ID A0A452HEE8_9SAUR Unreviewed; 977 AA.
AC A0A452HEE8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-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:ENSGAGP00000013193.1, 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:ENSGAGP00000013193.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 STRING; 38772.ENSGAGP00000013193; -.
DR Ensembl; ENSGAGT00000015103.1; ENSGAGP00000013193.1; ENSGAGG00000010106.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing 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: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; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013277; Pept_M12B_ADAM-TS8.
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:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 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; PR01861; ADAMTS8.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; 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|PROSITE-ProRule:PRU00276};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..977
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019311794"
FT DOMAIN 183..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 977 AA; 107980 MW; A69E20D0239316AB CRC64;
MPLSRREPPL PGRLAPAFPT LLLLLGTARA LPRQPGDFQE VVPVRIPDPR GGEQVSFCLS
AFSRDFVLQL APDASFLAPR LKIQRLGRPG QRAEEDDAEL RKCFYSGTVN SQPGSLAAVS
LCRGIRGSFL VDGDEYLLQP AALGGGDPLL QPHRLQRRRA PEPGSDLPVG TSRRARRFVS
EARFVETLLV ADASMVQFYG EELKNHILTL MSVAARIYQH PSLKNSVSLV VVKVLVVEDE
KAGPEVSDNG GLTLRNFCNW QQSFNPASDR HPEHYDTAVL LTRQDFCGHQ SCDTLGVADI
GTMCDPNKSC SVIEDEGLQA AYTLAHELGH VLSMPHDDSK TCERLFGPLG KHHMMAPFFV
HLNKTLPWSP CSAMYLTEFL DGGHGDCLLD APAEPIVLPT DLPGQLAMYD LDRQCQQIFG
KEFRHCPNTT DEDICAQLWC RIDTREPLCH TKNGSLPWAD GTPCGVGRLC WDSSCVAQDA
RKPQPVVDGN WGPWSPWGAC SRTCGGGVHF SYRDCNDPAP QNGGKYCEGQ RAKYQSCCTE
ECPPDGKSFR EQQCAKYNSY NFTDLDGNLL EWLPKYSGVS PRDRCKLFCR ARGRSEFKVF
EAKVRHLPLI IIVLAWNITG VTELSHYCLL LLAQVIDGTL CGPETLSICV HGQCIKAGCD
HVVGSSKKLD KCGVCGGNGS TCRKISGSLN RSKYGYNDIV TIPAGATNID IKQRSHRGVR
HDGNYLALRT LDGKYLLNGD FAISAMEQDL LVKGTILKYS GSLTTLERLQ SFQQLPESLT
VQLLTVSSEV FPPKVKYTFF LPKXTTLERL QSFQQLPESL TVQLLTVSSE VFPPKVKYTF
FLPKDIPFSK QKVKEKKSAN IIQPMLTSQW VMGDWSECSK TCGSGWQRRT VECRDVEDQA
STTCDKALKP EDIKPCSDLP CPIWRLGPWS PCSRTCGEGV RTRSTACIDY AGKIIAPEKC
SLPLLLAATT TCVLQEC
//
