ID G1NR24_MELGA Unreviewed; 1576 AA.
AC G1NR24;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 12 {ECO:0000313|Ensembl:ENSMGAP00000016354.3};
GN Name=ADAMTS12 {ECO:0000313|Ensembl:ENSMGAP00000016354.3};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000016354.3, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000016354.3, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000016354.3}
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 RefSeq; XP_019465894.1; XM_019610349.1.
DR MEROPS; M12.237; -.
DR Ensembl; ENSMGAT00000017328.3; ENSMGAP00000016354.3; ENSMGAG00000015413.3.
DR GeneID; 100541229; -.
DR CTD; 81792; -.
DR GeneTree; ENSGT00940000155855; -.
DR HOGENOM; CLU_000660_2_1_1; -.
DR InParanoid; G1NR24; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000001645; Chromosome Z.
DR Bgee; ENSMGAG00000015413; Expressed in gizzard and 15 other cell types or tissues.
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:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:2001113; P:negative regulation of cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:1902548; P:negative regulation of cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:1902203; P:negative regulation of hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR GO; GO:0030167; P:proteoglycan catabolic process; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; IEA:Ensembl.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
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; 7.
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:SF189; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 12; 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; 6.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 7.
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:UP000001645};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1576
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032411336"
FT DOMAIN 251..461
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1499..1539
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1049..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 213
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 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 397
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 401
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 407
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 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 327..381
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 356..363
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 375..456
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 414..440
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 483..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 525..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 1576 AA; 177317 MW; F7A547918AE1062B CRC64;
MPCVPPSRAA SGSFWLLVLH VPALCGTAGS LFPDGRQGQF IKTLQEYEVV DPARVDANGH
FVSFNLHHHI SNTRKKRDLG KKENAIYYKI NHKEKDLFFN LTIHMGFLSH NYVVERRRGN
YSRARIAMHS GVPCHFIGTV LQPGSGSGTA AISTCNGLTG YFHLPHGDYF IEPIKKHLQK
KGTPQPHIIY EANTLQNALR RKRAIPVEEE QACGVNDTLN FFKQEDHRRE KWEQNRVAVR
RVSRRSVSKE RWVETLVVAD SKMVEYHGSD HVESYILTIM NMVTGLFHDP SIGNAIHIVL
VRLILFEEEE QGLKIVHHAD KTLASFCKWQ KSVNPKSDIN PTHHDVAVLL TRKDICAGMN
RPCETLGLSH LSGMCQPHRS CNINEDSGLP LAFTIAHELG HSFGIQHDGK ENDCEPVGKR
PYIMSRQLQY DPTPLTWSQC SKEYITRFLD RGWGFCLDDI PQKEVLKSPI IAPGVIYDVH
HQCQLQYGSN ATFCEDVDNL CQTLWCSVKG SCRSKLDAAA DGTRCGENKW CFSGECITVG
KTPEAIHGGW GVWSSWSHCT RTCGAGVQSA ERPCDNPEPQ FGGDYCTGER KRYRVCNISP
CRKGLPTFRQ MQCTEFDTVP YQNEFYHWVP VYNTANPCEL HCRPIDRHFS EKMLDAVIDG
TPCFEGRHSR DICINGMCKA VGCDYEINSN ATEDQCGVCL GDGSACHTVK MTFNQSEGFG
YVDIGLIPKG ARGIRVTEVA EAGNFLAVRS KDPEKYYLNG GFIIQWNGEY KVAGTIFQYD
RTGDLENLTA PGPTNESIWI QLLFQETNPG IKYEYTVRKE ENHENEIGEP EYFWQYGEWT
ACTVTCGRGV RRQIAHCMRK GGGAIKNSFC DPATQPNGRQ KKCYEKDCPP RWWAGEWQKC
STTCGPTGQK KRTVLCIQTV GSDEQALAVT ECQHLLKPKT HLSCNRDVLC PSDWTVSNWT
ECTVTCGGGI RTRSVTCAKN NHEPCDSSKR PNSKALCGLQ QCPSARRFLI PPQVPRRGKI
IIRKTTNPNW SPPRRIPILV PSPRFHATTR IPKPETVTPS PTSSGLDKIP QKEETADVTL
QNKFAGSSDV YNYPVFSTEN SFHQNTTSWP FPNSLSTEII KHAEKVSKSE TVSTVGDELQ
NSEDTPVSSF TNSPEITSSY DYLTEESDDV DGSTEGSEKP TDFLYSTEHN LEIRTRSTML
DTNSPILQNG DVTSDLPPLS HPQEASMPLP DSRAAQGLTT ASAISLQVDV PMREITTQEV
TVVPTMFGNV WRGQADSRTE MKLPDNITSS TQLLVNKHAL KNHIETSERI LMNVTESSLL
ITSSSLPGDD YWIVGNWSEC STSCGMGTFW RHVECSSKNV SHCEHTKKPD HARKCYLRPC
ASWKTGNWSK CSAYCNGGFK TRDVQCIDIR EKQLLRPFHC QLLGYKPQLT TSCNMEPCLQ
WRVEPWNECT VSCGGGIQQR TVKCRNIETD ETEDDSMCVD KPKPTEHQQC NQQACRKNAG
LPCSKDQLSI HFCQRLRDIG KCLVPSIQLQ CCSTCSHPRI RNKARYWDQR GLKQHYTKSR
RKSPENQENN SQDAQH
//
