ID A0A1V6PGL7_PENDC Unreviewed; 1917 AA.
AC A0A1V6PGL7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Polycystin cation channel PKD1/PKD2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENDEC_c005G04946 {ECO:0000313|EMBL:OQD76144.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD76144.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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:OQD76144.1}.
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DR EMBL; MDYL01000005; OQD76144.1; -; Genomic_DNA.
DR STRING; 69771.A0A1V6PGL7; -.
DR OMA; QKTKYVW; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07543; P-type_ATPase_cation; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
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.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522};
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}.
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 651..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..701
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1038..1057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1577..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1917 AA; 215897 MW; EBC554D2D79387C9 CRC64;
MGRWGVILGF DRRRANHRFH VERRGLLPAY AADEPQISES SKEIAKVALR LKYQIEQLVS
CEVAESFLTD PNSRIITEEV IKTAKNAGGE DYEACVVYCL LTCLRWFKIQ ASLELWDADL
HECRAIACEV VAKRIIEGEQ NQNYLLKNIL LKRYSIFLEG EETDPANVFE RSVDLHALRI
ISSSGYQKCI SYLWQGWICQ EEGNPTNFVE YADKSNTDYW AHFHPDRMRT PLYQNVCQIV
FSLIYLILYT AVINSVNPTG DLDVTECILY IMTFAFICDE TVKFWKVGWN YLEFWNAFNS
TLYALLAISF VMRVVALAHS PSSGDEKRLM FNELSYNFLA FAGPMFWMRM MLYLDSFRFF
GAMFVVLRVM MKESLIFFAL LFVVLAGFFQ AFIGMAQVDG DVDITRPIIQ GMANSVMQSP
EFETFQDFAF PFGIILYYVF NFVVMIVLLN ILIALYNSAY EDISGNAIDE YMAIFAQKTM
QFVRAPDENV FIPPFNLIEI LGLVAPFEWW LSREYYAKLN DIVMGVIYSP LLVITAWIET
RQAEHIQRNR SHGEEDENHT QEWEHMAEEV DFDLEDNWKE EVKQSTPDIK ADTCTVEVRQ
LKEQVAVLTE MCAIYWTLFV VTSAAIMAKL ADDPQIQHAS LHNPLPFQLH TYIWPFLIIW
PAFFAFYLSP ERYDTYIQGQ EWTFVFAGSI ITVQSLLWLM TKWNININTL FTTTTAKSVD
TARLIKVIPI TNAGSAEICP LIPENSGGKK TLSFLFQKRR FLFYPETRSF APLSYVLDVE
PKPPLKYFQQ SKGLTTKAEI DSIQHHYGDN TFDIPVPTFL ELFQEHAVAP FFVFQVFCVG
LWMLDEYWYY SLFTLFMLVT FESTVVWQRQ RTLNEFRGMS IKPYDVWVFR ENKWLQITSD
KLLPGDLMSV NRTKEDGGVA CDILLIEGSV IVNEAMLSGE STPLLKESVQ LRPGDDLIEP
EGLDKNSFVH GGTKVLQITH PNANGDETLK NLADGVTTPP DNGALGVVVK TGFETSQGSL
VRTMIYSTER VSANNVEALL FILFLLIFAI AASWYVWQEG VAKDRKRSKL LLDCVLIVTS
VVPPELPMEL SLAVNTSLAA LSKFAIFCTE PFRIPFAGRV DVACFDKTGT LTGEDLLVDG
IAGLTLGQTG ANVQADGAHT ELAKAATIGP ETTLVLASAH AMVKLDEGDV VGDPMEKATL
EWIGWTLGKK DTLTSRGNAP IVSSRPVESV QIKRRFQFSS ALKRQSTIAT LTTNEPKTSK
KSKATFVGVK GAPETISTML VDLPPNYEET YKHFTRNGAR VLALAYKYLS TESELSQNRV
NNYVREEIEA DLIFAGFLVL QCPLKDDAVK AVRMLNESSH RVVMITGDNP LTAVHVARQV
EIVDREVVIL DAPEHDTSGT RVVWRTIDDK LSIDVDPTKP LDPEILKTKD ICITGYALAK
FKGQQALPDL LRHTWVYARV SPKQKEDILL GLKDAGYTTL MCGDGTNDVG ALKQAHVGVA
LLNGSPDDLT KIAEHYRTTK MKELYEKQVG MMQRFNQPAP PVPVHIAHLY PPGPTNPNYQ
KAIEREAQKK GAVAKPGEEI PTITSPGAQA LQSSQGTTPQ QQRQQQAQAA AAGFADKITS
SMLEQELDES EPPTIKLGDA SVAAPFTSKL ANVIAIPNII RQGRCTLVAT IQMYKILALN
CLISAYSLSV IYLDGIKFGD GQVTISGMMM SVCFLSISRA KSVEGLSKER PQPNIFNVYI
IGSVLGQFAI HIATLIYLSN YVYSIEPRSD NVDLEGEFEP SLLNSAIYLL QLIQQISTFS
INYQGRPFRE SIRENKAMYW GLVAASGVAF SCATEFVPEL NEKLRLVPFS NEFKLTLTVL
MILDYGGCWV IENVLKNLFS DFRPKDIAVR RPDQLTREAE RKAKEEAEAA KEQQRKI
//
