ID G1RKF9_NOMLE Unreviewed; 1224 AA.
AC G1RKF9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 16 {ECO:0000313|Ensembl:ENSNLEP00000013716.1};
GN Name=ADAMTS16 {ECO:0000313|Ensembl:ENSNLEP00000013716.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000013716.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000013716.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000013716.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; ADFV01014565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01014566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01014567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01014568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01014569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003263262.1; XM_003263214.1.
DR AlphaFoldDB; G1RKF9; -.
DR STRING; 61853.ENSNLEP00000013716; -.
DR MEROPS; M12.026; -.
DR Ensembl; ENSNLET00000014394.2; ENSNLEP00000013716.1; ENSNLEG00000011241.3.
DR GeneID; 100604876; -.
DR KEGG; nle:100604876; -.
DR CTD; 170690; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159433; -.
DR HOGENOM; CLU_000660_1_0_1; -.
DR InParanoid; G1RKF9; -.
DR OMA; LRCAEKY; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000001073; Chromosome 6.
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:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
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:SF140; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 16; 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; 6.
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:UP000001073};
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};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1224
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003421461"
FT DOMAIN 290..495
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1186..1223
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 434
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 433
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 437
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="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 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 366..417
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 392..399
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 411..490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 450..474
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 518..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..550
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..569
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..574
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 598..635
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 602..640
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 613..625
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1224 AA; 136140 MW; 53E32E14819A1F3E CRC64;
MKPRARGWQG WAALWMLLAQ VAEQALARAM GPAAAAPGSP SVPRPPPPAE RPGWMENGEY
DLVSAYEVDH RGDYVSHEIM HHQRRRRAVA VSGVESLHLR LKGSRHDFHM ELRTSSRLVA
PGFIVQTLGK TGTKSVQTLP PENFCFYQGS LRSHRNSSVA LSTCQGLSGM IRTEEADYFL
KPLPSHLSWK LGRAAQGSSP SHVLYKRSTE PHAPGASEVL VTSRTWELAH QPLHSSDLHL
GLPQKQHFCG RRKKYMPQPP KEDLFILPDE YKSCLRHKRS LLRSHRNEEL NVETLVVVDK
KMMQNHGHEN ITTYVLTILN MVSALFKDGT IGGNINIAIV GLILLEDEQP GLVISHHADH
TLSSFCQWQS GLMGKDGTRH DHAILLTGLD ICSWKNEPCD TLGFAPISGM CSKYRSCTIN
EDTGLGLAFT IAHESGHNFG MIHDGEGNMC KKSEGNIMSP TLAGRNGVFS WSPCSRQYLH
KFLSTAQAIC LADQPKPVKE YKYPEKLPGE LYDANTQCKW QFGEKAKLCM LDFKKDICKA
LWCHRIGRKC ETKFMPAAEG TICGHDMWCR GGQCVKYGDE GPKPTHGHWS DWSSWSPCSR
TCGGGVSHRS RLCTNPKPSH GGKFCEGSTR TLKLCNSQNC PRDSVDFRAA QCAEHNSRRF
RGRHYKWKPY TQVEDQDLCK LYCIAEGFDF FFSLSNKVKD GTPCSEDSRN VCIDGICERV
GCDNVLGSDA VEDVCGVCNG NNSACTIHRG LYTKHHHTNQ YYHMVTIPSG ARSIHIYEMN
VSTSYISVRN ALRRYYLNGH WTVDWPGRYK FSGTTFDYRR SYNEPENLIA AGPTNETLIV
ELLFQGRNPG VAWEYSMPHL GTEKQPPAQP SYTWAIVRSE CSVSCGGGQI TVREGCYRDL
KFQVNTSFCN PKTRPVTGLV PCKVSACPPS WSVGNWSACS RTCGGGAQSR PVQCTRRVHY
DSEPVPASLC PQPAPSSRQA CNSQSCPPAW STGPWAECSH TCGKGWRKRA VACKSTNPSA
RAQLLPDAVC TSEPKPRMHE ACLLQRCHKP KKLQWLVSAW SQCSVTCERG TQKRFLKCAE
KYVSGKYREL ASKKCSHLPK PSLELERACV PLPCPKHPPF AAAGPSRGSW FASPWSQCTA
SCGGGVQTRS VQCLAGGRPA SGCLLHQKPS ASLACNTHFC PIAEKKDAFC KDYFHWCYLV
PQHGMCSHKF YGKQCCKTCS KSNL
//
