ID A0A3B4YXV1_SERLL Unreviewed; 1162 AA.
AC A0A3B4YXV1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 3 {ECO:0000313|Ensembl:ENSSLDP00000033268.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000033268.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000033268.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4YXV1; -.
DR Ensembl; ENSSLDT00000034195.1; ENSSLDP00000033268.1; ENSSLDG00000025458.1.
DR GeneTree; ENSGT00940000156085; -.
DR Proteomes; UP000261360; 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:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 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 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 244..448
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 996..1039
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 102..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 386
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 390
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 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 446
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 321..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 364..443
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 403..429
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 470..495
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..504
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..523
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 517..528
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 551..588
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 555..593
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 566..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1162 AA; 130728 MW; 29931DDAACD7E9A1 CRC64;
CIFLGLWLNF PPNLTEMSRL KEYGLVTPFS TDSHGHYLSH LLSATHKQRV KREVFSSSEA
EQKLFFNITA FGKEFHLRLH PNNRLVAPGA MVEWHDEVQG FGNVSNSAGD DPSTDTNQTE
SSNGTERILR RELLKTDCTF IGDISDVPGA SVAINNCDGL AGMIRTDSDE YFIEPLERGT
QELEDQGRVH VVYRRSALLQ TPSDISVDYQ LQELDVPGTL DSVARQVNDT VRRRRRRDAG
EDDYNIEILL GVDDSVVRFH GKEHVQNYLL TLMNIVNEIY HDESLGVHIN VVLVRMIMLG
YAKSISLIER GNPSRSLENV CRWAFVQQKG DPDHAEHHDH AIFLTRQGFG PTGMQGYAPV
TGMCHPVRSC TLNHEDGFSS AFVVAHETGH VLGMEHDGQG NRCGDETTMG SVMAPLVQAA
FHRYHWSMCS GQELKRYIHT YDCLLDDPFK HDWPQLPELP GINYSMDEQC RFDFGVGYKI
CTSFRTFDPC KQLWCSHPDN PYFCKTKKGP PLDGTECAPG KWCYKGHCMW KNPNQVKQDG
TWGSWSKYGS CSRSCGTGVR FRTRQCNNPA PSNGGQDCPG VNYEYQLCNT DDCPKHFEDF
RAQQCQLRNS HFEFQNAKHH WLPYEHPDTN KRCHLYCQSR ETGDVAYMKQ LVHDGTRCSY
KDAYSICVRG ECVKVGCDRE IGSNKVEDKC GVCGGDNSHC RTVKGTFTRT PKKAGYLKMF
LIPPGARHVI IQEHEASPQI LAIKNQATGH YILNGKGEEV KSRSFIDLGV EWHYIIEEDV
ETLHTDGPLH DPVVVLIIPK DNETRSTLMY KYIIHEDSVP VNNNNVIQED TYEWALKSWS
PCSKPCAGGF QYTKYGCRKK GDTKMVHRGY CDTSKKPKPI RRMCNLQDCT QPQWVSEEWE
YCTKTCSSLG FQIRTVRCVQ LLHDSTNRSV HSKYCSGEKP ESRRPCNRVP CPAQWRTGAW
SECSVTCGEG MERRLVTCRI GDQCNGEKPE TVRPCRPGPC HDEPCNGDKS IFCQMEVLAR
YCSIPGYNKL CCESCSKRSG ALSLFTEAAE TEEHIRFGSA SQLLETLTAS VAANATRGAK
QGSGKASATS GNAARHITTP APLKKTQSKI TTAPRRVPRH MGLTGRKLPA MAPSPLADPT
EGQRSSSSTD SRRPTPYSKV ER
//
