ID A0A194PJ99_PAPXU Unreviewed; 1902 AA.
AC A0A194PJ99;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=proton-translocating NAD(P)(+) transhydrogenase {ECO:0000256|ARBA:ARBA00012943};
DE EC=7.1.1.1 {ECO:0000256|ARBA:ARBA00012943};
GN ORFNames=RR46_10662 {ECO:0000313|EMBL:KPI93402.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI93402.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI93402.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI93402.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI93402.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+);
CC Xref=Rhea:RHEA:47992, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57945, ChEBI:CHEBI:58349; EC=7.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000006};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005624}.
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DR EMBL; KQ459602; KPI93402.1; -; Genomic_DNA.
DR STRING; 66420.A0A194PJ99; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008746; F:NAD(P)+ transhydrogenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR CDD; cd04030; C2C_KIAA1228; 1.
DR CDD; cd05304; Rubrum_tdh; 1.
DR CDD; cd21670; SMP_ESyt; 1.
DR Gene3D; 2.60.40.150; C2 domain; 4.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037752; C2C_KIAA1228.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR037749; Ext_Synaptotagmin_C2B.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR026255; NADP_transhyd_a.
DR InterPro; IPR024605; NADP_transhyd_a_C.
DR InterPro; IPR034300; PNTB-like.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR NCBIfam; TIGR00561; pntA; 1.
DR PANTHER; PTHR10160; NAD(P) TRANSHYDROGENASE; 1.
DR PANTHER; PTHR10160:SF19; PROTON-TRANSLOCATING NAD(P)(+) TRANSHYDROGENASE; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF00168; C2; 4.
DR Pfam; PF02233; PNTB; 1.
DR Pfam; PF12769; PNTB_4TM; 1.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 4.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 469..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 520..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 707..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 745..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1145..1324
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 1322..1445
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1525..1646
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1790..1902
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1687..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1902 AA; 205032 MW; 5A9BE41EC22C40BF CRC64;
MCGCVRVLSI RKPLPRSWHR RLFSSSSTPP PPQGVPYTKL TVGVPKEIWQ DERRVAVVPA
VVSKLVKKGF NVNIEENAGL LANFPNKAYE EAGAKITSLK DTYQSNIILK VRPFIENEVP
NVNDESSVIS FLYPAQNQEL IKQLAAKKVN AFAMDCIPRI SRAQAFDALS SMANVAGYRA
VIEAAAHFPR FFSGQMTAAG RVPPCRVLVV GGGVAGLAAA AQARCMGAAV RAFDTRPAVR
EQIESLGAQF ITMDMTEEGA GEGGYAKEMS DAFLQAERAL LGKEARTSDV VISTALIPGK
PAPLLILEDA VRDMAPGSVI VDLAAEMGGN IETTKKGEIA KVHGVTHIGL TDLPSRRPAH
ASTLYANNIS GFLFSVGNND HFYIDLEDEV TRGAIVLKAG ELLWPAPPPR SMATPTTATK
QTAAAKVEPP NPFNETLKDT FLYSTGLASL IGLGIASPNP AFTTMTTTLA LAGVVGYHTV
WGVVPALHSP LMSVTNAVSG ITAVGGLLLM GGGYVPETPV QWLASTAALI SFINVFGGFL
VTQRMLDMFK RPGDPPEYGY LYGIPAAALL GGYITTAMQG YPEVHQMAYL ASSLCCVGAL
AGLSSQATAR KGNYLGMIGV AGGIAATLGA MTPNAEVLAQ MIGVAGIGGL LGSVIAKKIE
ITDLPQLVAG FHSLVGMAAV LTCVATYMHD FPAMALDPTA ATLKTSLFLG TYIGGITFTG
SLVAYGKLQG SLSSAPLLLP GRHAINAGLL AGSLGCGGAL IALPDAPGLP LLSAAAVLSG
IQGLTLTAAI GGADMPVVIT VLNSYSGWAL CAEGFMLNNS LMTIVGALIG SSGAILSYIM
CKAMNRSLPN VILGGYGVTT GGSARPAGAT HTELNIDSVA DLIHRASSII ITPGYGLCVA
KAQYPIAELV EMLKEAGKKV RFAIHPVAGR MPGQLNVLLA EAGVPYDDVF EMEEINDEFP
DTDLVLVIGA NDTVNSAAED DPESPIAGMP VLKVWKANQV VVMKRSMGVG YAAVDNPIFY
NPNTAMLLGD AKKTCDALLE RANNNMAVTS KFALPVSSED NMDVLGMIYR FFKKVSIVGA
VYLVGYMQWS VAWLIGPVVL SVIRDQWRRE NEYRRNLAKA AASSSEKDVV LARLDDLPAW
VFFPDIERAE WLNRILLQVW PNVNHYARTI LKESIEPAVA ESLANYKLNG FRFERMILGT
IAPRVGGVKV YDKNLSRNEI IMDIDLFYAG DCDISFVLQR IRGGIKDLQI HGMVRVVMKP
LITKMPLVGG LQVFFLNNPS IDFNLVGAAD ILDMPGFSDI LRRCIVEQVS RIMVLPNKLP
IKLSDEIPTV DLRMPEPEGV LRIHLVQAQN LMKKDVSMLG KGKSDPYAII TVGAQQWKTK
HIDNDVNPHW DFWCEARIMQ SLGQALEIEV FDKDEGNDDD KLGSSRKSQV LQCELWDWDP
GMGIQNDDYL GRSSMLQSSA TSVTVRLFDW DRAGRDERLG RCSLDISQVV RAGRLDTWQT
LQQAKHGKVH LRLSWHRLST DLIDLSHAIT ETQLVKTGEL SSAVLSVYID SCKKLPNART
VSRPDPYLTV TVGKKTENTA VQMRTDDPVY EIGYSFLVQN PEIDLLEIKA LDQKTGSILG
QLTYSIRALL KEKDLCMLTQ PITLQKSGPE SKIILALQLK ILKEAIKEED VDTESVSDVP
VVPEPVAVSS PLPPAPQPAS SAPPSAQPAT PPPTPAVMDS TDAAQPPLTL NAELKKLEDN
LQDNASDKSI PVEHIERAVD VPQEETPSGR DSPKLVHRTS SITTSAGEAG LGRILLSLRY
SMQHQTLYVV VHKIMNIPLK DPTNVPDPYV KLYLLPGRSK DSKRKTAVLK DNCMPEYDEQ
FEWVISHAEL HSRQIEVTVA THKGFLGGSP IIGQVHSNIL IP
//
