ID A0A060S8N4_PYCCI Unreviewed; 2227 AA.
AC A0A060S8N4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=P-type phospholipid transporter {ECO:0000256|ARBA:ARBA00012189};
DE EC=7.6.2.1 {ECO:0000256|ARBA:ARBA00012189};
GN ORFNames=BN946_scf184382.g6 {ECO:0000313|EMBL:CDO68649.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO68649.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO68649.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO68649.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO68649.1}.
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DR EMBL; CCBP010000022; CDO68649.1; -; Genomic_DNA.
DR STRING; 5643.A0A060S8N4; -.
DR HOGENOM; CLU_230934_0_0_1; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF08518; GIT_SHD; 2.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SMART; SM00555; GIT; 2.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1340..1362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1972..1994
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2015..2039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2051..2068
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2080..2103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2123..2142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..103
FT /note="GIT Spa2 homology (SHD)"
FT /evidence="ECO:0000259|SMART:SM00555"
FT DOMAIN 123..153
FT /note="GIT Spa2 homology (SHD)"
FT /evidence="ECO:0000259|SMART:SM00555"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 423..593
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2227 AA; 247772 MW; F176497A6F244202 CRC64;
MRRNGSTRAT SPTNTTYSGI SNYRTDSYRP LPTGEKSQPA ADPRSIARVH FEELSRYLAS
YLAKEPANSR SSARQKLTRL TRQQFQELST DVYDELMRRK NNTDNEVPFL PVRDDFHPKR
NQARQKLATL PTGRFKDLSS DVYYELSRRY PEFKEESPEA VPEKSPGSAY DDYPSPDFPR
NGRASEDRGN DSGYGESASG AGRRPSEDNE RRSADAYGGT NSSRRKPSQD MYGGDRRRPS
QDTTSGLGRR PSESVSINSE STSASNAQSA TAGMAMIIPN KSTIAEEDIE VPYGRDARDS
ASTAMDRDRG RDRSVDRGGG GGGASDSERD GDFSPRSPPV GGLGGLNGLS ARFQGADGDE
DDEGAGGARS GDDYYDRMSY GRQSAASDRS TGAASIGARM LGGRASVTGE EQERMRREYE
FKIATMQTRI TGLERDLENV QERGRKWTED EKRVRAMEEE LAELRRRLEE KSNSMLSLQQ
ELETLREERA REKDIAARRQ RQNEEEIESL RERCERLEAS GDGSSVDSEI LDQLRSDMEG
LLSELSDLSR RNDELMAAKE NDLATIRDLD AQLKDYKRKY EQAKTELRSV KATSQLFLPP
PKVDDRLPVA RDGGLVDIHV TAFVSSIDSL LTAGRSNAPT RVLQPMKDVV NAVTAIIEDV
RAFERRPQRE RDRAEVDPEA LQNLRERLDA TLSNLVAAAK THATSAEIGK TIHVRKATKA
EQEQFAPPMA AGQGSSSSAT NGYAPSLRSV DELRSAHQRS GSSTSSRNGE DKFSPVSPPR
AGSAGRQSLE GRRPSSNMSS SNANSPPPAF DRTIPNSANN KGDSPAAGKN PEDAWAELKP
YLEAQTESIV YAIQSVLSGV RSPTPSPTLN ENLTQIITIV SSIVAVCKDS FPPGAQQQGE
EILRELGEHA NKLSEVQAQA EVTKEARQVM AKSSFAVANA MKGLMKLQYQ PANTGYPPSS
SPPQALDPFF DDDDDDVPDS AFGRNPAMQS KESGLPLARS GAPPAGFGSS QHSLPNTIQP
DQWSLEDEQP GSKPFAGSAS FSGPSKTHQR KPSSSFKKRW KWPWDKKETV LSGNRVIALN
NPDANADFCN NYVSTSKYNV ATFVPKFLLE QFSKYANLFF LFTALIQQIP DVSPTNRYTT
IAPLSVVLLA SAFKETQEDL KRHQSDSELN SRKAKVLTPE GTFVEKKWKD IAVGDVLRLE
SDEFIPADVI LLSSSEPEGF CYIETSNLDG ETNLKIKQAS PQTSNLTSPN LVTSLHGTLR
SEHPNNSLYT YEGTLELISS GGVPKQIPLG PDQLLLRGAQ IRNTPWAYGL VVFTGHETKL
MRNATAAPIK RTAVERQVNV HIVFLFIFLL ALSIGSTIGS SIRSWFFSSQ QWYLLEQATI
TGRAKEFIED ILTFIILYNN LIPISLIVTM EVVKYQQAQL INSDLDMYYA KTDTPALCRT
SSLVEELGQI EYVFSDKTGT LTRNEMEFRF CSIGGVAYAD VVDESHRGDG DDDKEAWRSF
DDLRALASGA QNPFVDVPGD AGAGDEREVA NEFLTLLAVC HTVIPEVRDG KMRYQASSPD
EAALVAGAEL LGYQFHTRKP KSVFVNVHGQ SLEYEILNVC EFNSTRKRMS TVVRCPDGKI
KLFCKGADTV ILERLSENQP FTEKTLLHLE EYATDGLRTL CIASRDIPEA EYRQWSAIYD
QAAATINGRG EALDKAAELI ERDMFLLGAT AIEDKLQEGV PDTIHTLQMA GIKVSYAWFN
QHRVMMTNDI TQVWVLTGDR QETAINIGMA CRLISESMNL VIVNEETAHE TEEFLTKRLN
AIKSQRNAGD QEDLALVIDG KSLTFALEKE ISKTFLELAI LCKAVICCRV SPLQKALVVK
LVKKNQKSIL LAIGDGANDV SMIQAAHVGV GISGVEGLQA ARAADVAISQ FRFLKKLLLV
HGAWSYTRLS KMLLYSFYKN IVLYMTQFWY SFFNNFSGQI AYESWTLSLY NVVFTVLPPL
VIGVFDQFVS ARILDRYPQL YMLGQRNAFF TRTQFWAWVA NALYHSIILF GFSVILFWGD
LKQATGFDSG HWFWGTTLYL AVLLTVLGKA ALISDLWTKY TVAAIPGSFV FTMLFLPLYA
VVAPAIGFST EYRGIVPRLW TDAVFYFVLL LVPIVCLTRD FVWKYYRRTY MPETYHIAQE
IQKYNIPDYR PRQEQFQKAI KKVRAVQRMR RNRGFAFSQT ENAARQDQAR LIRAYDTSKT
GARPTGY
//
