ID T1F1D8_HELRO Unreviewed; 773 AA.
AC T1F1D8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Agrin {ECO:0008006|Google:ProtNLM};
GN Name=20202638 {ECO:0000313|EnsemblMetazoa:HelroP169093};
GN ORFNames=HELRODRAFT_169093 {ECO:0000313|EMBL:ESO09149.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP169093, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO09149.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP169093}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2};
CC -!- PTM: Glycosylated. {ECO:0000256|PIRSR:PIRSR602640-4}.
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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; AMQM01003172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB096023; ESO09149.1; -; Genomic_DNA.
DR RefSeq; XP_009013171.1; XM_009014923.1.
DR AlphaFoldDB; T1F1D8; -.
DR STRING; 6412.T1F1D8; -.
DR EnsemblMetazoa; HelroT169093; HelroP169093; HelroG169093.
DR GeneID; 20202638; -.
DR KEGG; hro:HELRODRAFT_169093; -.
DR CTD; 20202638; -.
DR eggNOG; KOG3649; Eukaryota.
DR HOGENOM; CLU_361808_0_0_1; -.
DR InParanoid; T1F1D8; -.
DR OrthoDB; 2874974at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00104; KAZAL_FS; 4.
DR Gene3D; 3.30.60.30; -; 4.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR11799; PARAOXONASE; 1.
DR PANTHER; PTHR11799:SF12; PARAOXONASE-RELATED; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR Pfam; PF07648; Kazal_2; 4.
DR Pfam; PF00053; Laminin_EGF; 1.
DR PRINTS; PR01785; PARAOXONASE.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00280; KAZAL; 4.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 4.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS51465; KAZAL_2; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602640-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101}.
FT DOMAIN 381..431
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 447..501
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 529..576
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 613..660
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 721..773
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 8
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT DISULFID 721..733
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 723..740
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 742..751
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 773 AA; 86519 MW; 82FFE3240CCDFF1F CRC64;
MKEFGSEDIK LLPGGKAFVS SGFKLSNDGR KNSVGGIYLF DFNKPSEKPL NLLMVDERGQ
QLPITPHGLS FWTDAASGVT YLYVVNHHNG VESIEKFRYH PEEKKLVRVK QFKDETFHVL
NSIHLVGEDQ FYFTNYLFFN AYFELFFGLE WGSVGYFNGE HGELVVKGLN IPNGVIMWKN
HLVVALSGSD ELNVYSVAKD HQLNLERTIP VKTSVDNLSV HPEHDDLILG CHPSPFKFPF
HSRNPDAYLS PSQVLRVNDK SEVTEIYSND GSELSASTVA VLYKDAMLIG SAYTKLLYCQ
DKTLPQYNVT QLYTTQCDTK SYNTAYHHTT SSQHYTTLHH TYTRWNGKSS DIRDPCLGRN
CSFGAKCVAS LDGMSARCQC REVCYNYGDS EGSTPICGSD GVDYANTCEM ERTACRDMKD
VKKKFDGKCD PCREIKCPIS QVCKLDSKRQ PVCRCFNPCP NNYSPVCANN GKTYVNKCFM
DLDACKLSKN LVVISKENCS YENSLCDKKK ECDYYADCYN TPKGLTKCIC PEWCDKIVKP
VCGSDGLTYD NICEMKRRSC LSKHWIRLVE YGMCSKDSEN NYRDLGLLTN YCEQFGCQPG
AECVVGEDGV ECFCANCSSH VTDEVCGTDG RSYRNVCEMK KYSCVNKKTV HVGHAGPCGQ
NLNCKQSKFG CCSDDGRFES QGPNEEGCPN VKIGKYKVKY EPKWNGLASI QLDIFLFHEQ
CQCNTFGSVG AQCGAATHAC SCKPGVGGIR CDRCVPTYWG FSGILDAQDG CLR
//
