GenomeNet

Database: UniProt
Entry: H0ZEQ5_TAEGU
LinkDB: H0ZEQ5_TAEGU
Original site: H0ZEQ5_TAEGU 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system