ID A0A2Y9L7B8_ENHLU Unreviewed; 1103 AA.
AC A0A2Y9L7B8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10 isoform X4 {ECO:0000313|RefSeq:XP_022381218.1, ECO:0000313|RefSeq:XP_022381219.1};
GN Name=LOC111161692 {ECO:0000313|RefSeq:XP_022381218.1,
GN ECO:0000313|RefSeq:XP_022381219.1, ECO:0000313|RefSeq:XP_022381220.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022381218.1};
RN [1] {ECO:0000313|RefSeq:XP_022381218.1, ECO:0000313|RefSeq:XP_022381219.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022381218.1,
RC ECO:0000313|RefSeq:XP_022381219.1};
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_022381218.1; XM_022525510.1.
DR RefSeq; XP_022381219.1; XM_022525511.1.
DR RefSeq; XP_022381220.1; XM_022525512.1.
DR Proteomes; UP000248482; 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; 5.
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:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
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:UP000248482};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1103
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041069332"
FT DOMAIN 239..457
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1065..1103
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 213..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 392
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 396
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 402
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 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 315..376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 351..358
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 370..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 409..436
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 479..501
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..508
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 496..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..536
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 559..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..601
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 574..586
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1103 AA; 120942 MW; 093E5959CCCF6AE3 CRC64;
MAPAYQILRW ALTLGLGLTF EVIHAFQSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPA
PRRQRRGTGP APESRLYYKV AAPSTHFLLN LTRSPRLLAG HVSVEYWTRE GLAWQRAARP
HCLYAGHLQG QAGSSHVAIS TCGGLHGLIV ADEEEYLIEP LQVGPKGTQG PEDSGPHVVY
KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY
VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GNIVNILVTR LILLTEDQPT
LEITHHAGKS LDSFCKWQKS IVNRSGHGNA IPENGVANHD TAVLITRYDI CIYRNKPCGT
LGLAPVGGMC ERERSCSINE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM
AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR
FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG
SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD
CPPGSQDFRE MQCSEFDSIP FRGKFYTWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD
GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPASPAAG
YEEVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ
GPDQTQSLEA LGPINASLII MVLARTELAA LRYRFNAPIA RDALPPYSWH YAPWTKCSAQ
CAGGSQVQAV ECRNQLDSSA VAPHHCSAHS KLPKRQRACN TEPCPPDWVV GNWSRCSRSC
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACQ GPACPPEWAA LDWSECTPSC
GPGLRHRVVL CKSSDHRATL PPAHCPPAAK PPATMRCNLR RCPPARWVTG EWGECSAQCG
IGQQQRAVRC SSHTGQPSRE CAEALRPPST QQCEAKCDSA PPGDGPEECK DVNKVAYCPL
VLKFQFCSRA YFRQMCCKTC HGR
//
