GenomeNet

Database: UniProt
Entry: A0A452GLE5_9SAUR
LinkDB: A0A452GLE5_9SAUR
Original site: A0A452GLE5_9SAUR 
ID   A0A452GLE5_9SAUR        Unreviewed;       934 AA.
AC   A0A452GLE5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000002438.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000002438.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A452GLE5; -.
DR   STRING; 38772.ENSGAGP00000002438; -.
DR   Ensembl; ENSGAGT00000002794.1; ENSGAGP00000002438.1; ENSGAGG00000001976.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
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; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR   InterPro; IPR006586; ADAM_Cys-rich.
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; IPR013274; Pept_M12B_ADAM-TS1.
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:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 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; 2.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01858; ADAMTS1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR01705; TSP1REPEAT.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00209; TSP1; 3.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50092; TSP1; 3.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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, ECO:0000256|PIRSR:PIRSR613274-
KW   4}; 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:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..934
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019301253"
FT   DOMAIN          211..420
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   REGION          167..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         175
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         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         304
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         354
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         358
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         364
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         415
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         418
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         418
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT   CARBOHYD        673
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT   DISULFID        286..338
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        315..320
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        332..415
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        370..399
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        441..464
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        452..474
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        459..493
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        487..498
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        524..561
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        528..566
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        539..551
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   934 AA;  102006 MW;  206AD33BE6DD8512 CRC64;
     MGTAPALASL LLAALLCLCP RGARCSPGPR EEQELIVPVR LDSAAEPAAK RLYRLDAFGK
     RLSLELEPDS SFLAPDFRLQ YLGSRPREEE EAVAEQGASL GNQPAADLAR CFYSGTVNRD
     PSSAAALSLC AGLRGAFYLQ GEEYFIQPAN ASQQQLHLLR RRLQSRGHQS GGSKCGVTDQ
     SSPLAAEGQQ AHVGQTETGS TRKKRFVSSP RYVETMLVAD QSMAEFHGSG LKHYLLTLLS
     VAAKLYKHPS IRNSISLVLV KILVIYDEQK GPDVSSNAAL TLRNFCSWQK QHNPPSDRHA
     EHYDTTILFT RQDLCGAKTC DTLGMADVGT ICDPNRSCSI IEDDGLQAAF TTAHELGHVF
     NMPHDDAKQC ANINGLSRDS HMMASMLSNL DRSQPWSPCS AYMITTFLDN GHGECLLDKP
     HKPIQLPSDL PGTLYDANRQ CQFTFGDESK HCPDAASTCT TLWCTGISGG LLVCQTKHFP
     WADGTNCGEG KWCVNGKCVN KTEKKHYDTP VHGGWGSWGP WGDCSRTCGG GVQYSFRECD
     NPIPKNGGKY CEGKRVQYRS CNIENCPDNN GKTFREEQCE THNDISKSPF GSGPAVEWTP
     KFAGVSPKDR CKLVCRAKGT GYFFVLQPKV VDGTSCSPDS TSVCVQGQCV KAGCDRMIGS
     SKKFDKCGIC GGNGSTCKKV SGTLISAKPG YHDVVTIPAG ATNLEVKQRN NRGSRHDGSF
     LAIKAADGTY ILNGDYTLST LEQDITYKGS VLRYSGSSAA LERIRSFSPL TEPLTIQVLT
     VGDSPQPKIK YTYFVKKPLQ SGSEKASSKK KESFNAIKET ILSEWVIEEW GECSKSCGSG
     WQRRSVKCRD LNGQSATDCA KELKPNDLRP CADMPCPQWQ LGDWSPCSKT CGKGFKKRLL
     KCMSYDGSML PQESCDPSKK PKHLIDFCNV TKCT
//
DBGET integrated database retrieval system