ID I3M3V6_ICTTR Unreviewed; 1218 AA.
AC I3M3V6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 16 {ECO:0000313|Ensembl:ENSSTOP00000003805.3};
GN Name=ADAMTS16 {ECO:0000313|Ensembl:ENSSTOP00000003805.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003805.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000003805.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGTP01081696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01081705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M3V6; -.
DR STRING; 43179.ENSSTOP00000003805; -.
DR Ensembl; ENSSTOT00000004238.3; ENSSTOP00000003805.3; ENSSTOG00000004197.3.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159433; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; I3M3V6; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000005215; 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:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR013273; ADAMTS/ADAMTS-like.
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 PANTHER; PTHR13723:SF140; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 16; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
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.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
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}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1218
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012316663"
FT DOMAIN 290..495
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1180..1217
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 433
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 437
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 443
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 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 366..417
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 392..399
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 411..490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 450..474
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..623
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 590..628
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 601..613
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1218 AA; 134147 MW; 7FD96CD5B0C8973D CRC64;
RGDPAMRVPD CATLWVLLLA QVCQAPACAM DPAAAASGSP SVPHLSPPPE RPGGMETGEY
DLVSAYEVDS RGDYVSHDIV HHQRRRRALA QPGGDSLHLR LKGSRHDFQV DLKASSNLVA
PGFVVQTLGK RGTKAVQMFP PEDFCFYQGS LRSHRNSSVA LSTCQGLAGM IRTEEADYFL
TPLPPHLAGR LKGSEQGGPA SHVLYKRAVE PQAPQAPPGL LLTRTGEPAS PGLQGLSDNL
GLWHRQHFCG RRKKYAPQPP TEDLFVLPDE YESVPRCRRS LLKSHRNKEL NVETLVVVDR
KMMQSHGQEN ITTYVLTILN MVSALFKDGT IGGNINIAVV GLILLEDEQP GLVISHHADH
TLSSFCQWQS GLMGKDGTRH DHAILLTGLD ICSWKNEPCD TLGFAPISGM CSKYRSCTIN
EDTGLGLAFT IAHESGHNFG MVHDGEGNMC KKSEGNIMSP TLAGRNGVFS WSPCSRQYLH
KFLSTTQAVC LADQPKPGKE YKYPEKLPGE LYDANTQCKW QFGEKAKLCM LDFKKAIYNE
IKRKIDKEYS PAATPWCRGG QCVKYGAEGP KPTHGHWSDW SPWSPCSRTC GGGVSHRDRL
CTNPRPSHGG KFCEGPTRTL KLCNSQPCPP DSMDFRAAQC AAYNSQRFRG WHYKWKPYTQ
VAGKPEPTLG HSPGFVTFAY QLCDWQRGCQ GTLTPPCGVG SAAHSNEGWC SLRVGCDNIL
GSDAAEDSCG VCRGNNSDCT THRGVYTAHH HTNQYYHVVT LPPGARSIRI YEMNTSTSYI
SVRNALKRYY LNGHWTVDWP GRYEFAGTTF RYRRSYKEPE SLTAAGPTNE TLMVELLFQG
RNPGISWEYS VPRSGAEKKP SAQPSYTWAI VRSECSVSCG GGQMVTKEGC YRDLKFQVNT
SFCSPKTRPI TGLVSCKVSA CPPSWSVGNW STCSRTCGGG TQSRPVRCTQ RANYKTETVL
ASLCPQPVPS SRQACNSQSC PPAWSAGPWA ECSQTCGKGW RKRAVACKST NPSARAQLLP
DATCTAEPKP RTHEPCLLRR CHKHKKLQWL VSAWSKCSAT CERGTQKRFL KCAEKYVSGK
YRELASRKCL HVPKPDLELA RPCALFPCPA YPLQAAAGPP RGSWVASPWS QCSASCGGGV
QRRSVQCMAG GRPASDCSPH QKPESSLACN THFCTIPEKK DTFCKDYFHW CHLVPQHGMC
SHKFYGKQCC KTCSKSNL
//
