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Database: UniProt
Entry: A0A182H0M1_AEDAL
LinkDB: A0A182H0M1_AEDAL
Original site: A0A182H0M1_AEDAL 
ID   A0A182H0M1_AEDAL        Unreviewed;       531 AA.
AC   A0A182H0M1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=SRCR domain-containing protein {ECO:0000259|PROSITE:PS50287};
GN   ORFNames=RP20_CCG019315 {ECO:0000313|EMBL:KXJ71944.1};
OS   Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF019315-PA.1, ECO:0000313|Proteomes:UP000069940};
RN   [1] {ECO:0000313|EMBL:KXJ71944.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ71944.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ71944.1};
RX   PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA   Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA   Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA   Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA   Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA   Yan G., Tu Z.J., Fang X., James A.A.;
RT   "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT   insights into its biology, genetics, and evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN   [2] {ECO:0000313|EMBL:KXJ71944.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Foshan {ECO:0000313|EMBL:KXJ71944.1};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KXJ71944.1};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:AALF019315-PA.1}
RP   IDENTIFICATION.
RC   STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF019315-PA.1};
RG   EnsemblMetazoa;
RL   Submitted (AUG-2022) to UniProtKB.
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; JXUM01101570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JXUM01101571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JXUM01101572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JXUM01101573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KQ564658; KXJ71944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182H0M1; -.
DR   STRING; 7160.A0A182H0M1; -.
DR   EnsemblMetazoa; AALF019315-RA; AALF019315-PA; AALF019315.
DR   VEuPathDB; VectorBase:AALC636_001073; -.
DR   VEuPathDB; VectorBase:AALF019315; -.
DR   VEuPathDB; VectorBase:AALFPA_056156; -.
DR   Proteomes; UP000069940; Unplaced.
DR   Proteomes; UP000249989; 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; PS00420; SRCR_1; 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:UP000249989};
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          81..181
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          212..319
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DISULFID        106..170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        119..180
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        150..160
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        285..295
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ   SEQUENCE   531 AA;  59559 MW;  B53220AF1E936394 CRC64;
     MSEVSQLEFL EEEWLEEPQG LLEECQLEYP KLLGVTLVVA IAFLVSVSHA LQGSALEEAR
     LHRENLVKKY LKKLKKEDGA IKLVGGRGDF EGNVEIFHDG KWGSVCDDEW DSTEAEVVCR
     QLGFPGHIKA THSGFFGKAK RKFWMDNLFC GGKETELANC HFDGWGHSDC EASESAGVIC
     KNDDEGGVST TPKPIPEKIK PKKVQLMKDL EVRLAGGRIP NEGRVEVRFA GSGTAWGTIC
     ADGWSLLEGN VVCRQLGLGY ANDAIQTDYF GGSNRSEILL SGTECYGNET SLGNCLHHEV
     GWHSSCSERG THVAAVTCVD VMADLVFDHV EMEQSLHLED RLMYLLQCAM EENCVASQAY
     EIQRDNPNWH LETRRLMKFT ARVLNTGTAD FRPHIPKHLW EWHLCHMHYH SMEVFATFDI
     YNGQGVKVAE GHKASFCLED NQCLPGTEPK YACANYGDQG ISVNCADIYR HNIDCQWVDI
     SELDFGLYTL RVAINPEFKV PEMSYDNNAA ICSLLYTETY ARAYDCKITR P
//
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