQSRVVQCMH KVTGRHGNEC PVLSKPAAYR
QCHQEVCNEK INVNTITSPR LAALTYKCTG DQWTVYCRVI REKNLCQDMR WYQRCCQTCR
DFYANKMQQK S
//
