ID A0A452C750_BALAS Unreviewed; 910 AA.
AC A0A452C750;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 14 {ECO:0000313|RefSeq:XP_028018771.1};
GN Name=ADAMTS14 {ECO:0000313|RefSeq:XP_028018771.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028018771.1};
RN [1] {ECO:0000313|RefSeq:XP_028018771.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028018771.1};
RG RefSeq;
RL Submitted (JAN-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 -!- 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_028018771.1; XM_028162970.1.
DR AlphaFoldDB; A0A452C750; -.
DR STRING; 310752.A0A452C750; -.
DR InParanoid; A0A452C750; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261681; 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; 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; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 57..258
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 197
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 196
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 200
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 206
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 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 256
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 134..180
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 174..253
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 213..239
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 280..305
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 291..314
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 300..333
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 327..338
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 362..399
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..404
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..389
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 910 AA; 101298 MW; A453BCB5088B617E CRC64;
MHVVYRREVV QQAWTEPLGD LHNEAFGLGD LPNLLGLVGD RLGEAERKRR HAKPGSYSME
VLLAVDDSVV RFHGKEHVQN YVLTLMNIVD EIYHDESLGV HINIALVRLI MVGYRQSLSL
IERGNPSRSL EQVCRWAHSQ QRQDPGHAEH HDHVVFLTRQ DFGPSGYAPV TGMCHPLRSC
ALNHEDGFSS AFVVAHETGH VLGMEHDGQG NGCADETSLG SVMAPLVQAA FHRFHWSHCS
KLELSRYLPS YDCLLDDPFA PAWPRPPELP GIDYSMDEQC RFDFGTGYHT CSAFRTFEAC
KQLWCSHPDN PYFCKTKKGP PLDGTECAPG KWCFKGHCIW KSPEQTYGQD GGWSSWTKFG
SCSRSCGGGV RSRSRSCDNP PPAYGGRLCS GPTFQYQVCN GEECPGPYED FRAQQCAKRN
SYYVHQNAKH SWIPYEPDDD AQKCELICQS EDTGDVVFMN QVVHDGTRCS YRDPYSVCAR
GECVPVGCDK EVGSMKADDK CGVCGGDNSH CRTVKGTLGK ASKQAGALKL VQIPAGARHI
QVEELEKVPH HIAVKNQVTG SFILNPKGKE ATSRTFTAMG LEWEYVVEDA KESLKTSGPL
PEAIAILVLP PAEGGPRSSL AYKYVIHEDL LPLIGSNNVL LEETDTYEWA LKNWAPCTKT
CGGGIQFTKY GCRRRRDHHL VQRHLCDHRK RPKPIRRRCN QHPCAQPAWV TEEWSACSRS
CGKLGVQTRG VQCLLPLSNG THKAMPAKAC PGDRPEARRP CHRVPCPAQW RTGAWSQCSV
TCGEGVQLRQ VVCRANASSL GQCEGDKPDT VQVCSLPACG GNLQNSTVRA DVRELVTAEG
EWMPQSGPLD PINKISSTEP CVEDRSIFCQ MEVLDRYCSI PGYHRLCFWG CDTFQPMKWV
YEEEKDQGKP
//
