ID G1P7C3_MYOLU Unreviewed; 1847 AA.
AC G1P7C3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 20 {ECO:0000313|Ensembl:ENSMLUP00000006016.2};
GN Name=ADAMTS20 {ECO:0000313|Ensembl:ENSMLUP00000006016.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006016.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006016.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006016.2}
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; AAPE02013366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 59463.ENSMLUP00000006016; -.
DR Ensembl; ENSMLUT00000006590.2; ENSMLUP00000006016.2; ENSMLUG00000006566.2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158636; -.
DR HOGENOM; CLU_000660_0_1_1; -.
DR InParanoid; G1P7C3; -.
DR OMA; WPSDLCL; -.
DR TreeFam; TF331949; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 11.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 13.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 13.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 13.
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:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 190..399
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1647..1847
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT ACT_SITE 335
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 132
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 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 334
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 338
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 344
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 394
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="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 265..318
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 294..300
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 312..394
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 350..378
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 421..443
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 432..453
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 438..472
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 466..477
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..537
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 504..542
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 515..527
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1847 AA; 207056 MW; F11AB9C080F6D1D6 CRC64;
PEPPPFRTHY RISAYGQLFQ LNLSADAAFL AEGFTEVHLG APARGAEESR AVSPGLRHCF
YRGQVNARED HIAVFSLCGG LMGTFKAHDG EYFLEPIMKA DGSEHEDDHN KPHLIYRQEL
KRNYFLHPHK PCDVSESQIK KTTLPFHNYS NMNEDLNTEV VLGHPSKNVS LENEKSQSHS
RKKRFLSYPR YVEVMVTADA KMVHHHGPNL QHYVLTLISI VAAIYKDSSI GNLINIVIVK
LIVIHNEQEG PVISFNAATT LRNFCLWQQT QNVLDDAHPS HHDTAVLITR EDICGAREKC
DTLGLAELGT LCDPLRSCSI SEENGLSAAF TIAHELGHVF NVPHDDSFKC KESGIKHQYH
VMAPTLNYHT SPWTWSKCSQ KYITEFLDTG HGDCLLDKPN GRIYDLSSQL PGLMYDVNKQ
CELMFGPGSQ VCPYLKQCRR LWCTSAEGVH KGCRTQHMPL ADGTNCGPGM HCHHGLCVNK
EMETRPVDGE WGPWGPYSSC SRTCGGGIKS TTRLCNRPEP RNGGKYCVGR RMKFRSCNTD
SCPKGKQDFR EKQCSDFDGK HFNINGLSPN VRWLPKYSGI AIKDRCKLYC RVAGTTNFYQ
LKDRVADGTP CGTETNDICV QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCRTMSGVFN
SAHYGYNVVV KIPAGATNID ILQHSYSGTP ADDNYLALSD TQGNFLLNGN FVVSMAKKEI
HVQGAIFEYS GSNSSTERIN STDRLEEELV LQVLCVGNLY NPDVRYSFNI PVEEKRDQFT
WDPYGPWQDC TRMCQDIGQG LHRRKITCIR KSDLMVVPDQ RCDHLPLPLF VTERCNTDCE
LRWHIIGKSE CSSHCGQGYR SLDVHCMKYS VHKGQTVPVD DHYCSDQLKP PTREPCHGDC
VLTRWHYSEW SQCSRSCGGG ERSRESYCIN HFGHRLADRE CQELPHVMTE NCNEFPCPSW
ATSEWSECPV TCGKGTKRRQ VWCELNEDHL SDGFCNPSTK PESLRPCELH TCASWQVGPW
GSCTATCGHG YQMRAVKCVD ELLSAVLDDR LCYGASRPSD RQDCIMIPCP VIPKTGTTSL
PAVPMGKTAQ WRYGSWTPCS ASCGRGNQAR YVSCRDAHDG IADESYCAHL PRPAEISICF
SPCGEWQTGD WSPCSASCGH GKTNRQVLCI KYHQPINENH CDPEVRPSAE QECNVAACQP
LYSNFPSSSE QPNHFPGRNF PLTHKPEDNE KWGVHPSVRG NQWRTGPWGS CSSSCAGGVQ
RRVVVCQDEN GQSAHYCDVA AKPPEAKHCD TGPCPQWNFG SWGECTQTCG GGIKSRFVIC
QFPNGQMSQE QNCEILNKPP SVAQCHVHAC PDDVSWHRGP WNSCSASCGK GLKYREVLCV
DQVQGKLEEK YCSHLRKPRT HKACRSGRCP SWKAKRWKEC SVTCGPGVEQ RDVYCRLRGV
GPVAEEMCDR STRPHSQRQC WRQDCIQSQW VAGEWSDCLT SCKIKETHRQ VQCIDAQNIQ
VNESFCDPST RPLSIKKCKN LPCKYIVVTG DSSQCAGNCG FSYRQRITYC IEIQSTDRYK
LHQLWPIDYR ECPVLPSPQT YKCNLRSCLH MATWKVGKWS KCSVTCGVGV MERRVECMAE
NGWSSDLCLK RLKPDAQKKC YVNDCKTFTS CKEIQGENNI TKDGDYYLNI EGRIIKVYCA
DMHLEDPKEY ISLVKGEEDN FSEVYGFRLQ NPYECPFNGS RRLDCECTND YLAAGHTVFS
KIRIDLTSMQ IKTTDLLFAQ TVFGKAVPFA TAGDCYSAAR CPQGRFSINL AGTGMKISST
AKWLAQGSYA SVVIHRSQDG TKVYGRCGGF CGKCVPHLMT GLPIQVI
//
