ID H0ZEQ5_TAEGU Unreviewed; 1105 AA.
AC H0ZEQ5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 08-NOV-2023, entry version 65.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 17 {ECO:0000313|Ensembl:ENSTGUP00000009067.2};
GN Name=ADAMTS17 {ECO:0000313|Ensembl:ENSTGUP00000009067.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000009067.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000009067.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000009067.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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 AlphaFoldDB; H0ZEQ5; -.
DR STRING; 59729.ENSTGUP00000009067; -.
DR Ensembl; ENSTGUT00000009164.2; ENSTGUP00000009067.2; ENSTGUG00000008763.2.
DR GeneTree; ENSGT00940000158773; -.
DR HOGENOM; CLU_000660_8_0_1; -.
DR InParanoid; H0ZEQ5; -.
DR OMA; TCVMAKA; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000007754; Chromosome 10.
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: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; IPR002870; Peptidase_M12B_N.
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; PF01562; Pep_M12B_propep; 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:ARBA00022801};
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:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1105
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025557716"
FT DOMAIN 218..438
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1058..1097
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 375
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 379
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 385
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 433
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 294..359
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 334..341
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 353..433
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 392..417
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 462..486
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 473..494
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 507..518
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 541..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 545..583
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 556..568
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1105 AA; 123391 MW; E43D0A11BD2ADF18 CRC64;
MFDGCLLPLV VPCLLLCGLD AGTAGGAELE MVIPERVPLE KIHLLQPGGD RGGPRRRRAA
AEQEEEEEAV LLRLPAAGAE LYLHLRRDLR FLARGFAVER RRGEARRPPR ERLCFFSGHA
LNRSDSFATL STCAGLVGYI QLGSEQLLIQ PVNASETSFS GKEHFIRRRR STKPGHPSWP
QGPEEHCKVV AEKKRQKKVK STSDWRERRN AIRLTSEYTV ETLVVADADM VQYHGAEAAQ
RFILTVMNMV YNMFQHQSLG IKVNIRVTKL VLLHSRPAKL SIGHHGERSL ESFCQWQNEE
YGGAKYLGNN QVPGARDDTP PVDAAVFVTR TDFCVHKDEP CDTVGIAYLG GVCSAKRKCV
LAEDNGLNLA FTIAHELGHN MGMSHDDDHQ PCAGRSHIMS GEWVKGRNPS DLSWSSCSRD
DLENFLKSKV STCLLLTDPR SQYSVRLPHK LPGMHYSADE QCQILFGTNA TFCKNMEYLM
CAGLWCLVEG DTSCKTKLDP PLDGTECGAD KWCRAGECVS KTPIPEHVDG DWSVWSQWSM
CSRTCGTGVR FRQRKCDNPP PGPGGKNCRG ASVEHTVCEN LPCPKGVPSF RDQQCQAHDR
YTNKKKSLLT AVIVDDKPCE LFCSPLGKDS PVLVTDRVLD GTPCGPYETD LCVHGKCQKI
GCDGIIGSAA KEDRCGICSG DGKTCKVVKG DFNHTKGMGY IEAAVIPAGA RRIRVVEDKP
AHSFLALKDS SKRSINSDWK IELPGEFQIA GTTVRYVRRG LWEKISAKGP TKIPLHLMVL
LFHDQNYGIH YEYTIPVNYT AENRSEPEKQ QDSLYIWTHS GWEGCSVQCG GGERKTIVSC
TRLINKTMTL VNDSDCQRVT RPEPQVRKCN THPCQSRWVT GHWSPCSATC EKGVQHREVT
CVYQLQNGSY VNTRDLYCLG SKPATVQSCE GRDCLSIWEA SEWSKCSADC GRGIQKRTVT
CTNSQGKCDA ATKPRDEEEC EDHTGCYEWK TGDWSKCSST CGKGLQSRVV QCMHKVTGRH
GSECPVLAKP AAYRQCHQEV CNDRINVNTI TSPRLAALTY KCTGDQWTVY CRVIREKNLC
QDMRWYQRCC QTCRDFYANK MQQKS
//