ID A0A084W3F5_ANOSI Unreviewed; 541 AA.
AC A0A084W3F5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Hydroxysteroid dehydrogenase-like protein 2 {ECO:0000256|ARBA:ARBA00040243};
GN ORFNames=ZHAS_00012649 {ECO:0000313|EMBL:KFB44749.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB44749.1};
RN [1] {ECO:0000313|EMBL:KFB44749.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC012649-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: Has apparently no steroid dehydrogenase activity.
CC {ECO:0000256|ARBA:ARBA00037788}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; ATLV01019967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ATLV01019968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525286; KFB44749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084W3F5; -.
DR STRING; 74873.A0A084W3F5; -.
DR EnsemblMetazoa; ASIC012649-RA; ASIC012649-PA; ASIC012649.
DR VEuPathDB; VectorBase:ASIC012649; -.
DR VEuPathDB; VectorBase:ASIS002479; -.
DR VEuPathDB; VectorBase:ASIS006970; -.
DR Proteomes; UP000030765; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd09762; HSDL2_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42808; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR42808:SF3; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT DOMAIN 165..255
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 541 AA; 58787 MW; 1009E0FC2FF3B7C6 CRC64;
MAPHWFSNHV AYTMAKYGMS MCVLGMAKEF ESANIAVNAL WPRTAIFTAA MEMLTGKESD
QFSRKPEIMA DAAYAILSKE PKQQSGKFLI DDEVLTAEGI TDLKQYACVP ENADKLMPDF
FLDVAPEKLV EFAAEGSHAA SLKKPQADAA GGKIEGLFKK IESMLSEEIV RKTGAVYEFK
VKGEEAGTWF ADLKNGTGKV GKGNPPSTAD AVLTMDSKHF FDMFTGKLKP ANAFMTGKLK
ISGDLQKAMK LEKLMGGLKA KLKLAGLTLF ITGASRGIGK AIALKAARDG ANIVLAAKTA
EPHPKLPGTI YTAAAEIEAA GGKALPCIVD VRSEEAVRAA VKKAVATFGG IDILINNASA
ISLTPTEETD MKRYDLMHNI NTRGTFLVSK ECLPYLRRSR HAHILNISPP LNMEPHWFSN
HVAYTMAKYG MSMCVLGMAR EYESANISVN ALWPRTIVFT AAVEMLHGKE GYSYARKPEI
MADAAYAILS RPPGVSTGRF FIDDEVLAEE GVKDFEQYAC VPGNALILTP DIFVNEKKAK
L
//
