ID A0A1V4J7Z5_PATFA Unreviewed; 822 AA.
AC A0A1V4J7Z5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 15 {ECO:0000313|EMBL:OPJ68165.1};
GN Name=ADAMTS15 {ECO:0000313|EMBL:OPJ68165.1};
GN ORFNames=AV530_013686 {ECO:0000313|EMBL:OPJ68165.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ68165.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ68165.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ68165.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ68165.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ68165.1}.
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DR EMBL; LSYS01008642; OPJ68165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4J7Z5; -.
DR STRING; 372326.A0A1V4J7Z5; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing 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; -; 2.
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; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 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; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:OPJ68165.1};
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:UP000190648};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..822
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012234768"
FT DOMAIN 88..297
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 677..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 231
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 235
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 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 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 163..215
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 192..197
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 209..292
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 247..276
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 318..340
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 329..350
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 335..369
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 363..374
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 398..435
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 402..440
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 413..425
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 822 AA; 89587 MW; A5C2F519AA063A65 CRC64;
MLPLLPLLLL GAPGLSLPSG GAPADTDLLS AFGEDFYLHL TPDAHFIAPA FATHYLGRRS
PAHPALDKYR GRGGGKGGRA KRFASVPRYV ETLVVADESM VKFHGDDLQH YLLTLMATAA
RLYKHPSIRN PIQISVVKFL LIGQDDKGPK VTSNAALTLR NFCAWQKKWN KVSDKHPEYW
DTAILFTKQD LCGATTCDTL GMADVGTMCD PKRSCSVIED DGLPSAFTTA HELGHVFNMP
HDNVKACEEV FGRLKTNHMM SPTLIQIDRA NPWSACSAAI ITDFLDSGHG DCLLDQPTKP
IPLPEDLPGS SYSLNQQCEL AFGVGSKPCP YMQYCAKLWC TGKARGQIVC QTRHFPWADG
TGCGDGRFCL KGSCVERHNI SKYRVDGGWA KWAPYGQCSR SCGGGVQLAK RECTDPVPAN
GGSYCEGVRL KYRSCNLEPC SAAVPGKSFR EEQCEAFNGY SHSTNRLTAS VSWVPKYSGV
SPRDKCKLIC RANGTGYFYV LAPKVVDGTP CSPDSTSVCV QGKCIKAGCD GKLGSKKKFD
KCSVCGGDNK SCKKVSGLFT KPMHGYNFVV VIPAGASNID IRQRGYKGLI SDDNYLALKN
GQGKYLLNGH FIVSAVERDL MVKGSVLRYS GTGTAVESLQ AFKPIQEPLT LEVLSVGKMT
PPRVRYSFYL PKESKEDKSS YKKEGKTPPD LNNSVLSLSN RLDSGRPSYK RPSYKWAAGG
WEACSVTCGD GLQKRSVACR DSHGHPAAEC DAAQRPADVR LCGEPCPAWE AGPWSPCSKS
CGRGFKRRAL KCAVPAGRSL PRESCNFRRK PQELDFCTLR PC
//
