ID E1BFV4_BOVIN Unreviewed; 1216 AA.
AC E1BFV4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 14 {ECO:0000313|Ensembl:ENSBTAP00000028224.5};
GN Name=ADAMTS14 {ECO:0000313|Ensembl:ENSBTAP00000028224.5,
GN ECO:0000313|VGNC:VGNC:25618};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000028224.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000028224.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028224.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000028224.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000028224.5};
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 RefSeq; NP_001179176.1; NM_001192247.1.
DR AlphaFoldDB; E1BFV4; -.
DR SMR; E1BFV4; -.
DR STRING; 9913.ENSBTAP00000028224; -.
DR MEROPS; M12.024; -.
DR PaxDb; 9913-ENSBTAP00000028224; -.
DR Ensembl; ENSBTAT00000028224.6; ENSBTAP00000028224.5; ENSBTAG00000021177.6.
DR GeneID; 510214; -.
DR KEGG; bta:510214; -.
DR CTD; 140766; -.
DR VEuPathDB; HostDB:ENSBTAG00000021177; -.
DR VGNC; VGNC:25618; ADAMTS14.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158426; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; E1BFV4; -.
DR OMA; HRFHWSH; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.14; 908.
DR Reactome; R-BTA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-BTA-5173214; O-glycosylation of TSR domain-containing proteins.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000021177; Expressed in liver and 60 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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 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:UP000009136};
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..1216
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003144023"
FT DOMAIN 260..461
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1060..1098
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 63..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 399
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 403
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 409
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 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 337..383
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..456
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 416..442
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 483..508
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..517
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 503..536
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 530..541
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..602
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 569..607
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 580..592
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1216 AA; 133170 MW; 7119C902DFA4702A CRC64;
MAPVCARLSC LLLLHCALCA AAGSGTEELH FSRKLSDYGV TVPCSTDSQG RFLSHVVSGP
AAASAGSVKG DGPPSPLSHS GRLRVARSPL RPEGVTLQPG RMGRSSLYFN VTVFGEELHL
HLRPNRRLVV PGASVEWQED FQELFRQPLQ RECVYTGGVT GMPGAAVAIS NCDGLAGLIR
TDSTDYFIEP FERGQQEAEA GGRKHVVYRR EVVRQRWTEP LGDLHNEAFG LGDLPNLLGL
VGDRLGEAER KRRHATPGSY SIEVLLAVDD SVVRFHGKEH VQNYVLTLMN IVDEIYHDES
LGVHINIALV RLIMVGYRQS LSLIERGNPS RSLEQVCRWA HSQQRQDPGH AEHHDHVVFL
TRQDFGPSGY APVTGMCHPL RSCALNHEDG FSSAFVVAHE TGHVLGMEHD GQANGCADET
SLGSVMAPLV QAAFHRFHWS RCSKLELSRY LPSYDCLLDD PFAPAWPQPP ELPGIDYSMD
EQCRFDFGTG YHTCSAFRTF EACRQLWCSH PDNPYFCKTK KGPPLDGTEC APGKWCFKGH
CIWKSPEQTY GQDGGWSSWT KFGSCSRSCG GGVRSRSRSC DNPPPAYGGR MCSGPMFQYQ
ICNSEECPGP YEDFRAQQCA KRSSYYIHQN AKHSWIPYEP DDDAQKCELI CQSEDTGDVV
FMNQVVHDGT RCSYRDLYSV CARGECVPVG CDKEVGSMKA DDKCGVCGGD NSHCRTVKGT
LGKASKQAGA LKLVQIPAGA RHIQIEELEK VPHHIAVKNQ VTGSFILNPK GKEATSRTFT
AMGLEWEYVV EDAKESLKTS GPLPEAVTVL VLPPAESGPR SSLAYKYIIH EDLLPLIGSN
NVLLEETDTY EWALKSWAPC TKACGGGIQF TKYGCRRRRD HHMVQRHLCD HRKRPKPIRR
RCNQHACAQP GWVTEEWGTC SRSCGKLGVQ TRGVQCLLPL TNGTHKAMPA KACPGERPEA
RRPCLRVPCP LQWRTGAWSQ CSVTCGEGIQ QRQVVCRTNA NSLGQCEGAK PDMVQACSLP
ACGGNLQNST VKADVRELVT PEGQWVPQSG PLDPINKISS TELCVRDRSI FCQTEELDRY
CSIPGFHRLC CESCTKKTLS LDPGLASPPP FSTPGSPFSA PVAPPDAVEP SAGPTGSDQR
QRDQPTPLPG PLGTSAPVTQ SYFAPQKPTP TAFRGTSPSA PWGWTGAPTP ASENKGLLRE
DPKHSGTSLP STAPVT
//
