ID G1PFL2_MYOLU Unreviewed; 1207 AA.
AC G1PFL2;
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 14 {ECO:0000313|Ensembl:ENSMLUP00000009375.2};
GN Name=ADAMTS14 {ECO:0000313|Ensembl:ENSMLUP00000009375.2};
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:ENSMLUP00000009375.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009375.2, 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:ENSMLUP00000009375.2}
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; AAPE02039708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02039709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02039710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02039711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PFL2; -.
DR STRING; 59463.ENSMLUP00000009375; -.
DR Ensembl; ENSMLUT00000010290.2; ENSMLUP00000009375.2; ENSMLUG00000010277.2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158426; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; G1PFL2; -.
DR OMA; HRFHWSH; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000001074; 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:0030199; P:collagen fibril organization; IEA:Ensembl.
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:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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 Reference proteome {ECO:0000313|Proteomes:UP000001074};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1207
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003417004"
FT DOMAIN 247..448
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1041..1079
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Pro 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 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
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 324..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 552..589
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 556..594
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 567..579
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1207 AA; 132131 MW; 67A1B05C523521AE CRC64;
MVWLKGAPPR AGFPNMIALH CWLLGAAGRP TPAGLPLSGR LSDYGVTVPR STDFRGRFLS
HVVSGPAAAS TSGHLRVARS PQRPRGAAPQ PDRLYFNVTV FGEELHLRLR PNRRLVVPGA
SAEWQEDFRE LFRQPLQQEC VYTGSVTGMP GAAVAISNCD GLAGLIRTDV TDYFIEPLER
GQQEKEAGGR THVVYRREAV QQAWAEPGGD LHNEAFGLGD LPNLLGLVGG QLGEAERKRR
HAKPGSYSIE VLLAVDDSVV RFHGKEHVQN YVLTLMNIVN EIYHDESLGT HINIALVRLI
MVGYRQSLSL IERGNPSRSL EQVCRWAHSQ QRQDPGHAEH HDHVIFLTRQ DFGPSGYAPV
TGMCHPLRSC ALNHEDGFSS AFVVAHETGH VLGMEHDGQG NGCADETSLG SVMAPLVQAA
FHRFHWSRCS KLELSRYLPS YDCLLDDPFA PAWPQPPELP GTDYSMDEQC RFDFGTGYHT
CSAFTTFEPC KQLWCSHPDN PYFCKTKKGP PLDGTECAPG KWCFKGHCIW KSPEQTYGQD
GGWSSWSNFG SCSRSCGGGV RSRSRNCDNP FPAYGGRLCS GPMFQYQVCN SEECPGPYED
FRAQQCAKRN SYYLHQNAKH SWIPHEPDDD TQKCELICRS EDTGDVVFMN QVVHDGTRCS
YRDPYSVCAR GECVPVGCDK EVGSMKADDK CGVCGGDNSH CRTVKGTLGK ASKQPGALKL
VQIPAGARHI QIEKLEKAPH HIAVKNQVTG SFILNPKGKE ATSRTFTAMG LEWEYAVEDA
KENLKTSGPL PEAIAVLVLP PAKGGPRGSL AYKYVIHEDL LPLIGSNNVL LEETDTYEWA
LKSWAPCTKA CGGGIQFTKY GCRRRRDHHM VQRHLCDHKK RPKPIRRRCN QHQCPQPEWV
MEEWSTCSRS CGKLGVQTRA VQCLLPLSNG THKAMPAKAC PGDRPEARRP CLRVPCPAQW
RTGAWSQCSA TCGEGIQQRQ VVCRTNANSL GQCEGDKPDT IQACSLPACR GNLQNSTVRA
DVQALVTPQS GSLHPINKIT STEPCMGDRS ILCQMEVHER YCSIPGYHRL CCESCTKKAS
GPAASLDPGL TSPPPFSTPG SPSPGAKTPP EAVEPTVGPT GSDNHPHGRP TQLPGPLGTS
PPVTQRLGFA PQKLSPGALR STSPDATRGQ PWGWTPGPPL PASEDKGQLR EDLEHPGTGL
PDTSPVT
//
