ID A7SM43_NEMVE Unreviewed; 1136 AA.
AC A7SM43;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN ORFNames=NEMVEDRAFT_v1g246132 {ECO:0000313|EMBL:EDO35222.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO35222.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO35222.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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 EMBL; DS469705; EDO35222.1; -; Genomic_DNA.
DR RefSeq; XP_001627322.1; XM_001627272.1.
DR AlphaFoldDB; A7SM43; -.
DR EnsemblMetazoa; EDO35222; EDO35222; NEMVEDRAFT_v1g246132.
DR eggNOG; KOG3538; Eukaryota.
DR HOGENOM; CLU_279959_0_0_1; -.
DR InParanoid; A7SM43; -.
DR PhylomeDB; A7SM43; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 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; 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; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF13688; Reprolysin_5; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001593};
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}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1136
FT /note="Peptidase M12B domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002712160"
FT DOMAIN 234..462
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 204
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 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 405
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 411
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 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 379..457
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 418..441
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..570
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 536..575
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 547..559
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1136 AA; 125807 MW; 1C423EC099674BB8 CRC64;
MTPKLAMVFA LTLGLIGLVR GDLKLHHHMS TRELRRYFGV DTHDQVPDYE VASPFQVDHK
GDFLTYKLHH PSPHRHKRSA AEPHLQFVNI RALGLNLNMK LTPASGPSHA RLVMETHHEN
GTTTYSDPPQ AQYYQGHVVS KPGSMVALSN SGGITGMISL LDQLLYIHPL STHLAKYHGK
RGGGQPHVVV RHPVNAGKVY KRSCHVTSES RSRRGIRDLR NRRSVNNVTK PGRKTLEVAM
VADQYVIKTH GEGKIADFML MLAHVVNRMF QDESAGDTRI QLVVTKLVIS KQGGVGIDNP
TCTNQGVSMD NPTCTKQGVG MDNNLSYNAT DDLHTKIKIS SNWGILNIPL DPGQRGHADV
LVLVTAGTRG GLAQAASTCT TQFGRTVNSY VGLGTALLIT HEIGHTLGVR HDGGREECPD
ESFLMSTAVP GGKRAQSWSP CSRRDLQEFL SGSTSSCLDD FPGEETIVHA PARFHHKLPG
QVYDAATQCR MQYGPGYYHC KQLQWCISGE CVDDGSPMIN GGWSEWGNYS DCSHSCGGGV
QWRSRTCTNP APEAGGDNCE GSSRGHWRIC NTQACPEGSR SSRQQQCDDH DPGFQAYWHS
DPCRLGCRVG SSLILHGRVI DGTRCSSDDL NKDVCIEGKC RSVGCDSVLL SGTERDRCGV
CGGNSSSCDI IRGEYVKDWR GYGPWNPDKI VLIPKGASNV FVELREKTIH LLGVQNSKGQ
YVYNVGYTWS TVVPAAGTKV AYDHEDWLYK DKVKVKGPTK EPLWIMFVSD GSKNPGVDYS
FYSPSPSKVT ADDVEWTEGS WSTCTEPCAT GYQSRTVECR RTDDKTWVSD DVCKLKSGKP
DTERKCNEQP CASEWHETGW RPCSKTCGKG SQQRHVVCRR KVAIATYETR PDEECKEDDK
PQLSQLMRPC NELDCPAEWV PSSWSECSAT CGPDGVTVRT LSCKRLNQNG VYEPVHKIQC
KHAVQPSTQE ACNQDVNCPM ALIAANGKKF VPIGCYRDYS GYHAIPRMVA NLRNKIDWYE
IKKTVENCAE KVQKKNSTYT VFGIQVEYKL GLYLRVMRSQ LKRLRGFADR SVLTSELINT
LKSNNLFRFR GKKAGKRSKS SEISLSSESS CFAQYANVTS ETGRNAPRLA DRVQSL
//
