ID A0A151NLY7_ALLMI Unreviewed; 1184 AA.
AC A0A151NLY7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 6 isoform B {ECO:0000313|EMBL:KYO37842.1};
GN Name=ADAMTS6 {ECO:0000313|EMBL:KYO37842.1};
GN ORFNames=Y1Q_0010291 {ECO:0000313|EMBL:KYO37842.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO37842.1};
RN [1] {ECO:0000313|EMBL:KYO37842.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO37842.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO37842.1}.
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DR EMBL; AKHW03002566; KYO37842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NLY7; -.
DR STRING; 8496.A0A151NLY7; -.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 6.
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:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 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; 5.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
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 Integrin {ECO:0000313|EMBL:KYO37842.1};
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:UP000050525};
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 253..458
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1147..1184
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
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 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 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 400
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 406
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 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 DISULFID 329..380
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 355..362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..453
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 413..437
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..513
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..532
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 526..537
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 561..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..603
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..588
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1184 AA; 132583 MW; 1D12BEA3F685AD7B CRC64;
MRAALLAPLG LGRALKADYI FVTPVKVDSS GSYISHDVLH STRKKRSTQS SKSSLHYRFS
AFGQELHLEL KPSTILSNSF IVQVLGKDGV TDSQEREVDQ CFYQGFIRND STSSVAISTC
VGLSGLIRTR ENEFLISPLP QHLAQEHNYT APAGHHPHVL YKRTAEEKVH RYKVSSSPNH
FSPGHHRNHT YSKYHGQAND YHLGRFQKQH FCGRRKKYAP KPPTADRYIF SDEYGSFARF
KRSSVKIQKS GSLSVETLVV ADKKMLEKHG KENVTTYILT VMNMVSSLFK DGTIGSDINI
IVVSLLLLEQ EPGGLMINHH ADQSLNSFCQ WQSALVGKNG RRHDHAILLT GFDICSWKNE
PCDTLGFAPI SGMCSKYRSC TINEDTGLGL AFTIAHESGH NFGMIHDGEG NPCRKAEGNI
MSPTLTGNNG VFSWSVCSRQ YLNKFLSTAQ AACLIDEPKQ TGQYKYPDKL PGQIYDADTQ
CKWQFGTKAK LCNLSFVKDI CKSLWCHKVG HRCETKFMPA AEGTACGISM WCRRGQCVKY
GDHGPKPING QWSAWSEWSE CSRTCGGGVT YRERHCNNPK PQYGGKFCQG SSRIYQLCNI
QLCPPNRLGF RAQQCAEYNS KPFRGWYYKW KPYTKVEEED RCKLYCTAED FDFFFAMSSK
VKDGTPCFPN AYDVCIDGVC EQVGCDHGLG SKAVLDACGV CKGDNSTCKF FKGQYLIQHK
ANDYYPVVTV PAGARSIEIQ EMQISTSYLA VRNLNKKYYL TGDWTIDWPG KFSFAGTTFD
YQRSFNHPES LYAAGPTNET LVFEILLQGT NPGISWEYTF PKAISENKTS AKKHSYSWVT
IQSECSTACG GGHFTAKALC LQDHHMRVNS SFCDPRTKPV TETKLCNTNP CPAYWSTGEW
STCSKSCGGG QQSRLIQCVQ KKSFQKEEVV AHSLCPVSTP AQVQMCNNRD CPPEWSTGPW
SQCSKTCGRG IKKRDVYCKG NSSFKVKILP ESLCSREPKP EPQQTCVLGR CPKNDRLQWM
ISSWSECSTS CGPGVRKREM KCIEKSIHGK LITFPQRRCR NIKKPSIELE ETCSNGACPL
ITLYGMVSGW YSSPWQQCTV TCGGGVQTRT VQCLRQGRPA SGCLPHQKPA ISRACNTNFC
PAPEKKDDPS CVDFFTWCHL VPQHGVCNHK FYGKQCCKSC TKKI
//
