ID U4UDB5_DENPD Unreviewed; 477 AA.
AC U4UDB5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=SRCR domain-containing protein {ECO:0000259|PROSITE:PS50287};
GN ORFNames=D910_08389 {ECO:0000313|EMBL:ERL91047.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL91047.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL91047.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; KB632271; ERL91047.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UDB5; -.
DR STRING; 77166.U4UDB5; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IEA:InterPro.
DR Gene3D; 3.10.250.10; SRCR-like domain; 2.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR PANTHER; PTHR45817:SF4; LYSYL OXIDASE-LIKE-RELATED; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR Pfam; PF00530; SRCR; 2.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 2.
DR SUPFAM; SSF56487; SRCR-like; 2.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
DR PROSITE; PS50287; SRCR_2; 2.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; LTQ {ECO:0000256|ARBA:ARBA00022477};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW TPQ {ECO:0000256|ARBA:ARBA00022772}.
FT DOMAIN 60..100
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 127..247
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 69..79
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 216..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 477 AA; 53204 MW; 5E9E4039AE83D60E CRC64;
MGRVDSNRNR SNVCTLEIAA IHSHDALSKN KSILIRKHLK RLKKVDGGVR LVGGRDEYEG
KFWMDDVFCD GTEEELADCR FDGWGKNDCK DSEAAGVICL DPAQTSSIPN EAKADTKRLS
IGATRKIRLR GGRVATEGRV EVQTKGGRWD VICAEGWSLR EALVVCKTLS LGKLFNVYSE
KMIQFSGDIL GYAADAIQTK FFGGKLSKTS LAGVRCFSNE TSFATCTYQV SLTGKCSEEE
VAAVSCTQSL SDLVIGQFCL NPHCSSQFYI NSADHEELTR SAYLQDQTMF FLQCAMEENC
AASSAYQIQK ENEAWHLETR RLLRFTARIL NAGTADFRPL IPKHLWEWHM CHMHYHSMEV
FATFDIFDAK GARVAEGHKA SFCLEDNQCL PGVEPKYACA NYGDQGITVN CSDIYKHTVD
CQWVDISDLD PGNYKIKIAV NPECKIAEMD YRNNAALCDF IYTPAFGTVT NCALELP
//