ID A0A1S3F9I3_DIPOR Unreviewed; 1148 AA.
AC A0A1S3F9I3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|RefSeq:XP_012872517.1};
GN Name=Adamts14 {ECO:0000313|RefSeq:XP_012872517.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012872517.1};
RN [1] {ECO:0000313|RefSeq:XP_012872517.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012872517.1};
RG RefSeq;
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 RefSeq; XP_012872517.1; XM_013017063.1.
DR AlphaFoldDB; A0A1S3F9I3; -.
DR STRING; 10020.ENSDORP00000020338; -.
DR GeneID; 105986250; -.
DR KEGG; dord:105986250; -.
DR CTD; 140766; -.
DR InParanoid; A0A1S3F9I3; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 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:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 220..421
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 978..1021
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 22..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 360
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 359
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 363
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 369
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 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 297..343
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 337..416
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 376..402
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 443..468
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 454..477
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 463..496
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..501
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 525..562
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..567
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 540..552
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1148 AA; 126466 MW; 7ED8686AB935E296 CRC64;
MTVPCSTDFR GHFLSHVVSG PSAASTRSVG VDRPPLPSSH SSHRVARSPL RPEGGPRHPG
RAGHHFLYFN VTVFGKELHL RLQPKRRLVV PGASVEWQED FQEVFRQPLR QECVYTGGVT
GMPGAAVALS NCDGLAGLIR TDSTDYFIEP LQRGQQEKEA SGRTHVVYRR EAVRREWAEP
HGDLHNEAFG LGDLPNLLGL VGEQLGDTER KRRHAQPGSY SIEVLLAVDD SVVRFHGREH
VQNYVLTLMN IVDEIYHDES LGAHVNIALV RLIMVGYRQS LSLIERGNPA RSLEQVCRWA
HSQQRQDPSH TEHHDHVVFL TRQNFGPSGY APVTGMCHPL RSCALNHEDG FSSAFVVAHE
TGHVLGMEHD GQGNGCADET SLGSVMAPLV QAAFHRFHWS RCSKLELSRY LPSYDCLLDD
PFERTWPLPP ELPGINYSMD EQCRFDFGTG YHTCLAFRTS EPCKQLWCSH PDNPYFCKTK
KGPPLDGTEC SPGKWCFKGH CIWKSPEQTY GQNGGWSSWT KFGSCSRSCG GGVRSRSRSC
DNPPPAYGGR QCSGPTFEYQ ICNSEECPGP YEDFRAQQCA KRNSYYIHQN AKHSWIPYEP
EDDAQKCELI CQSADTGDVV FMNQVVHDGT RCSYRDPYSI CARGECVPVG CDKEVGSMKA
DDKCGVCGGD NAHCRTVKGT LGKASKQAAA TKLVQIPAGA RHIQIDMLEK APHRIAVKNQ
VTGSFILNPK GKEASSRTFT ALGLEWEHVV EDAKDSLKTS GPLPEAIAVL VLPPAEGGPR
GSLAYKYVIH EDLLPLIGSN NVLLEETDTY EWALKSWAPC TKTCGGGIQF TKYGCRRRRD
HHMVQRHLCD HKKRPKPIRR RCNQHPCAQP AWVMEEWGAC SRSCGKLGVQ TRGVQCLLPI
SNGTHKAMPA KACPGDRPEA RRPCLRVPCP AQWRTGAWSQ CSATCGEGIQ QRQVVCRTNA
NSLGQCDGNK PDTVQVCSLP ACAVEPCVGD RSIFCQMEVL DRYCTIPGYY RLCCESCTKK
SSGLNSSLDP SLASLPPFST PGSPLLEPSA TFKATEPTRR PSGSTDQQQG QPTQLPEPLD
TSTSVTQHHL GPGTSSSRSL RDPSSATPQG PPLGWTQAAV PASKDQGQPW EEDPRHWGTS
LPATSPVT
//
