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Database: UniProt
Entry: A0A182XV12_ANOST
LinkDB: A0A182XV12_ANOST
Original site: A0A182XV12_ANOST 
ID   A0A182XV12_ANOST        Unreviewed;      1876 AA.
AC   A0A182XV12;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 37.
DE   RecName: Full=uS12 prolyl 3-hydroxylase {ECO:0000256|ARBA:ARBA00029938};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI00048-PA, ECO:0000313|Proteomes:UP000076408};
RN   [1] {ECO:0000313|Proteomes:UP000076408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX   PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA   Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA   Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA   Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA   George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA   Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA   Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA   Sharakhov I.V., Tu Z.;
RT   "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT   stephensi.";
RL   Genome Biol. 15:459-459(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASTEI00048-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI00048-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC         [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC         Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC         Evidence={ECO:0000256|ARBA:ARBA00001792};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGS family.
CC       {ECO:0000256|ARBA:ARBA00005316}.
CC   -!- SIMILARITY: Belongs to the TPA1 family.
CC       {ECO:0000256|ARBA:ARBA00007443}.
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DR   STRING; 30069.A0A182XV12; -.
DR   EnsemblMetazoa; ASTEI00048-RA; ASTEI00048-PA; ASTEI00048.
DR   VEuPathDB; VectorBase:ASTE007159; -.
DR   VEuPathDB; VectorBase:ASTEI00048; -.
DR   VEuPathDB; VectorBase:ASTEI20_032120; -.
DR   VEuPathDB; VectorBase:ASTEI20_038540; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IEA:UniProt.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 2.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR045363; CERK_C.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR019540; PtdIno-glycan_biosynth_class_S.
DR   InterPro; IPR039558; TPA1/OFD1_N.
DR   PANTHER; PTHR21072; GPI TRANSAMIDASE COMPONENT PIG-S; 1.
DR   PANTHER; PTHR21072:SF13; GPI TRANSAMIDASE COMPONENT PIG-S; 1.
DR   Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR   Pfam; PF19280; CERK_C; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF10637; Ofd1_CTDD; 1.
DR   Pfam; PF10510; PIG-S; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   1876 AA;  209795 MW;  A92C52E4111D4D78 CRC64;
     MKPTDKRRAH GDDADDGGGT AEQSDRSGST AREDGKALLR ILTRFHIFHI ALNNPRASLH
     ASENAPTPPA AKRTKRGTIV DDSNTELVSI NGCFFDDDFR ERFKVAWQRK ESIAGNNYQL
     KQDPFQLAVF QHFLQEDVNR ADATKRLEAE FSTVDWKRKQ MDLYEFYQTN DLCSLERDYL
     QAFYTVLKEQ MMPLVEELTG IKLTHVSASC SMYNAGDYLL VHDDLLSDRR IAYVFYLSPW
     DCHREWCEKD GGALELFKAD GNQLPVFPVT DKIYPQNNQL VLFRVCEKSF HQVGEVTTFD
     YPRLTINGWF HGPTAPAAQC AGKTSSNSVP QPPAIIVDTH YLSPRKVDID LAGWINDVYL
     EDEVKQNVQK KVEMFSEVSL EQFLLLPRFS VLLETLCNVP NLEWKIKGPA HLRKYEVLNF
     KTLPTDASPL GELYDLFTSR TMFRLLYDYT ELDLYGRKAK APKCAIELQR WERGCYTVLG
     DSSTYADSTL DLTFYLNAQE NVGVITYLVP EADQQQQQQQ QGSSGHDQPS SSSSAAYAEC
     YDEDPVLLTL LPKDNVLNVV YRAEGTTKFT KYVSHNTHLE RANASSTGHA YTYILVCTAA
     IHIYATLAFI VIIIVIGVPM WWKTTEVYRV SLPYSEIRAL NEEPIRAAFR LGLYCPSAER
     REILAFELRK KFEQNFVFEL DLELLSLDAA TVASIKTPAR LEAELLHRYP TSAGQFLFIE
     WHKLDDDILV TSDRTAFISE SASSLKAYQV LSSWILQEYK LKAILGSRDA QQTLRGRQLR
     LNSAPLQGQY EVLITVLNPR PDLQKVHWNA RAAAETYIEP FLNELSGITN FTIKTQWIYQ
     VGIVEGASTQ PKQVPDDTKL GRHYALAEDS LPHIITSLEK KLGTQITDHP CIHLVVYVPP
     CAQAPLKIYR RDGQRAPPAS GGSVEAFTSA KWGGIVFANP AEATCVRYME SEQFSDVYLH
     AQDVMPVLLY QLRKIFDLEN NTPLLGGTLV PYSTIEPRLW EVDTFVRTNT IYLVHSATTT
     LQSLIQLLGG IEYIVINDEV GAAIQNAYQK IVEAKQQLAA GSLQRAALLA REAYASAERA
     FFDPSMLALL YFPNEQKYAI YIPLFLPIMI PVVFSFNTII KYFRGKSGPA SAKTKHDFIS
     SLLFSGKAIP QQCRANLEQN PSAVQRATNG TARSPQSSSK VSSSVSEAAC HTLCATGSEQ
     HQRLAVHRQI IQALCKLPER SKQGFPPSWW PSSCVAFFVR VSAMDKEQEV LLNAFVIAKK
     RYRVFYNAGI LVWEDESSKK AKTTVPITDV LSVAVSKHPH ANGKQWMGKR SSKAPPPPSP
     TAPPIARNDA HGSLDSDRIP VLSGSTTTNT LATNASNNIP HHHSNRGSLN ELSDSHDDRR
     DTSDYFDGGI QAGNFNYLIL HYAALVCAKT SRWRVKSVAL HNSEQRIVEL WYNRLSSDLR
     DQNRPKNLLL FLNPYGGKKN ALALYERFAK PLFRLAQVDI NLIITQRAQQ IYDIVTSKSI
     VLDNYDGLVC CGGDGTFAEL FNGLVTRTMM DCGIDVKHPP FLPKPNIPIG IIPAGSTDTV
     ACCLNGTTDI KTSIIHIILG QHSGLDISAV YGADAVAQDD DGSPSLGGKP RRPELLKLFA
     SALSYGYLGD IAYDSEKYRW MGPKRYDYSG FKKFLANRGY SAEIVVHLDR RGKQDPNDGV
     RCLDQCSRCK KALCSSQVGS EAGAEPDDTE PLVVRGKFLM VSGANISCSC ERSPQGFSPF
     CHLGDGLLDL VLVRHTSMLN NLRLLLTMTS KTKKLSELPF VEVYRTKEFR FTANGQQQQQ
     GDTNGGEVAP ALSSEMLKRR SKWNCDGEVL LDTNIIVESN CQLIRVFRRG ILPSGGHGGN
     TLDTDDKDAC CFGLCN
//
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