ID A0A3Q0HGL0_ALLSI Unreviewed; 621 AA.
AC A0A3Q0HGL0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 15 isoform X2 {ECO:0000313|RefSeq:XP_025070787.1};
GN Name=ADAMTS15 {ECO:0000313|RefSeq:XP_025070787.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025070787.1};
RN [1] {ECO:0000313|RefSeq:XP_025070787.1}
RP IDENTIFICATION.
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 -!- 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_025070787.1; XM_025215002.1.
DR AlphaFoldDB; A0A3Q0HGL0; -.
DR Proteomes; UP000189705; 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 Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
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:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 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; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:UP000189705};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 1..96
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 31
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 30
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 34
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 40
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 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 8..91
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 46..75
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 117..139
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 128..149
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 134..168
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 162..173
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 197..234
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 201..239
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 212..224
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 621 AA; 68098 MW; D2A91AD0E3AE4D9F CRC64;
MADVGTMCDP KRSCSVIEDD GLPSAFTTAH ELGHVFNMPH DNVKVCEETF GRLKTNHMMS
PTLIQIDRAN PWSACSAAII TDFLDSGHGD CLLDQPTKPI PLPEDLPGAS YTLNQQCELA
FGIGSKPCPY MQYCTKLWCT GKARGQIVCQ TRHFPWADGT SCGEGRFCMK GACVERHNIS
KYRVDGNWGK WAPYGQCSRT CGGGVQLAKR ECNNPVPANG GKYCEGIRVK YRSCNLDPCS
DSVPGKSFRE EQCEAFNGYS HSTNRLTASV SWVPKYSGVS PRDKCKLICR ANGTGYFYVL
APKVVDGTPC APDSTSVCVQ GKCIKAGCDG KLGSKKKFDK CSVCGGDNKS CKKVSGLFTK
PMHGYNFVVV IPAGASSIDI RQRGYKGLIN DDNYLAVKNG QGKYLLNGHF IVSAVERDLM
VKGSVLRYSG TGTAVESLQS FKPIQEPLTV EVLSVGKMTP PRVRYSFYLP KERKDDKSSY
KSDGKSLPDL TNSVLSLSNR LDMGRPSYKR PSYKWAAGGW EACSVTCGNG LQKRAVDCRD
SYGHLASECD ATQRPVDVRI CGDPCPTWEA GPWSPCSKTC GRGFKRRMLK CTAQAGQLLP
RDRCNLRKKP QELDFCTLRP C
//
