ID G3JCR1_CORMM Unreviewed; 577 AA.
AC G3JCR1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Protein ARV {ECO:0000256|RuleBase:RU368065};
GN ORFNames=CCM_02940 {ECO:0000313|EMBL:EGX94669.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94669.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX94669.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX94669.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC -!- FUNCTION: Mediator of sterol homeostasis involved in sterol uptake,
CC trafficking and distribution into membranes.
CC {ECO:0000256|RuleBase:RU368065}.
CC -!- FUNCTION: Regulates also the sphingolipid metabolism.
CC {ECO:0000256|RuleBase:RU368065}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368065}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368065}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU368065}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU368065}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ARV1 family. {ECO:0000256|ARBA:ARBA00009187,
CC ECO:0000256|RuleBase:RU368065}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. NP60 subfamily.
CC {ECO:0000256|ARBA:ARBA00007598}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368065}.
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DR EMBL; JH126400; EGX94669.1; -; Genomic_DNA.
DR RefSeq; XP_006668155.1; XM_006668092.1.
DR AlphaFoldDB; G3JCR1; -.
DR STRING; 983644.G3JCR1; -.
DR GeneID; 18164967; -.
DR KEGG; cmt:CCM_02940; -.
DR VEuPathDB; FungiDB:CCM_02940; -.
DR eggNOG; KOG0409; Eukaryota.
DR eggNOG; KOG3134; Eukaryota.
DR HOGENOM; CLU_472520_0_0_1; -.
DR InParanoid; G3JCR1; -.
DR OrthoDB; 2715114at2759; -.
DR Proteomes; UP000001610; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0032366; P:intracellular sterol transport; IEA:UniProtKB-UniRule.
DR GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IEA:UniProtKB-UniRule.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016125; P:sterol metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR007290; Arv1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43580:SF3; 6-PHOSPHOGLUCONATE DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_2G11600); 1.
DR PANTHER; PTHR43580; OXIDOREDUCTASE GLYR1-RELATED; 1.
DR Pfam; PF04161; Arv1; 2.
DR Pfam; PF03446; NAD_binding_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368065};
KW Golgi apparatus {ECO:0000256|RuleBase:RU368065};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU368065};
KW Lipid transport {ECO:0000256|RuleBase:RU368065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368065};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW Sphingolipid metabolism {ECO:0000256|RuleBase:RU368065};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368065};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368065};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368065}.
FT TRANSMEM 112..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368065"
FT DOMAIN 277..431
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
SQ SEQUENCE 577 AA; 61832 MW; 5C0643ECF3463334 CRC64;
MPICIECRHP VKTLWTQYSG AGDKASGHNI RLTVCRKCGR FCDKYVEHDF VVLFIDLVLI
KPQPSIVRLG ILLLLFDVYL TWARIENQGL PGETPGERNE SSLGQLAQQP IVIQYFFFLM
LCTLSTLAFH AVIRFLVASS LSPLVALGVL PRYRRPNSVS TALLVSSSTK LFPILLVIWD
YDVPAAATSL GWAVVANNVE ALRILLDCRY YVACLLALIG AATRWSVARL VLVAVGLNGT
DSMSVDASMA TDAKALWGAV TLHQAKSRST MAPTLLWIGL GNMGRAMCKN IVDKGNLDAP
LLIYNRSKQR AVDLSQKLPG GKTEVVESLV DAVAKVDIIF TCVANDEAVS EVIAAALQAD
IKGKLFIECS TIHPDATQAT ADKLLAQGAE FVAAPVFGAP AAAEAGQLIA VLAGPSASVD
RARPWFKGVT ARAEIDLTGA PYGKATTLKV IGNTFVLNMV EQLAEAHVLA ETSGLGTQPI
HALVEALFPG PYAAYSTRML SGDYHTRAEP LWAVDLARKD ARHAKALAAA AGTRVQNVET
ADAHLASLRE HAGPSGDIAA IYGVVRKKAG LNFKNDV
//
