ID I3M1F7_ICTTR Unreviewed; 1213 AA.
AC I3M1F7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 14 {ECO:0000313|Ensembl:ENSSTOP00000002648.3};
GN Name=ADAMTS14 {ECO:0000313|Ensembl:ENSSTOP00000002648.3};
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:ENSSTOP00000002648.3, 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:ENSSTOP00000002648.3}
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; AGTP01042446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01042447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01042448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01042449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M1F7; -.
DR STRING; 43179.ENSSTOP00000002648; -.
DR Ensembl; ENSSTOT00000002962.3; ENSSTOP00000002648.3; ENSSTOG00000002932.3.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158426; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; I3M1F7; -.
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:0030199; P:collagen fibril organization; IEA:Ensembl.
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; 4.
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 PANTHER; PTHR13723:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1213
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012294088"
FT DOMAIN 248..452
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1049..1087
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1090..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 391
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 390
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 394
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 400
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 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 325..374
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 368..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 407..433
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 474..499
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 485..508
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..527
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..532
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 556..593
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 560..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..583
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1213 AA; 132925 MW; 7917528229340767 CRC64;
MARLCALLSC LLPLHCSLCA AVGSQTPELR LSGKLSDYGV TVPFSTDFRG RFLSHVVSGP
AAASPLHSSH LRVARSPLHP EGETLKPGQV GRHFLYFNVT VFGKELHLCL RPNRRLVVPG
ASVEWQEDFR ELFRQPLQQE CVYTGGVTGM PGAAVAISNC DGLAGLIRTD SSDYFIEPLE
RGQQETEASG RTHVVYRREA VQREWAEPHG DLHNEAFGLG NLPNLLGLAG ARLGDAERKR
RHAKPGSYSI EVLLAVDDSV VRFHGKEHVQ NYVLTLMNIV DEIYHDESLG AHVNIVLVRL
VMVGYRQSLS LIERGNPSRS LEQVCRWAHS QQRQDPGHAE HHDHVIFLTR QNFGPSGMPG
YAPVTGMCHP LRSCALNHED GFSSAFVVAH ETGHVLGMEH DGQGNGCADE TSLGSVMAPL
VQAAFHRFHW SRCSKLELSR YLPSYDCLLD DPFEPTWPQP PELPGIDYSM DEQCRFDFGT
GYQTCLAFRT FEPCKQLWCS HPDNPYFCKT KKGPPLDGTE CAPGKWCFKG YCIWKSPEQI
YGQDGGWSSW TKFGSCSRSC GGGVRSRSRS CDNPPPAYGG RLCSGPSFEY QVCNPEECPG
PYEDFRAQQC AKRNSYYTHQ NTKHSWLPYE SEDDTQKCEL ICQSADTGDV VFMNQVVHDG
TRCSYRDPYS LCARGECVPV GCDKEVGSMK ADDKCGVCGG DNSHCRTVKG TLGKASKQAA
AAKLVQIPAG ARHIQMEALE KAPHRIVVKN QVTGSFIFNP KGKEATGRTF TALGLEWEHT
VEDAKDSLKT SGPLPEAIAV LVLPPTEGGP RGSLAYKYVI HEDLLPLIGS NNVLLEETDT
YEWALKSWAP CTKACGGGIQ FTKYGCRRRR DHHTVQRHLC DYRKRPKPIR RRCNQHPCSQ
PVWVTDEWST CSRSCGKLGV QTREVHCFLP LSNGTRKALP AKVCPGDRPE ARRPCLRVPC
PAQWRTGAWS QCSATCGEGI QQRQVVCRTN TNSLGQCEGD KPDTVQVCSL PACGGNLRNS
TVKAQEPVTP EGQWVPQSGP SPATNKIASV EPCAGDRSIF CHLEVLGRYC TIPGYHRLCC
ESCTKKASGP ATSPDPIMAS PPPFSTPGTS LPEPKATPEA VEPTRGPGEL DGHQQGRPTQ
LPGPWDRGSS VAQLHMASQT LSPRTFGGTS PTTPQGPPWG WTQPPVPASE GQGQPREDPG
HPGTGLPATS PVT
//
